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Volumn 18, Issue 6, 2007, Pages 716-731

The endoplasmic reticulum and the unfolded protein response

Author keywords

Apoptosis; Endoplasmic reticulum; ER; Secretory pathway; Unfolded protein response

Indexed keywords

CALCIUM; CHAPERONE; PROTEIN;

EID: 36248949141     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.semcdb.2007.09.003     Document Type: Review
Times cited : (822)

References (170)
  • 1
    • 0036853914 scopus 로고    scopus 로고
    • Orchestrating the unfolded protein response in health and disease
    • Kaufman R.J. Orchestrating the unfolded protein response in health and disease. J Clin Invest 110 (2002) 1389-1398
    • (2002) J Clin Invest , vol.110 , pp. 1389-1398
    • Kaufman, R.J.1
  • 2
    • 0035370949 scopus 로고    scopus 로고
    • Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals
    • Patil C., and Walter P. Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals. Curr Opin Cell Biol 13 (2001) 349-355
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 349-355
    • Patil, C.1    Walter, P.2
  • 3
    • 0027305620 scopus 로고
    • A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus
    • Mori K., Ma W., Gething M.J., and Sambrook J. A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus. Cell 74 (1993) 743-756
    • (1993) Cell , vol.74 , pp. 743-756
    • Mori, K.1    Ma, W.2    Gething, M.J.3    Sambrook, J.4
  • 4
    • 0036437307 scopus 로고    scopus 로고
    • Transcriptional and translational control in the mammalian unfolded protein response
    • Harding H.P., Calfon M., Urano F., Novoa I., and Ron D. Transcriptional and translational control in the mammalian unfolded protein response. Annu Rev Cell Dev Biol 18 (2002) 575-599
    • (2002) Annu Rev Cell Dev Biol , vol.18 , pp. 575-599
    • Harding, H.P.1    Calfon, M.2    Urano, F.3    Novoa, I.4    Ron, D.5
  • 5
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder M., and Kaufman R.J. The mammalian unfolded protein response. Annu Rev Biochem 74 (2005) 739-789
    • (2005) Annu Rev Biochem , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 6
    • 33645156429 scopus 로고    scopus 로고
    • From acute ER stress to physiological roles of the unfolded protein response
    • Wu J., and Kaufman R.J. From acute ER stress to physiological roles of the unfolded protein response. Cell Death Differ 13 (2006) 374-384
    • (2006) Cell Death Differ , vol.13 , pp. 374-384
    • Wu, J.1    Kaufman, R.J.2
  • 7
    • 34248997838 scopus 로고    scopus 로고
    • N-glycan structure dictates extension of protein folding or onset of disposal
    • Molinari M. N-glycan structure dictates extension of protein folding or onset of disposal. Nat Chem Biol 3 (2007) 313-320
    • (2007) Nat Chem Biol , vol.3 , pp. 313-320
    • Molinari, M.1
  • 8
    • 0030954870 scopus 로고    scopus 로고
    • The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response
    • Sidrauski C., and Walter P. The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response. Cell 90 (1997) 1031-1039
    • (1997) Cell , vol.90 , pp. 1031-1039
    • Sidrauski, C.1    Walter, P.2
  • 9
    • 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., and 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 107 (2001) 881-891
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 10
    • 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., and Ron D. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol Cell 5 (2000) 897-904
    • (2000) Mol Cell , vol.5 , pp. 897-904
    • Harding, H.P.1    Zhang, Y.2    Bertolotti, A.3    Zeng, H.4    Ron, D.5
  • 11
    • 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., et al. ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response. Mol Cell Biol 20 (2000) 6755-6767
    • (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
  • 12
    • 1542316306 scopus 로고    scopus 로고
    • Regulation of mRNA translation by protein folding in the endoplasmic reticulum
    • Kaufman R.J. Regulation of mRNA translation by protein folding in the endoplasmic reticulum. Trends Biochem Sci 29 (2004) 152-158
    • (2004) Trends Biochem Sci , vol.29 , pp. 152-158
    • Kaufman, R.J.1
  • 13
    • 0034973982 scopus 로고    scopus 로고
    • Translational control is required for the unfolded protein response and in vivo glucose homeostasis
    • Scheuner D., Song B., McEwen E., Liu C., Laybutt R., Gillespie P., et al. Translational control is required for the unfolded protein response and in vivo glucose homeostasis. Mol Cell 7 (2001) 1165-1176
    • (2001) Mol Cell , vol.7 , pp. 1165-1176
    • Scheuner, D.1    Song, B.2    McEwen, E.3    Liu, C.4    Laybutt, R.5    Gillespie, P.6
  • 14
    • 0037353039 scopus 로고    scopus 로고
    • An integrated stress response regulates amino acid metabolism and resistance to oxidative stress
    • Harding H.P., Zhang Y., Zeng H., Novoa I., Lu P.D., Calfon M., et al. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol Cell 11 (2003) 619-633
    • (2003) Mol Cell , vol.11 , pp. 619-633
    • Harding, H.P.1    Zhang, Y.2    Zeng, H.3    Novoa, I.4    Lu, P.D.5    Calfon, M.6
  • 15
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding H.P., Zhang Y., and Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397 (1999) 271-274
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 16
    • 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., et al. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol Cell 6 (2000) 1099-1108
    • (2000) Mol Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6
  • 17
    • 0036856008 scopus 로고    scopus 로고
    • Translational control in the endoplasmic reticulum stress response
    • Ron D. Translational control in the endoplasmic reticulum stress response. J Clin Invest 110 (2002) 1383-1388
    • (2002) J Clin Invest , vol.110 , pp. 1383-1388
    • Ron, D.1
  • 18
    • 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., and Hendershot L.M. Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response. J Mol Biol 318 (2002) 1351-1365
    • (2002) J Mol Biol , vol.318 , pp. 1351-1365
    • Ma, Y.1    Brewer, J.W.2    Diehl, J.A.3    Hendershot, L.M.4
  • 20
    • 0037763721 scopus 로고    scopus 로고
    • Regulatory mechanisms controlling gene expression mediated by the antioxidant response element
    • Nguyen T., Sherratt P.J., and Pickett C.B. Regulatory mechanisms controlling gene expression mediated by the antioxidant response element. Annu Rev Pharmacol Toxicol 43 (2003) 233-260
    • (2003) Annu Rev Pharmacol Toxicol , vol.43 , pp. 233-260
    • Nguyen, T.1    Sherratt, P.J.2    Pickett, C.B.3
  • 21
    • 33745807575 scopus 로고    scopus 로고
    • Nrf1 is targeted to the endoplasmic reticulum membrane by an N-terminal transmembrane domain. Inhibition of nuclear translocation and transacting function
    • Wang W., and Chan J.Y. Nrf1 is targeted to the endoplasmic reticulum membrane by an N-terminal transmembrane domain. Inhibition of nuclear translocation and transacting function. J Biol Chem 281 (2006) 19676-19687
    • (2006) J Biol Chem , vol.281 , pp. 19676-19687
    • Wang, W.1    Chan, J.Y.2
  • 22
    • 0030297537 scopus 로고    scopus 로고
    • A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response
    • Cox J.S., and Walter P. A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell 87 (1996) 391-404
    • (1996) Cell , vol.87 , pp. 391-404
    • Cox, J.S.1    Walter, P.2
  • 23
    • 0034712734 scopus 로고    scopus 로고
    • mRNA splicing-mediated C-terminal replacement of transcription factor Hac1p is required for efficient activation of the unfolded protein response
    • Mori K., Ogawa N., Kawahara T., Yanagi H., and Yura T. mRNA splicing-mediated C-terminal replacement of transcription factor Hac1p is required for efficient activation of the unfolded protein response. Proc Natl Acad Sci USA 97 (2000) 4660-4665
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 4660-4665
    • Mori, K.1    Ogawa, N.2    Kawahara, T.3    Yanagi, H.4    Yura, T.5
  • 24
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers K.J., Patil C.K., Wodicka L., Lockhart D.J., Weissman J.S., and Walter P. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101 (2000) 249-258
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5    Walter, P.6
  • 25
    • 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., and 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 12 (1998) 1812-1824
    • (1998) Genes Dev , vol.12 , pp. 1812-1824
    • Tirasophon, W.1    Welihinda, A.A.2    Kaufman, R.J.3
  • 26
    • 0032190546 scopus 로고    scopus 로고
    • Cloning of mammalian Ire1 reveals diversity in the ER stress responses
    • Wang X.Z., Harding H.P., Zhang Y., Jolicoeur E.M., Kuroda M., and Ron D. Cloning of mammalian Ire1 reveals diversity in the ER stress responses. Embo J 17 (1998) 5708-5717
    • (1998) Embo J , vol.17 , pp. 5708-5717
    • Wang, X.Z.1    Harding, H.P.2    Zhang, Y.3    Jolicoeur, E.M.4    Kuroda, M.5    Ron, D.6
  • 27
    • 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., and Walter P. A role for presenilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response. Cell 99 (1999) 691-702
    • (1999) Cell , vol.99 , pp. 691-702
    • Niwa, M.1    Sidrauski, C.2    Kaufman, R.J.3    Walter, P.4
  • 28
    • 0032509216 scopus 로고    scopus 로고
    • Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors
    • Yoshida H., Haze K., Yanagi H., Yura T., and Mori K. Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors. J Biol Chem 273 (1998) 33741-33749
    • (1998) J Biol Chem , vol.273 , pp. 33741-33749
    • Yoshida, H.1    Haze, K.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 29
    • 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., et al. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 415 (2002) 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
  • 30
    • 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., et al. IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. Genes Dev 16 (2002) 452-466
    • (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
  • 31
    • 18244405070 scopus 로고    scopus 로고
    • Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development
    • Shen X., Ellis R.E., Lee K., Liu C.Y., Yang K., Solomon A., et al. Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development. Cell 107 (2001) 893-903
    • (2001) Cell , vol.107 , pp. 893-903
    • Shen, X.1    Ellis, R.E.2    Lee, K.3    Liu, C.Y.4    Yang, K.5    Solomon, A.6
  • 32
    • 0037320265 scopus 로고    scopus 로고
    • A time-dependent phase shift in the mammalian unfolded protein response
    • Yoshida H., Matsui T., Hosokawa N., Kaufman R.J., Nagata K., and Mori K. A time-dependent phase shift in the mammalian unfolded protein response. Dev Cell 4 (2003) 265-271
    • (2003) Dev Cell , vol.4 , pp. 265-271
    • Yoshida, H.1    Matsui, T.2    Hosokawa, N.3    Kaufman, R.J.4    Nagata, K.5    Mori, K.6
  • 33
    • 0034650851 scopus 로고    scopus 로고
    • An essential role in liver development for transcription factor XBP-1
    • Reimold A.M., Etkin A., Clauss I., Perkins A., Friend D.S., Zhang J., et al. An essential role in liver development for transcription factor XBP-1. Genes Dev 14 (2000) 152-157
    • (2000) Genes Dev , vol.14 , pp. 152-157
    • Reimold, A.M.1    Etkin, A.2    Clauss, I.3    Perkins, A.4    Friend, D.S.5    Zhang, J.6
  • 34
    • 0035094262 scopus 로고    scopus 로고
    • Increased sensitivity to dextran sodium sulfate colitis in IRE1beta-deficient mice
    • Bertolotti A., Wang X., Novoa I., Jungreis R., Schlessinger K., Cho J.H., et al. Increased sensitivity to dextran sodium sulfate colitis in IRE1beta-deficient mice. J Clin Invest 107 (2001) 585-593
    • (2001) J Clin Invest , vol.107 , pp. 585-593
    • Bertolotti, A.1    Wang, X.2    Novoa, I.3    Jungreis, R.4    Schlessinger, K.5    Cho, J.H.6
  • 35
    • 5644231992 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes
    • Ozcan U., Cao Q., Yilmaz E., Lee A.H., Iwakoshi N.N., Ozdelen E., et al. Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes. Science 306 (2004) 457-461
    • (2004) Science , vol.306 , pp. 457-461
    • Ozcan, U.1    Cao, Q.2    Yilmaz, E.3    Lee, A.H.4    Iwakoshi, N.N.5    Ozdelen, E.6
  • 37
    • 0037385313 scopus 로고    scopus 로고
    • Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-1
    • Iwakoshi N.N., Lee A.H., Vallabhajosyula P., Otipoby K.L., Rajewsky K., and Glimcher L.H. Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-1. Nat Immunol 4 (2003) 321-329
    • (2003) Nat Immunol , vol.4 , pp. 321-329
    • Iwakoshi, N.N.1    Lee, A.H.2    Vallabhajosyula, P.3    Otipoby, K.L.4    Rajewsky, K.5    Glimcher, L.H.6
  • 38
    • 14944371187 scopus 로고    scopus 로고
    • The unfolded protein response sensor IRE1alpha is required at 2 distinct steps in B cell lymphopoiesis
    • Zhang K., Wong H.N., Song B., Miller C.N., Scheuner D., and Kaufman R.J. The unfolded protein response sensor IRE1alpha is required at 2 distinct steps in B cell lymphopoiesis. J Clin Invest 115 (2005) 268-281
    • (2005) J Clin Invest , vol.115 , pp. 268-281
    • Zhang, K.1    Wong, H.N.2    Song, B.3    Miller, C.N.4    Scheuner, D.5    Kaufman, R.J.6
  • 39
    • 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., and Glimcher L.H. XBP-1 is required for biogenesis of cellular secretory machinery of exocrine glands. Embo J 24 (2005) 4368-4380
    • (2005) Embo J , vol.24 , pp. 4368-4380
    • Lee, A.H.1    Chu, G.C.2    Iwakoshi, N.N.3    Glimcher, L.H.4
  • 40
    • 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., and 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 10 (1999) 3787-3799
    • (1999) Mol Biol Cell , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 41
    • 0035141230 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced formation of transcription factor complex ERSF including NF-Y (CBF) and activating transcription factors 6alpha and 6beta that activates the mammalian unfolded protein response
    • Yoshida H., Okada T., Haze K., Yanagi H., Yura T., Negishi M., et al. Endoplasmic reticulum stress-induced formation of transcription factor complex ERSF including NF-Y (CBF) and activating transcription factors 6alpha and 6beta that activates the mammalian unfolded protein response. Mol Cell Biol 21 (2001) 1239-1248
    • (2001) Mol Cell Biol , vol.21 , pp. 1239-1248
    • Yoshida, H.1    Okada, T.2    Haze, K.3    Yanagi, H.4    Yura, T.5    Negishi, M.6
  • 42
    • 0033920261 scopus 로고    scopus 로고
    • ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1
    • Li M., Baumeister P., Roy B., Phan T., Foti D., Luo S., et al. ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1. Mol Cell Biol 20 (2000) 5096-5106
    • (2000) Mol Cell Biol , vol.20 , pp. 5096-5106
    • Li, M.1    Baumeister, P.2    Roy, B.3    Phan, T.4    Foti, D.5    Luo, S.6
  • 43
    • 0034515724 scopus 로고    scopus 로고
    • ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs
    • Ye J., Rawson R.B., Komuro R., Chen X., Dave U.P., Prywes R., et al. ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol Cell 6 (2000) 1355-1364
    • (2000) Mol Cell , vol.6 , pp. 1355-1364
    • Ye, J.1    Rawson, R.B.2    Komuro, R.3    Chen, X.4    Dave, U.P.5    Prywes, R.6
  • 44
  • 45
    • 0036713724 scopus 로고    scopus 로고
    • Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response
    • Okada T., Yoshida H., Akazawa R., Negishi M., and Mori K. Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response. Biochem J 366 (2002) 585-594
    • (2002) Biochem J , vol.366 , pp. 585-594
    • Okada, T.1    Yoshida, H.2    Akazawa, R.3    Negishi, M.4    Mori, K.5
  • 46
    • 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., et al. Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response. Cell 124 (2006) 587-599
    • (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
  • 47
  • 48
    • 33847188475 scopus 로고    scopus 로고
    • BBF2H7, a novel transmembrane bZIP transcription factor, is a new type of endoplasmic reticulum stress transducer
    • Kondo S., Saito A., Hino S., Murakami T., Ogata M., Kanemoto S., et al. BBF2H7, a novel transmembrane bZIP transcription factor, is a new type of endoplasmic reticulum stress transducer. Mol Cell Biol 27 (2007) 1716-1729
    • (2007) Mol Cell Biol , vol.27 , pp. 1716-1729
    • Kondo, S.1    Saito, A.2    Hino, S.3    Murakami, T.4    Ogata, M.5    Kanemoto, S.6
  • 49
    • 20944445990 scopus 로고    scopus 로고
    • Tisp40, a spermatid specific bZip transcription factor, functions by binding to the unfolded protein response element via the Rip pathway
    • Nagamori I., Yabuta N., Fujii T., Tanaka H., Yomogida K., Nishimune Y., et al. Tisp40, a spermatid specific bZip transcription factor, functions by binding to the unfolded protein response element via the Rip pathway. Genes Cells 10 (2005) 575-594
    • (2005) Genes Cells , vol.10 , pp. 575-594
    • Nagamori, I.1    Yabuta, N.2    Fujii, T.3    Tanaka, H.4    Yomogida, K.5    Nishimune, Y.6
  • 50
    • 33750350899 scopus 로고    scopus 로고
    • Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element
    • Liang G., Audas T.E., Li Y., Cockram G.P., Dean J.D., Martyn A.C., et al. Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element. Mol Cell Biol 26 (2006) 7999-8010
    • (2006) Mol Cell Biol , vol.26 , pp. 7999-8010
    • Liang, G.1    Audas, T.E.2    Li, Y.3    Cockram, G.P.4    Dean, J.D.5    Martyn, A.C.6
  • 51
    • 0036315042 scopus 로고    scopus 로고
    • Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis
    • Raggo C., Rapin N., Stirling J., Gobeil P., Smith-Windsor E., O'Hare P., et al. Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis. Mol Cell Biol 22 (2002) 5639-5649
    • (2002) Mol Cell Biol , vol.22 , pp. 5639-5649
    • Raggo, C.1    Rapin, N.2    Stirling, J.3    Gobeil, P.4    Smith-Windsor, E.5    O'Hare, P.6
  • 52
    • 30044441047 scopus 로고    scopus 로고
    • CREB4, a transmembrane bZip transcription factor and potential new substrate for regulation and cleavage by S1P
    • Stirling J., and O'Hare P. CREB4, a transmembrane bZip transcription factor and potential new substrate for regulation and cleavage by S1P. Mol Biol Cell 17 (2006) 413-426
    • (2006) Mol Biol Cell , vol.17 , pp. 413-426
    • Stirling, J.1    O'Hare, P.2
  • 53
    • 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., and Ron D. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat Cell Biol 2 (2000) 326-332
    • (2000) Nat Cell Biol , vol.2 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 54
    • 0031054643 scopus 로고    scopus 로고
    • Immunoglobulin binding protein (BiP) function is required to protect cells from endoplasmic reticulum stress but is not required for the secretion of selective proteins
    • Morris J.A., Dorner A.J., Edwards C.A., Hendershot L.M., and Kaufman R.J. Immunoglobulin binding protein (BiP) function is required to protect cells from endoplasmic reticulum stress but is not required for the secretion of selective proteins. J Biol Chem 272 (1997) 4327-4334
    • (1997) J Biol Chem , vol.272 , pp. 4327-4334
    • Morris, J.A.1    Dorner, A.J.2    Edwards, C.A.3    Hendershot, L.M.4    Kaufman, R.J.5
  • 55
    • 0027081774 scopus 로고
    • Analysis in vivo of GRP78-BiP/substrate interactions and their role in induction of the GRP78-BiP gene
    • Ng D.T., Watowich S.S., and Lamb R.A. Analysis in vivo of GRP78-BiP/substrate interactions and their role in induction of the GRP78-BiP gene. Mol Biol Cell 3 (1992) 143-155
    • (1992) Mol Biol Cell , vol.3 , pp. 143-155
    • Ng, D.T.1    Watowich, S.S.2    Lamb, R.A.3
  • 56
    • 0025258970 scopus 로고
    • Accumulation of the insoluble PiZ variant of human alpha 1-antitrypsin within the hepatic endoplasmic reticulum does not elevate the steady-state level of grp78/BiP
    • Graham K.S., Le A., and Sifers R.N. Accumulation of the insoluble PiZ variant of human alpha 1-antitrypsin within the hepatic endoplasmic reticulum does not elevate the steady-state level of grp78/BiP. J Biol Chem 265 (1990) 20463-20468
    • (1990) J Biol Chem , vol.265 , pp. 20463-20468
    • Graham, K.S.1    Le, A.2    Sifers, R.N.3
  • 57
    • 12844257546 scopus 로고    scopus 로고
    • Stable binding of ATF6 to BiP in the endoplasmic reticulum stress response
    • Shen J., Snapp E.L., Lippincott-Schwartz J., and Prywes R. Stable binding of ATF6 to BiP in the endoplasmic reticulum stress response. Mol Cell Biol 25 (2005) 921-932
    • (2005) Mol Cell Biol , vol.25 , pp. 921-932
    • Shen, J.1    Snapp, E.L.2    Lippincott-Schwartz, J.3    Prywes, R.4
  • 59
    • 33749233991 scopus 로고    scopus 로고
    • The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response
    • Zhou J., Liu C.Y., Back S.H., Clark R.L., Peisach D., Xu Z., et al. The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. Proc Natl Acad Sci USA 103 (2006) 14343-14348
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 14343-14348
    • Zhou, J.1    Liu, C.Y.2    Back, S.H.3    Clark, R.L.4    Peisach, D.5    Xu, Z.6
  • 60
    • 0026546365 scopus 로고
    • CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcription
    • Ron D., and Habener J.F. CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcription. Genes Dev 6 (1992) 439-453
    • (1992) Genes Dev , vol.6 , pp. 439-453
    • Ron, D.1    Habener, J.F.2
  • 61
    • 0032054744 scopus 로고    scopus 로고
    • CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum
    • Zinszner H., Kuroda M., Wang X., Batchvarova N., Lightfoot R.T., Remotti H., et al. CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum. Genes Dev 12 (1998) 982-995
    • (1998) Genes Dev , vol.12 , pp. 982-995
    • Zinszner, H.1    Kuroda, M.2    Wang, X.3    Batchvarova, N.4    Lightfoot, R.T.5    Remotti, H.6
  • 62
    • 0035947778 scopus 로고    scopus 로고
    • Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha
    • Novoa I., Zeng H., Harding H.P., and Ron D. Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha. J Cell Biol 153 (2001) 1011-1022
    • (2001) J Cell Biol , vol.153 , pp. 1011-1022
    • Novoa, I.1    Zeng, H.2    Harding, H.P.3    Ron, D.4
  • 63
    • 10644233167 scopus 로고    scopus 로고
    • CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum
    • Marciniak S.J., Yun C.Y., Oyadomari S., Novoa I., Zhang Y., Jungreis R., et al. CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. Genes Dev 18 (2004) 3066-3077
    • (2004) Genes Dev , vol.18 , pp. 3066-3077
    • Marciniak, S.J.1    Yun, C.Y.2    Oyadomari, S.3    Novoa, I.4    Zhang, Y.5    Jungreis, R.6
  • 64
    • 8544283103 scopus 로고    scopus 로고
    • CHOP is involved in endoplasmic reticulum stress-induced apoptosis by enhancing DR5 expression in human carcinoma cells
    • Yamaguchi H., and Wang H.G. CHOP is involved in endoplasmic reticulum stress-induced apoptosis by enhancing DR5 expression in human carcinoma cells. J Biol Chem 279 (2004) 45495-45502
    • (2004) J Biol Chem , vol.279 , pp. 45495-45502
    • Yamaguchi, H.1    Wang, H.G.2
  • 65
    • 17144417669 scopus 로고    scopus 로고
    • TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death
    • Ohoka N., Yoshii S., Hattori T., Onozaki K., and Hayashi H. TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death. Embo J 24 (2005) 1243-1255
    • (2005) Embo J , vol.24 , pp. 1243-1255
    • Ohoka, N.1    Yoshii, S.2    Hattori, T.3    Onozaki, K.4    Hayashi, H.5
  • 66
    • 0032940099 scopus 로고    scopus 로고
    • CHOP-dependent stress-inducible expression of a novel form of carbonic anhydrase VI
    • Sok J., Wang X.Z., Batchvarova N., Kuroda M., Harding H., and Ron D. CHOP-dependent stress-inducible expression of a novel form of carbonic anhydrase VI. Mol Cell Biol 19 (1999) 495-504
    • (1999) Mol Cell Biol , vol.19 , pp. 495-504
    • Sok, J.1    Wang, X.Z.2    Batchvarova, N.3    Kuroda, M.4    Harding, H.5    Ron, D.6
  • 67
    • 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., and Holbrook N.J. Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state. Mol Cell Biol 21 (2001) 1249-1259
    • (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
  • 68
    • 33751069967 scopus 로고    scopus 로고
    • Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins
    • Rutkowski D.T., Arnold S.M., Miller C.N., Wu J., Li J., Gunnison K.M., et al. Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins. PLoS Biol 4 (2006) e374
    • (2006) PLoS Biol , vol.4
    • Rutkowski, D.T.1    Arnold, S.M.2    Miller, C.N.3    Wu, J.4    Li, J.5    Gunnison, K.M.6
  • 69
    • 9644295726 scopus 로고    scopus 로고
    • Translocation of Bim to the endoplasmic reticulum (ER) mediates ER stress signaling for activation of caspase-12 during ER stress-induced apoptosis
    • Morishima N., Nakanishi K., Tsuchiya K., Shibata T., and Seiwa E. Translocation of Bim to the endoplasmic reticulum (ER) mediates ER stress signaling for activation of caspase-12 during ER stress-induced apoptosis. J Biol Chem 279 (2004) 50375-50381
    • (2004) J Biol Chem , vol.279 , pp. 50375-50381
    • Morishima, N.1    Nakanishi, K.2    Tsuchiya, K.3    Shibata, T.4    Seiwa, E.5
  • 71
    • 0037810844 scopus 로고    scopus 로고
    • Bax and Bak can localize to the endoplasmic reticulum to initiate apoptosis
    • Zong W.X., Li C., Hatzivassiliou G., Lindsten T., Yu Q.C., Yuan J., et al. Bax and Bak can localize to the endoplasmic reticulum to initiate apoptosis. J Cell Biol 162 (2003) 59-69
    • (2003) J Cell Biol , vol.162 , pp. 59-69
    • Zong, W.X.1    Li, C.2    Hatzivassiliou, G.3    Lindsten, T.4    Yu, Q.C.5    Yuan, J.6
  • 72
    • 0034698878 scopus 로고    scopus 로고
    • Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis
    • Nakagawa T., and Yuan J. Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J Cell Biol 150 (2000) 887-894
    • (2000) J Cell Biol , vol.150 , pp. 887-894
    • Nakagawa, T.1    Yuan, J.2
  • 73
    • 0035876483 scopus 로고    scopus 로고
    • BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak
    • Zong W.X., Lindsten T., Ross A.J., MacGregor G.R., and Thompson C.B. BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Genes Dev 15 (2001) 1481-1486
    • (2001) Genes Dev , vol.15 , pp. 1481-1486
    • Zong, W.X.1    Lindsten, T.2    Ross, A.J.3    MacGregor, G.R.4    Thompson, C.B.5
  • 74
    • 33646373219 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced apoptosis: multiple pathways and activation of p53-up-regulated modulator of apoptosis (PUMA) and NOXA by p53
    • Li J., Lee B., and Lee A.S. Endoplasmic reticulum stress-induced apoptosis: multiple pathways and activation of p53-up-regulated modulator of apoptosis (PUMA) and NOXA by p53. J Biol Chem 281 (2006) 7260-7270
    • (2006) J Biol Chem , vol.281 , pp. 7260-7270
    • Li, J.1    Lee, B.2    Lee, A.S.3
  • 75
    • 4143087106 scopus 로고    scopus 로고
    • BI-1 regulates an apoptosis pathway linked to endoplasmic reticulum stress
    • Chae H.J., Kim H.R., Xu C., Bailly-Maitre B., Krajewska M., Krajewski S., et al. BI-1 regulates an apoptosis pathway linked to endoplasmic reticulum stress. Mol Cell 15 (2004) 355-366
    • (2004) Mol Cell , vol.15 , pp. 355-366
    • Chae, H.J.1    Kim, H.R.2    Xu, C.3    Bailly-Maitre, B.4    Krajewska, M.5    Krajewski, S.6
  • 76
    • 21244462014 scopus 로고    scopus 로고
    • 2+ from endoplasmic reticulum stores and mitochondrial apoptosis during stress-induced cell death
    • 2+ from endoplasmic reticulum stores and mitochondrial apoptosis during stress-induced cell death. J Biol Chem 280 (2005) 23829-23836
    • (2005) J Biol Chem , vol.280 , pp. 23829-23836
    • Mathai, J.P.1    Germain, M.2    Shore, G.C.3
  • 77
    • 33646237823 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alpha
    • Hetz C., Bernasconi P., Fisher J., Lee A.H., Bassik M.C., Antonsson B., et al. Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alpha. Science 312 (2006) 572-576
    • (2006) Science , vol.312 , pp. 572-576
    • Hetz, C.1    Bernasconi, P.2    Fisher, J.3    Lee, A.H.4    Bassik, M.C.5    Antonsson, B.6
  • 78
    • 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., et al. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 287 (2000) 664-666
    • (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
  • 79
    • 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., et al. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev 16 (2002) 1345-1355
    • (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
  • 80
    • 33646365640 scopus 로고    scopus 로고
    • Central role of the scaffold protein tumor necrosis factor receptor-associated factor 2 in regulating endoplasmic reticulum stress-induced apoptosis
    • Mauro C., Crescenzi E., De Mattia R., Pacifico F., Mellone S., Salzano S., et al. Central role of the scaffold protein tumor necrosis factor receptor-associated factor 2 in regulating endoplasmic reticulum stress-induced apoptosis. J Biol Chem 281 (2006) 2631-2638
    • (2006) J Biol Chem , vol.281 , pp. 2631-2638
    • Mauro, C.1    Crescenzi, E.2    De Mattia, R.3    Pacifico, F.4    Mellone, S.5    Salzano, S.6
  • 81
    • 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., et al. 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 276 (2001) 13935-13940
    • (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
  • 82
    • 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., et al. 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 289 (2001) 718-724
    • (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
  • 83
    • 33744800561 scopus 로고    scopus 로고
    • Tumour necrosis factor receptor 1 mediates endoplasmic reticulum stress-induced activation of the MAP kinase JNK
    • Yang Q., Kim Y.S., Lin Y., Lewis J., Neckers L., and Liu Z.G. Tumour necrosis factor receptor 1 mediates endoplasmic reticulum stress-induced activation of the MAP kinase JNK. EMBO Rep 7 (2006) 622-627
    • (2006) EMBO Rep , vol.7 , pp. 622-627
    • Yang, Q.1    Kim, Y.S.2    Lin, Y.3    Lewis, J.4    Neckers, L.5    Liu, Z.G.6
  • 84
    • 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., and 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 26 (2006) 3071-3084
    • (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
  • 85
    • 0036193169 scopus 로고    scopus 로고
    • Activation of apoptosis signal-regulating kinase 1 by the stress-induced activating phosphorylation of pre-formed oligomer
    • Tobiume K., Saitoh M., and Ichijo H. Activation of apoptosis signal-regulating kinase 1 by the stress-induced activating phosphorylation of pre-formed oligomer. J Cell Physiol 191 (2002) 95-104
    • (2002) J Cell Physiol , vol.191 , pp. 95-104
    • Tobiume, K.1    Saitoh, M.2    Ichijo, H.3
  • 86
    • 3042636436 scopus 로고    scopus 로고
    • JAB1 participates in unfolded protein responses by association and dissociation with IRE1
    • Oono K., Yoneda T., Manabe T., Yamagishi S., Matsuda S., Hitomi J., et al. JAB1 participates in unfolded protein responses by association and dissociation with IRE1. Neurochem Int 45 (2004) 765-772
    • (2004) Neurochem Int , vol.45 , pp. 765-772
    • Oono, K.1    Yoneda, T.2    Manabe, T.3    Yamagishi, S.4    Matsuda, S.5    Hitomi, J.6
  • 87
    • 33745242294 scopus 로고    scopus 로고
    • Involvement of caspase-2 and caspase-9 in endoplasmic reticulum stress-induced apoptosis: a role for the IAPs
    • Cheung H.H., Lynn Kelly N., Liston P., and Korneluk R.G. Involvement of caspase-2 and caspase-9 in endoplasmic reticulum stress-induced apoptosis: a role for the IAPs. Exp Cell Res 312 (2006) 2347-2357
    • (2006) Exp Cell Res , vol.312 , pp. 2347-2357
    • Cheung, H.H.1    Lynn Kelly, N.2    Liston, P.3    Korneluk, R.G.4
  • 88
    • 20344392461 scopus 로고    scopus 로고
    • Caspases-2, -3, and -7 are involved in thapsigargin-induced apoptosis of SH-SY5Y neuroblastoma cells
    • Dahmer M.K. Caspases-2, -3, and -7 are involved in thapsigargin-induced apoptosis of SH-SY5Y neuroblastoma cells. J Neurosci Res 80 (2005) 576-583
    • (2005) J Neurosci Res , vol.80 , pp. 576-583
    • Dahmer, M.K.1
  • 89
    • 33645124763 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induces apoptosis by an apoptosome-dependent but caspase 12-independent mechanism
    • Di Sano F., Ferraro E., Tufi R., Achsel T., Piacentini M., and Cecconi F. Endoplasmic reticulum stress induces apoptosis by an apoptosome-dependent but caspase 12-independent mechanism. J Biol Chem 281 (2006) 2693-2700
    • (2006) J Biol Chem , vol.281 , pp. 2693-2700
    • Di Sano, F.1    Ferraro, E.2    Tufi, R.3    Achsel, T.4    Piacentini, M.5    Cecconi, F.6
  • 90
    • 2442432416 scopus 로고    scopus 로고
    • Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death
    • Hitomi J., Katayama T., Eguchi Y., Kudo T., Taniguchi M., Koyama Y., et al. Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death. J Cell Biol 165 (2004) 347-356
    • (2004) J Cell Biol , vol.165 , pp. 347-356
    • Hitomi, J.1    Katayama, T.2    Eguchi, Y.3    Kudo, T.4    Taniguchi, M.5    Koyama, Y.6
  • 91
    • 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., and Greer P.A. Ubiquitous calpains promote caspase-12 and JNK activation during endoplasmic reticulum stress-induced apoptosis. J Biol Chem 281 (2006) 16016-16024
    • (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
  • 92
    • 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., and Yasuhiko Y. An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12. J Biol Chem 277 (2002) 34287-34294
    • (2002) J Biol Chem , vol.277 , pp. 34287-34294
    • Morishima, N.1    Nakanishi, K.2    Takenouchi, H.3    Shibata, T.4    Yasuhiko, Y.5
  • 93
    • 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., et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 403 (2000) 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
  • 95
    • 33744741034 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced caspase-4 activation mediates apoptosis and neurodegeneration in INCL
    • Kim S.J., Zhang Z., Hitomi E., Lee Y.C., and Mukherjee A.B. Endoplasmic reticulum stress-induced caspase-4 activation mediates apoptosis and neurodegeneration in INCL. Hum Mol Genet 15 (2006) 1826-1834
    • (2006) Hum Mol Genet , vol.15 , pp. 1826-1834
    • Kim, S.J.1    Zhang, Z.2    Hitomi, E.3    Lee, Y.C.4    Mukherjee, A.B.5
  • 96
    • 0346487261 scopus 로고    scopus 로고
    • Role of calcium and superoxide dismutase in sensitizing mitochondria to peroxynitrite-induced permeability transition
    • Brookes P.S., and Darley-Usmar V.M. Role of calcium and superoxide dismutase in sensitizing mitochondria to peroxynitrite-induced permeability transition. Am J Physiol Heart Circ Physiol 286 (2004) H39-H46
    • (2004) Am J Physiol Heart Circ Physiol , vol.286
    • Brookes, P.S.1    Darley-Usmar, V.M.2
  • 97
    • 0036710399 scopus 로고    scopus 로고
    • Importance of individuality in oxidative stress and aging
    • Stadtman E.R. Importance of individuality in oxidative stress and aging. Free Radic Biol Med 33 (2002) 597-604
    • (2002) Free Radic Biol Med , vol.33 , pp. 597-604
    • Stadtman, E.R.1
  • 98
    • 0034634281 scopus 로고    scopus 로고
    • Endothelial dysfunction in cardiovascular diseases: the role of oxidant stress
    • Cai H., and Harrison D.G. Endothelial dysfunction in cardiovascular diseases: the role of oxidant stress. Circ Res 87 (2000) 840-844
    • (2000) Circ Res , vol.87 , pp. 840-844
    • Cai, H.1    Harrison, D.G.2
  • 99
    • 0036139524 scopus 로고    scopus 로고
    • Reactive oxygen species and signal transduction
    • Finkel T. Reactive oxygen species and signal transduction. IUBMB Life 52 (2001) 3-6
    • (2001) IUBMB Life , vol.52 , pp. 3-6
    • Finkel, T.1
  • 103
    • 33750902737 scopus 로고    scopus 로고
    • The endoplasmic reticulum: folding, calcium homeostasis, signaling, and redox control
    • Gorlach A., Klappa P., and Kietzmann T. The endoplasmic reticulum: folding, calcium homeostasis, signaling, and redox control. Antioxid Redox Signal 8 (2006) 1391-1418
    • (2006) Antioxid Redox Signal , vol.8 , pp. 1391-1418
    • Gorlach, A.1    Klappa, P.2    Kietzmann, T.3
  • 104
    • 0041324740 scopus 로고    scopus 로고
    • Effects of EGb 761 Ginkgo biloba extract on mitochondrial function and oxidative stress
    • Eckert A., Keil U., Kressmann S., Schindowski K., Leutner S., Leutz S., et al. Effects of EGb 761 Ginkgo biloba extract on mitochondrial function and oxidative stress. Pharmacopsychiatry 36 Suppl. 1 (2003) S15-S23
    • (2003) Pharmacopsychiatry , vol.36 , Issue.SUPPL. 1
    • Eckert, A.1    Keil, U.2    Kressmann, S.3    Schindowski, K.4    Leutner, S.5    Leutz, S.6
  • 105
    • 0037160091 scopus 로고    scopus 로고
    • Topology of superoxide production from different sites in the mitochondrial electron transport chain
    • St-Pierre J., Buckingham J.A., Roebuck S.J., and Brand M.D. Topology of superoxide production from different sites in the mitochondrial electron transport chain. J Biol Chem 277 (2002) 44784-44790
    • (2002) J Biol Chem , vol.277 , pp. 44784-44790
    • St-Pierre, J.1    Buckingham, J.A.2    Roebuck, S.J.3    Brand, M.D.4
  • 106
    • 0037087782 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress and cell death in astrocytes-requirement for stored Ca2+ and sustained opening of the permeability transition pore
    • Jacobson J., and Duchen M.R. Mitochondrial oxidative stress and cell death in astrocytes-requirement for stored Ca2+ and sustained opening of the permeability transition pore. J Cell Sci 115 (2002) 1175-1188
    • (2002) J Cell Sci , vol.115 , pp. 1175-1188
    • Jacobson, J.1    Duchen, M.R.2
  • 107
    • 0036877142 scopus 로고    scopus 로고
    • The endoplasmic reticulum: a multifunctional signaling organelle
    • Berridge M.J. The endoplasmic reticulum: a multifunctional signaling organelle. Cell Calcium 32 (2002) 235-249
    • (2002) Cell Calcium , vol.32 , pp. 235-249
    • Berridge, M.J.1
  • 108
    • 0034665152 scopus 로고    scopus 로고
    • Nitric oxide-dependent modification of the sarcoplasmic reticulum Ca-ATPase: localization of cysteine target sites
    • Viner R.I., Williams T.D., and Schoneich C. Nitric oxide-dependent modification of the sarcoplasmic reticulum Ca-ATPase: localization of cysteine target sites. Free Radic Biol Med 29 (2000) 489-496
    • (2000) Free Radic Biol Med , vol.29 , pp. 489-496
    • Viner, R.I.1    Williams, T.D.2    Schoneich, C.3
  • 109
    • 0028828942 scopus 로고
    • 2+ release channel from skeletal muscle sarcoplasmic reticulum
    • 2+ release channel from skeletal muscle sarcoplasmic reticulum. J Biol Chem 270 (1995) 25557-25563
    • (1995) J Biol Chem , vol.270 , pp. 25557-25563
    • Favero, T.G.1    Zable, A.C.2    Abramson, J.J.3
  • 110
    • 0032498185 scopus 로고    scopus 로고
    • Activation of the cardiac calcium release channel (ryanodine receptor) by poly-S-nitrosylation
    • Xu L., Eu J.P., Meissner G., and Stamler J.S. Activation of the cardiac calcium release channel (ryanodine receptor) by poly-S-nitrosylation. Science 279 (1998) 234-237
    • (1998) Science , vol.279 , pp. 234-237
    • Xu, L.1    Eu, J.P.2    Meissner, G.3    Stamler, J.S.4
  • 111
    • 0041761700 scopus 로고    scopus 로고
    • Oxidation of ER resident proteins upon oxidative stress: effects of altering cellular redox/antioxidant status and implications for protein maturation
    • van der Vlies D., Makkinje M., Jansens A., Braakman I., Verkleij A.J., Wirtz K.W., et al. Oxidation of ER resident proteins upon oxidative stress: effects of altering cellular redox/antioxidant status and implications for protein maturation. Antioxid Redox Signal 5 (2003) 381-387
    • (2003) Antioxid Redox Signal , vol.5 , pp. 381-387
    • van der Vlies, D.1    Makkinje, M.2    Jansens, A.3    Braakman, I.4    Verkleij, A.J.5    Wirtz, K.W.6
  • 112
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang C., Sinskey A.J., and Lodish H.F. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257 (1992) 1496-1502
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 113
    • 4544249202 scopus 로고    scopus 로고
    • Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway
    • Chakravarthi S., and Bulleid N.J. Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway. J Biol Chem 279 (2004) 39872-39879
    • (2004) J Biol Chem , vol.279 , pp. 39872-39879
    • Chakravarthi, S.1    Bulleid, N.J.2
  • 114
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell J.C., McGovern K., and Beckwith J. Identification of a protein required for disulfide bond formation in vivo. Cell 67 (1991) 581-589
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.1    McGovern, K.2    Beckwith, J.3
  • 115
    • 0030765707 scopus 로고    scopus 로고
    • Cysteine and glutathione secretion in response to protein disulfide bond formation in the ER
    • Carelli S., Ceriotti A., Cabibbo A., Fassina G., Ruvo M., and Sitia R. Cysteine and glutathione secretion in response to protein disulfide bond formation in the ER. Science 277 (1997) 1681-1684
    • (1997) Science , vol.277 , pp. 1681-1684
    • Carelli, S.1    Ceriotti, A.2    Cabibbo, A.3    Fassina, G.4    Ruvo, M.5    Sitia, R.6
  • 116
    • 0034494605 scopus 로고    scopus 로고
    • Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum
    • Frand A.R., and Kaiser C.A. Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum. Mol Biol Cell 11 (2000) 2833-2843
    • (2000) Mol Biol Cell , vol.11 , pp. 2833-2843
    • Frand, A.R.1    Kaiser, C.A.2
  • 117
    • 0031609760 scopus 로고    scopus 로고
    • The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
    • Frand A.R., and Kaiser C.A. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol Cell 1 (1998) 161-170
    • (1998) Mol Cell , vol.1 , pp. 161-170
    • Frand, A.R.1    Kaiser, C.A.2
  • 119
    • 0033163758 scopus 로고    scopus 로고
    • Competition between glutathione and protein thiols for disulphide-bond formation
    • Cuozzo J.W., and Kaiser C.A. Competition between glutathione and protein thiols for disulphide-bond formation. Nat Cell Biol 1 (1999) 130-135
    • (1999) Nat Cell Biol , vol.1 , pp. 130-135
    • Cuozzo, J.W.1    Kaiser, C.A.2
  • 120
    • 0031610364 scopus 로고    scopus 로고
    • Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum
    • Pollard M.G., Travers K.J., and Weissman J.S. Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol Cell 1 (1998) 171-182
    • (1998) Mol Cell , vol.1 , pp. 171-182
    • Pollard, M.G.1    Travers, K.J.2    Weissman, J.S.3
  • 121
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: mechanisms and consequences
    • Tu B.P., and Weissman J.S. Oxidative protein folding in eukaryotes: mechanisms and consequences. J Cell Biol 164 (2004) 341-346
    • (2004) J Cell Biol , vol.164 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 122
    • 0034681340 scopus 로고    scopus 로고
    • ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
    • Cabibbo A., Pagani M., Fabbri M., Rocchi M., Farmery M.R., Bulleid N.J., et al. ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. J Biol Chem 275 (2000) 4827-4833
    • (2000) J Biol Chem , vol.275 , pp. 4827-4833
    • Cabibbo, A.1    Pagani, M.2    Fabbri, M.3    Rocchi, M.4    Farmery, M.R.5    Bulleid, N.J.6
  • 123
    • 0034604675 scopus 로고    scopus 로고
    • Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response
    • Pagani M., Fabbri M., Benedetti C., Fassio A., Pilati S., Bulleid N.J., et al. Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response. J Biol Chem 275 (2000) 23685-23692
    • (2000) J Biol Chem , vol.275 , pp. 23685-23692
    • Pagani, M.1    Fabbri, M.2    Benedetti, C.3    Fassio, A.4    Pilati, S.5    Bulleid, N.J.6
  • 124
    • 0037517089 scopus 로고    scopus 로고
    • The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha
    • Gess B., Hofbauer K.H., Wenger R.H., Lohaus C., Meyer H.E., and Kurtz A. The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha. Eur J Biochem 270 (2003) 2228-2235
    • (2003) Eur J Biochem , vol.270 , pp. 2228-2235
    • Gess, B.1    Hofbauer, K.H.2    Wenger, R.H.3    Lohaus, C.4    Meyer, H.E.5    Kurtz, A.6
  • 125
    • 33749492425 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress signaling in disease
    • Marciniak S.J., and Ron D. Endoplasmic reticulum stress signaling in disease. Physiol Rev 86 (2006) 1133-1149
    • (2006) Physiol Rev , vol.86 , pp. 1133-1149
    • Marciniak, S.J.1    Ron, D.2
  • 126
    • 0035856949 scopus 로고    scopus 로고
    • Insulin signalling and the regulation of glucose and lipid metabolism
    • Saltiel A.R., and Kahn C.R. Insulin signalling and the regulation of glucose and lipid metabolism. Nature 414 (2001) 799-806
    • (2001) Nature , vol.414 , pp. 799-806
    • Saltiel, A.R.1    Kahn, C.R.2
  • 127
    • 0033927667 scopus 로고    scopus 로고
    • Cellular mechanisms of insulin resistance
    • Shulman G.I. Cellular mechanisms of insulin resistance. J Clin Invest 106 (2000) 171-176
    • (2000) J Clin Invest , vol.106 , pp. 171-176
    • Shulman, G.I.1
  • 128
    • 33644845569 scopus 로고    scopus 로고
    • Role of oxidative stress, endoplasmic reticulum stress, and c-Jun N-terminal kinase in pancreatic beta-cell dysfunction and insulin resistance
    • Kaneto H., Nakatani Y., Kawamori D., Miyatsuka T., Matsuoka T.A., Matsuhisa M., et al. Role of oxidative stress, endoplasmic reticulum stress, and c-Jun N-terminal kinase in pancreatic beta-cell dysfunction and insulin resistance. Int J Biochem Cell Biol 38 (2006) 782-793
    • (2006) Int J Biochem Cell Biol , vol.38 , pp. 782-793
    • Kaneto, H.1    Nakatani, Y.2    Kawamori, D.3    Miyatsuka, T.4    Matsuoka, T.A.5    Matsuhisa, M.6
  • 129
  • 131
    • 33748069813 scopus 로고    scopus 로고
    • Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes
    • Ozcan U., Yilmaz E., Ozcan L., Furuhashi M., Vaillancourt E., Smith R.O., et al. Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes. Science 313 (2006) 1137-1140
    • (2006) Science , vol.313 , pp. 1137-1140
    • Ozcan, U.1    Yilmaz, E.2    Ozcan, L.3    Furuhashi, M.4    Vaillancourt, E.5    Smith, R.O.6
  • 132
    • 0034425698 scopus 로고    scopus 로고
    • EIF2AK3, encoding translation initiation factor 2-alpha kinase 3 is mutated in patients with Wolcott-Rallison syndrome
    • Delepine M., Nicolino M., Barrett T., Golamaully M., Lathrop G.M., and Julier C. EIF2AK3, encoding translation initiation factor 2-alpha kinase 3 is mutated in patients with Wolcott-Rallison syndrome. Nat Genet 25 (2000) 406-409
    • (2000) Nat Genet , vol.25 , pp. 406-409
    • Delepine, M.1    Nicolino, M.2    Barrett, T.3    Golamaully, M.4    Lathrop, G.M.5    Julier, C.6
  • 133
    • 33746361817 scopus 로고    scopus 로고
    • Double-stranded RNA-dependent protein kinase phosphorylation of the alpha-subunit of eukaryotic translation initiation factor 2 mediates apoptosis
    • Scheuner D., Patel R., Wang F., Lee K., Kumar K., Wu J., et al. Double-stranded RNA-dependent protein kinase phosphorylation of the alpha-subunit of eukaryotic translation initiation factor 2 mediates apoptosis. J Biol Chem 281 (2006) 21458-21468
    • (2006) J Biol Chem , vol.281 , pp. 21458-21468
    • Scheuner, D.1    Patel, R.2    Wang, F.3    Lee, K.4    Kumar, K.5    Wu, J.6
  • 134
    • 30944458057 scopus 로고    scopus 로고
    • Activation-dependent substrate recruitment by the eukaryotic translation initiation factor 2 kinase PERK
    • Marciniak S.J., Garcia-Bonilla L., Hu J., Harding H.P., and Ron D. Activation-dependent substrate recruitment by the eukaryotic translation initiation factor 2 kinase PERK. J Cell Biol 172 (2006) 201-209
    • (2006) J Cell Biol , vol.172 , pp. 201-209
    • Marciniak, S.J.1    Garcia-Bonilla, L.2    Hu, J.3    Harding, H.P.4    Ron, D.5
  • 135
    • 33750502270 scopus 로고    scopus 로고
    • Oxidative stress and impaired insulin secretion in type 2 diabetes
    • Robertson R.P. Oxidative stress and impaired insulin secretion in type 2 diabetes. Curr Opin Pharmacol 6 (2006) 615-619
    • (2006) Curr Opin Pharmacol , vol.6 , pp. 615-619
    • Robertson, R.P.1
  • 136
    • 2542440824 scopus 로고    scopus 로고
    • Antioxidant enzyme activity and mRNA expression in the islets of Langerhans from the BB/S rat model of type 1 diabetes and an insulin-producing cell line
    • Sigfrid L.A., Cunningham J.M., Beeharry N., Hakan Borg L.A., Rosales Hernandez A.L., Carlsson C., et al. Antioxidant enzyme activity and mRNA expression in the islets of Langerhans from the BB/S rat model of type 1 diabetes and an insulin-producing cell line. J Mol Med 82 (2004) 325-335
    • (2004) J Mol Med , vol.82 , pp. 325-335
    • Sigfrid, L.A.1    Cunningham, J.M.2    Beeharry, N.3    Hakan Borg, L.A.4    Rosales Hernandez, A.L.5    Carlsson, C.6
  • 137
    • 0142090441 scopus 로고    scopus 로고
    • 'Unfolding' pathways in neurodegenerative disease
    • Forman M.S., Lee V.M., and Trojanowski J.Q. 'Unfolding' pathways in neurodegenerative disease. Trends Neurosci 26 (2003) 407-410
    • (2003) Trends Neurosci , vol.26 , pp. 407-410
    • Forman, M.S.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 138
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe D.J. Folding proteins in fatal ways. Nature 426 (2003) 900-904
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 139
  • 140
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N.F., Sampat R.M., and Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292 (2001) 1552-1555
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 141
    • 0033933048 scopus 로고    scopus 로고
    • Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
    • Shimura H., Hattori N., Kubo S., Mizuno Y., Asakawa S., Minoshima S., et al. Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat Genet 25 (2000) 302-305
    • (2000) Nat Genet , vol.25 , pp. 302-305
    • Shimura, H.1    Hattori, N.2    Kubo, S.3    Mizuno, Y.4    Asakawa, S.5    Minoshima, S.6
  • 142
    • 0035967883 scopus 로고    scopus 로고
    • An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
    • Imai Y., Soda M., Inoue H., Hattori N., Mizuno Y., and Takahashi R. An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell 105 (2001) 891-902
    • (2001) Cell , vol.105 , pp. 891-902
    • Imai, Y.1    Soda, M.2    Inoue, H.3    Hattori, N.4    Mizuno, Y.5    Takahashi, R.6
  • 143
    • 0034680913 scopus 로고    scopus 로고
    • Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity
    • Imai Y., Soda M., and Takahashi R. Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. J Biol Chem 275 (2000) 35661-35664
    • (2000) J Biol Chem , vol.275 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 144
    • 10744224825 scopus 로고    scopus 로고
    • Ubiquitin carboxy-terminal hydrolase L1 binds to and stabilizes monoubiquitin in neuron
    • Osaka H., Wang Y.L., Takada K., Takizawa S., Setsuie R., Li H., et al. Ubiquitin carboxy-terminal hydrolase L1 binds to and stabilizes monoubiquitin in neuron. Hum Mol Genet 12 (2003) 1945-1958
    • (2003) Hum Mol Genet , vol.12 , pp. 1945-1958
    • Osaka, H.1    Wang, Y.L.2    Takada, K.3    Takizawa, S.4    Setsuie, R.5    Li, H.6
  • 145
    • 0032846416 scopus 로고    scopus 로고
    • Intragenic deletion in the gene encoding ubiquitin carboxy-terminal hydrolase in gad mice
    • Saigoh K., Wang Y.L., Suh J.G., Yamanishi T., Sakai Y., Kiyosawa H., et al. Intragenic deletion in the gene encoding ubiquitin carboxy-terminal hydrolase in gad mice. Nat Genet 23 (1999) 47-51
    • (1999) Nat Genet , vol.23 , pp. 47-51
    • Saigoh, K.1    Wang, Y.L.2    Suh, J.G.3    Yamanishi, T.4    Sakai, Y.5    Kiyosawa, H.6
  • 146
    • 0037131567 scopus 로고    scopus 로고
    • The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility
    • Liu Y., Fallon L., Lashuel H.A., Liu Z., and Lansbury Jr. P.T. The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility. Cell 111 (2002) 209-218
    • (2002) Cell , vol.111 , pp. 209-218
    • Liu, Y.1    Fallon, L.2    Lashuel, H.A.3    Liu, Z.4    Lansbury Jr., P.T.5
  • 147
    • 0038143287 scopus 로고    scopus 로고
    • Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons
    • Holtz W.A., and O'Malley K.L. Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons. J Biol Chem 278 (2003) 19367-19377
    • (2003) J Biol Chem , vol.278 , pp. 19367-19377
    • Holtz, W.A.1    O'Malley, K.L.2
  • 148
    • 4444237848 scopus 로고    scopus 로고
    • Identification of the protein disulfide isomerase family member PDIp in experimental Parkinson's disease and Lewy body pathology
    • Conn K.J., Gao W., McKee A., Lan M.S., Ullman M.D., Eisenhauer P.B., et al. Identification of the protein disulfide isomerase family member PDIp in experimental Parkinson's disease and Lewy body pathology. Brain Res 1022 (2004) 164-172
    • (2004) Brain Res , vol.1022 , pp. 164-172
    • Conn, K.J.1    Gao, W.2    McKee, A.3    Lan, M.S.4    Ullman, M.D.5    Eisenhauer, P.B.6
  • 150
    • 25144520251 scopus 로고    scopus 로고
    • Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP
    • Zhao L., Longo-Guess C., Harris B.S., Lee J.W., and Ackerman S.L. Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP. Nat Genet 37 (2005) 974-979
    • (2005) Nat Genet , vol.37 , pp. 974-979
    • Zhao, L.1    Longo-Guess, C.2    Harris, B.S.3    Lee, J.W.4    Ackerman, S.L.5
  • 152
    • 33846080531 scopus 로고    scopus 로고
    • Oxidative stress mediates tau-induced neurodegeneration in Drosophila
    • Dias-Santagata D., Fulga T.A., Duttaroy A., and Feany M.B. Oxidative stress mediates tau-induced neurodegeneration in Drosophila. J Clin Invest 117 (2007) 236-245
    • (2007) J Clin Invest , vol.117 , pp. 236-245
    • Dias-Santagata, D.1    Fulga, T.A.2    Duttaroy, A.3    Feany, M.B.4
  • 153
    • 0034304391 scopus 로고    scopus 로고
    • NO synthase and NO-dependent signal pathways in brain aging and neurodegenerative disorders: the role of oxidant/antioxidant balance
    • Calabrese V., Bates T.E., and Stella A.M. NO synthase and NO-dependent signal pathways in brain aging and neurodegenerative disorders: the role of oxidant/antioxidant balance. Neurochem Res 25 (2000) 1315-1341
    • (2000) Neurochem Res , vol.25 , pp. 1315-1341
    • Calabrese, V.1    Bates, T.E.2    Stella, A.M.3
  • 154
    • 24644487812 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress response and neurodegeneration
    • Paschen W., and Mengesdorf T. Endoplasmic reticulum stress response and neurodegeneration. Cell Calcium 38 (2005) 409-415
    • (2005) Cell Calcium , vol.38 , pp. 409-415
    • Paschen, W.1    Mengesdorf, T.2
  • 155
    • 33745315287 scopus 로고    scopus 로고
    • S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration
    • Uehara T., Nakamura T., Yao D., Shi Z.Q., Gu Z., Ma Y., et al. S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration. Nature 441 (2006) 513-517
    • (2006) Nature , vol.441 , pp. 513-517
    • Uehara, T.1    Nakamura, T.2    Yao, D.3    Shi, Z.Q.4    Gu, Z.5    Ma, Y.6
  • 156
    • 0035014266 scopus 로고    scopus 로고
    • Homocysteine-induced endoplasmic reticulum stress causes dysregulation of the cholesterol and triglyceride biosynthetic pathways
    • Werstuck G.H., Lentz S.R., Dayal S., Hossain G.S., Sood S.K., Shi Y.Y., et al. Homocysteine-induced endoplasmic reticulum stress causes dysregulation of the cholesterol and triglyceride biosynthetic pathways. J Clin Invest 107 (2001) 1263-1273
    • (2001) J Clin Invest , vol.107 , pp. 1263-1273
    • Werstuck, G.H.1    Lentz, S.R.2    Dayal, S.3    Hossain, G.S.4    Sood, S.K.5    Shi, Y.Y.6
  • 157
    • 0027472128 scopus 로고
    • Homocysteine inhibits von Willebrand factor processing and secretion by preventing transport from the endoplasmic reticulum
    • Lentz S.R., and Sadler J.E. Homocysteine inhibits von Willebrand factor processing and secretion by preventing transport from the endoplasmic reticulum. Blood 81 (1993) 683-689
    • (1993) Blood , vol.81 , pp. 683-689
    • Lentz, S.R.1    Sadler, J.E.2
  • 158
    • 0345535616 scopus 로고    scopus 로고
    • Homocysteine-induced endoplasmic reticulum stress and growth arrest leads to specific changes in gene expression in human vascular endothelial cells
    • Outinen P.A., Sood S.K., Pfeifer S.I., Pamidi S., Podor T.J., Li J., et al. Homocysteine-induced endoplasmic reticulum stress and growth arrest leads to specific changes in gene expression in human vascular endothelial cells. Blood 94 (1999) 959-967
    • (1999) Blood , vol.94 , pp. 959-967
    • Outinen, P.A.1    Sood, S.K.2    Pfeifer, S.I.3    Pamidi, S.4    Podor, T.J.5    Li, J.6
  • 159
    • 0035844038 scopus 로고    scopus 로고
    • Homocysteine thiolactone induces apoptotic DNA damage mediated by increased intracellular hydrogen peroxide and caspase 3 activation in HL-60 cells
    • Huang R.F., Huang S.M., Lin B.S., Wei J.S., and Liu T.Z. Homocysteine thiolactone induces apoptotic DNA damage mediated by increased intracellular hydrogen peroxide and caspase 3 activation in HL-60 cells. Life Sci 68 (2001) 2799-2811
    • (2001) Life Sci , vol.68 , pp. 2799-2811
    • Huang, R.F.1    Huang, S.M.2    Lin, B.S.3    Wei, J.S.4    Liu, T.Z.5
  • 160
    • 0035929641 scopus 로고    scopus 로고
    • Homocysteine induces programmed cell death in human vascular endothelial cells through activation of the unfolded protein response
    • Zhang C., Cai Y., Adachi M.T., Oshiro S., Aso T., Kaufman R.J., et al. Homocysteine induces programmed cell death in human vascular endothelial cells through activation of the unfolded protein response. J Biol Chem 276 (2001) 35867-35874
    • (2001) J Biol Chem , vol.276 , pp. 35867-35874
    • Zhang, C.1    Cai, Y.2    Adachi, M.T.3    Oshiro, S.4    Aso, T.5    Kaufman, R.J.6
  • 161
    • 4344575903 scopus 로고    scopus 로고
    • Role of hyperhomocysteinemia in endothelial dysfunction and atherothrombotic disease
    • Austin R.C., Lentz S.R., and Werstuck G.H. Role of hyperhomocysteinemia in endothelial dysfunction and atherothrombotic disease. Cell Death Differ 11 Suppl. 1 (2004) S56-S64
    • (2004) Cell Death Differ , vol.11 , Issue.SUPPL. 1
    • Austin, R.C.1    Lentz, S.R.2    Werstuck, G.H.3
  • 162
    • 0035107609 scopus 로고    scopus 로고
    • Hyperhomocysteinemia enhances vascular inflammation and accelerates atherosclerosis in a murine model
    • Hofmann M.A., Lalla E., Lu Y., Gleason M.R., Wolf B.M., Tanji N., et al. Hyperhomocysteinemia enhances vascular inflammation and accelerates atherosclerosis in a murine model. J Clin Invest 107 (2001) 675-683
    • (2001) J Clin Invest , vol.107 , pp. 675-683
    • Hofmann, M.A.1    Lalla, E.2    Lu, Y.3    Gleason, M.R.4    Wolf, B.M.5    Tanji, N.6
  • 163
    • 0036790413 scopus 로고    scopus 로고
    • Consequences of cellular cholesterol accumulation: basic concepts and physiological implications
    • Tabas I. Consequences of cellular cholesterol accumulation: basic concepts and physiological implications. J Clin Invest 110 (2002) 905-911
    • (2002) J Clin Invest , vol.110 , pp. 905-911
    • Tabas, I.1
  • 164
    • 0036732030 scopus 로고    scopus 로고
    • Cholesterol in health and disease
    • Tabas I. Cholesterol in health and disease. J Clin Invest 110 (2002) 583-590
    • (2002) J Clin Invest , vol.110 , pp. 583-590
    • Tabas, I.1
  • 165
    • 0042972934 scopus 로고    scopus 로고
    • The endoplasmic reticulum is the site of cholesterol-induced cytotoxicity in macrophages
    • Feng B., Yao P.M., Li Y., Devlin C.M., Zhang D., Harding H.P., et al. The endoplasmic reticulum is the site of cholesterol-induced cytotoxicity in macrophages. Nat Cell Biol 5 (2003) 781-792
    • (2003) Nat Cell Biol , vol.5 , pp. 781-792
    • Feng, B.1    Yao, P.M.2    Li, Y.3    Devlin, C.M.4    Zhang, D.5    Harding, H.P.6
  • 166
    • 33645567816 scopus 로고    scopus 로고
    • Macrophage insulin receptor deficiency increases ER stress-induced apoptosis and necrotic core formation in advanced atherosclerotic lesions
    • Han S., Liang C.P., DeVries-Seimon T., Ranalletta M., Welch C.L., Collins-Fletcher K., et al. Macrophage insulin receptor deficiency increases ER stress-induced apoptosis and necrotic core formation in advanced atherosclerotic lesions. Cell Metab 3 (2006) 257-266
    • (2006) Cell Metab , vol.3 , pp. 257-266
    • Han, S.1    Liang, C.P.2    DeVries-Seimon, T.3    Ranalletta, M.4    Welch, C.L.5    Collins-Fletcher, K.6
  • 167
    • 0036176783 scopus 로고    scopus 로고
    • Plasma free fatty acid levels and the risk of ischemic heart disease in men: prospective results from the Quebec cardiovascular study
    • Pirro M., Mauriege P., Tchernof A., Cantin B., Dagenais G.R., Despres J.P., et al. Plasma free fatty acid levels and the risk of ischemic heart disease in men: prospective results from the Quebec cardiovascular study. Atherosclerosis 160 (2002) 377-384
    • (2002) Atherosclerosis , vol.160 , pp. 377-384
    • Pirro, M.1    Mauriege, P.2    Tchernof, A.3    Cantin, B.4    Dagenais, G.R.5    Despres, J.P.6
  • 168
    • 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., et al. 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 280 (2005) 21763-21772
    • (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
  • 169
    • 0033552883 scopus 로고    scopus 로고
    • Atherosclerosis-an inflammatory disease
    • Ross R. Atherosclerosis-an inflammatory disease. N Engl J Med 340 (1999) 115-126
    • (1999) N Engl J Med , vol.340 , pp. 115-126
    • Ross, R.1


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