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Volumn 4, Issue 12, 2004, Pages 966-977

The role of the unfolded protein response in tumour development: Friend or foe?

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ANTINEOPLASTIC AGENT;

EID: 10344222124     PISSN: 1474175X     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrc1505     Document Type: Review
Times cited : (640)

References (109)
  • 1
    • 0026843954 scopus 로고
    • Mammalian stress response: Induction of the glucose-regulated protein family
    • Lee, A. S. Mammalian stress response: induction of the glucose-regulated protein family. Curr. Opin. Cell Biol. 4, 267-273 (1992).
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 267-273
    • Lee, A.S.1
  • 2
    • 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 286, 1882-1888 (1999).
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 3
    • 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. Neuro. 28, 51-65 (2004).
    • (2004) J. Chem. Neuro. , vol.28 , pp. 51-65
    • Ma, Y.1    Hendershot, L.M.2
  • 4
    • 0033525198 scopus 로고    scopus 로고
    • The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct
    • Brodsky, J. L. et al. The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct. J. Biol. Chem. 274, 3453-3460 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 3453-3460
    • Brodsky, J.L.1
  • 5
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • Kozutsumi, Y., Segal, M., Normington, K., Gething, M. J. & Sambrook, J. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332, 462-464 (1988). A range of pharmacological agents had been used to activate an undefined signal-transduction cascade that led to the coordinate upregulation of resident ER chaperones. The authors of this paper hypothesized that all of the agents used could affect normal protein folding in the ER and demonstrated that the upstream signal was the presence of unfolded proteins in the ER.
    • (1988) Nature , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.J.4    Sambrook, J.5
  • 6
    • 0027305620 scopus 로고
    • +/CDC28-related kinase activity is required for signalling from the ER to the nucleus
    • +/CDC28-related kinase activity is required for signalling from the ER to the nucleus. Cell 74, 743-756 (1993).
    • (1993) Cell , vol.74 , pp. 743-756
    • Mori, K.1    Ma, W.2    Gething, M.J.3    Sambrook, J.4
  • 7
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • Cox, J. S., Shamu, C. E. & Walter, P. Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 73, 1197-1206 (1993).
    • (1993) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 8
    • 0034694896 scopus 로고    scopus 로고
    • Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast
    • Okamura, K., Kimata, Y., Higashio, H., Tsuru, A. & Kohno, K. Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast. Biochem. Biophys. Res. Commun. 279, 445-450 (2000).
    • (2000) Biochem. Biophys. Res. Commun. , vol.279 , pp. 445-450
    • Okamura, K.1    Kimata, Y.2    Higashio, H.3    Tsuru, A.4    Kohno, K.5
  • 9
    • 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. & Walter, P. The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response. Cell 90, 1031-1039 (1997). Demonstrated that during ER stress the endonuclease domain of the Ire1 kinase is activated to cleave the mRNA of the Hac1 transcription factor, allowing it to be synthesized and transactivate target genes of the UPR. This laid the foundation for future efforts to decipher the UPR pathway in higher organisms.
    • (1997) Cell , vol.90 , pp. 1031-1039
    • Sidrauski, C.1    Walter, P.2
  • 10
    • 0030297537 scopus 로고    scopus 로고
    • A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response
    • Cox, J. S. & Walter, P. A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell 87, 391-404 (1996).
    • (1996) Cell , vol.87 , pp. 391-404
    • Cox, J.S.1    Walter, P.2
  • 11
    • 0035978485 scopus 로고    scopus 로고
    • The unfolded protein response and Alzheimer's disease
    • Imaizumi, K. et al. The unfolded protein response and Alzheimer's disease. Biochim. Biophys. Acta 1536, 85-96 (2001).
    • (2001) Biochim. Biophys. Acta , vol.1536 , pp. 85-96
    • Imaizumi, K.1
  • 12
    • 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. 22, 5435-5445 (2003).
    • (2003) EMBO J. , vol.22 , pp. 5435-5445
    • Hetz, C.1    Russelakis-Carneiro, M.2    Maundrell, K.3    Castilla, J.4    Soto, C.5
  • 13
    • 0043032816 scopus 로고    scopus 로고
    • 2+-ATPase in a mouse model of Sandhoff disease and prevention by treatment with N-butyldeoxynojirimycin
    • 2+-ATPase in a mouse model of Sandhoff disease and prevention by treatment with N-butyldeoxynojirimycin. J. Biol. Chem. 278, 29496-29501 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 29496-29501
    • Pelled, D.1
  • 14
    • 4444355320 scopus 로고    scopus 로고
    • G(M1)-ganglioside-mediated actuation of the unfolded protein response causes neuronal death in a neurodegenerative gangliosidosis
    • Tessitore, A. et al. G(M1)-ganglioside-mediated actuation of the unfolded protein response causes neuronal death in a neurodegenerative gangliosidosis. Mol. Cell 15, 753-766 (2004).
    • (2004) Mol. Cell , vol.15 , pp. 753-766
    • Tessitore, A.1
  • 15
    • 0042972934 scopus 로고    scopus 로고
    • The endoplasmic reticulum is the site of cholesterol-induced cytotoxicity in macrophages
    • Feng, B. et al. The endoplasmic reticulum is the site of cholesterol-induced cytotoxicity in macrophages. Nature Cell Biol. 5, 781-792 (2003).
    • (2003) Nature Cell Biol. , vol.5 , pp. 781-792
    • Feng, B.1
  • 16
    • 0035423875 scopus 로고    scopus 로고
    • The glucose-regulated proteins: Stress induction and clinical applications
    • Lee, A. S. The glucose-regulated proteins: stress induction and clinical applications. Trends Biochem. Sci. 26, 504-510 (2001).
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 504-510
    • Lee, A.S.1
  • 17
    • 0034973982 scopus 로고    scopus 로고
    • Translational control is required for the unfolded protein response and in vivo glucose homeostasis
    • Scheuner, D. et al. Translational control is required for the unfolded protein response and in vivo glucose homeostasis. Mol. Cell 7, 1165-1176 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 1165-1176
    • Scheuner, D.1
  • 18
    • 0037385313 scopus 로고    scopus 로고
    • Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-1
    • Iwakoshi, N. N. et al. Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-1. Nature Immunol. 4, 321-329 (2003).
    • (2003) Nature Immunol. , vol.4 , pp. 321-329
    • Iwakoshi, N.N.1
  • 19
    • 0034650851 scopus 로고    scopus 로고
    • An essential role in liver development for transcription factor XBP-1
    • Reimold, A. M. et al. An essential role in liver development for transcription factor XBP-1. Genes Dev. 14, 152-157 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 152-157
    • Reimold, A.M.1
  • 20
    • 0037073712 scopus 로고    scopus 로고
    • Activation of an unfolded protein response during differentiation of antibody-secreting B cells
    • Gass, J. N., Gifford, N. M. & Brewer, J. W. Activation of an unfolded protein response during differentiation of antibody-secreting B cells. J. Biol. Chem. 277, 49047-49054 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 49047-49054
    • Gass, J.N.1    Gifford, N.M.2    Brewer, J.W.3
  • 21
    • 0034021399 scopus 로고    scopus 로고
    • Overexpression of the glucose-regulated stress gene GRP78 in malignant but not benign human breast lesions
    • Femandez, P. M. et al. Overexpression of the glucose-regulated stress gene GRP78 in malignant but not benign human breast lesions. Breast Cancer Res. Treat. 59, 15-26 (2000). Correlated increased malignancy of human breast cancers malignancy to upregulation of BiP at both the transcriptional and translational level.
    • (2000) Breast Cancer Res. Treat. , vol.59 , pp. 15-26
    • Femandez, P.M.1
  • 22
    • 0038216621 scopus 로고    scopus 로고
    • Activation of the ATF6, XBP1 and grp78 genes in human hepatocellular carcinoma: A possible involvement of the ER stress pathway in hepatocarcinogenesis
    • Shuda, M. et al. Activation of the ATF6, XBP1 and grp78 genes in human hepatocellular carcinoma: a possible involvement of the ER stress pathway in hepatocarcinogenesis. J. Hepatol. 38, 605-614 (2003). Demonstrated the activation of both the ATF6 and IRE1-dependent branches of the UPR pathway in human hepatocellular carcinoma tissue samples at both the mRNA and protein level.
    • (2003) J. Hepatol. , vol.38 , pp. 605-614
    • Shuda, M.1
  • 23
    • 0035890417 scopus 로고    scopus 로고
    • Induction of glucose-regulated protein 78 by chronic hypoxia in human gastric tumor cells through a protein kinase C-ε/ERK/AP-1 signaling cascade
    • Song, M. S., Park, Y. K., Lee, J. H. & Park, K. Induction of glucose-regulated protein 78 by chronic hypoxia in human gastric tumor cells through a protein kinase C-ε/ERK/AP-1 signaling cascade. Cancer Res. 61, 8322-8330 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 8322-8330
    • Song, M.S.1    Park, Y.K.2    Lee, J.H.3    Park, K.4
  • 24
    • 0036193187 scopus 로고    scopus 로고
    • Overexpression of glucose-regulated protein 94 (Grp94) in esophageal adenocarcinomas of a rat surgical model and humans
    • Chen, X., Ding, Y., Liu, C. G., Mikhail, S. & Yang, C. S. Overexpression of glucose-regulated protein 94 (Grp94) in esophageal adenocarcinomas of a rat surgical model and humans. Carcinogenesis 23, 123-130 (2002).
    • (2002) Carcinogenesis , vol.23 , pp. 123-130
    • Chen, X.1    Ding, Y.2    Liu, C.G.3    Mikhail, S.4    Yang, C.S.5
  • 25
    • 0033014498 scopus 로고    scopus 로고
    • De-regulation of GRP stress protein expression in human breast cancer cell lines
    • Gazit, G., Lu, J. & Lee, A. S. De-regulation of GRP stress protein expression in human breast cancer cell lines. Breast Cancer Res. Treat. 54, 135-146 (1999).
    • (1999) Breast Cancer Res. Treat. , vol.54 , pp. 135-146
    • Gazit, G.1    Lu, J.2    Lee, A.S.3
  • 26
    • 0004913317 scopus 로고
    • Conduction of glucose-regulated proteins and doxorubicin resistance in Chinese hamster cells
    • Shen, J. et al. Conduction of glucose-regulated proteins and doxorubicin resistance in Chinese hamster cells. Proc. Natl Acad. Sci. USA 84, 3278-3282 (1987).
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3278-3282
    • Shen, J.1
  • 27
    • 0035872446 scopus 로고    scopus 로고
    • Regulation of tumor angiogenesis by oxygen-regulated protein 150, an inducible endoplasmic reticulum chaperone
    • Ozawa, K. et al. Regulation of tumor angiogenesis by oxygen-regulated protein 150, an inducible endoplasmic reticulum chaperone. Cancer Res. 61, 4206-4213 (2001). Showed that GRP170, a gene that is regulated by both hypoxic and ER-stress response pathways, has an important role in facilitating the secretion of VEGF in vitro and angiogenesis during tumour development in vivo.
    • (2001) Cancer Res. , vol.61 , pp. 4206-4213
    • Ozawa, K.1
  • 28
    • 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 93, 7690-7694 (1996). Directly demonstrated the significance of ER-chaperone upregulation in tumour progression.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7690-7694
    • Jamora, C.1    Dennert, G.2    Lee, A.S.3
  • 29
    • 4444302042 scopus 로고    scopus 로고
    • Effect on tumor cells of blocking survival response to glucose deprivation
    • Park, H. R. et al. Effect on tumor cells of blocking survival response to glucose deprivation. J. Natl Cancer Inst. 96, 1300-1310 (2004).
    • (2004) J. Natl. Cancer Inst. , vol.96 , pp. 1300-1310
    • Park, H.R.1
  • 30
    • 4344660747 scopus 로고    scopus 로고
    • XBP1 is essential for survival under hypoxic conditions and is required for tumor growth
    • Romero-Ramirez, L. et al. XBP1 is essential for survival under hypoxic conditions and is required for tumor growth. Cancer Res. 64, 5943-5947 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 5943-5947
    • Romero-Ramirez, L.1
  • 31
    • 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 100, 9946-9951 (2003).
    • (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
  • 32
    • 2342667387 scopus 로고    scopus 로고
    • The development of proteasome inhibitors as anticancer drugs
    • Adams, J. The development of proteasome inhibitors as anticancer drugs. Cancer Cell 5, 417-421 (2004).
    • (2004) Cancer Cell , vol.5 , pp. 417-421
    • Adams, J.1
  • 33
    • 11144353536 scopus 로고    scopus 로고
    • 18F]fluorodeoxyglucose positron emission tomography imaging
    • 18F]fluorodeoxyglucose positron emission tomography imaging. Clin. Cancer Res. 10, 2245-2252 (2004).
    • (2004) Clin. Cancer Res. , vol.10 , pp. 2245-2252
    • Rajendran, J.G.1
  • 34
    • 0141961152 scopus 로고    scopus 로고
    • The vascular network of tumours: What is it not for?
    • Sivridis, E., Giatromanolaki, A. & Koukourakis, M. I. The vascular network of tumours: what is it not for? J. Pathol. 201, 173-180 (2003).
    • (2003) J. Pathol. , vol.201 , pp. 173-180
    • Sivridis, E.1    Giatromanolaki, A.2    Koukourakis, M.I.3
  • 35
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding, H. P. et al. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol. Cell 6, 1099-1108 (2000). Identified a new section of the UPR that is found in higher eukaryotes. This signalling pathway is downstream of PERK and activates a distinct group of genes that are also activated by various other cellular stress conditions, including amino-acid deprivation and hypoxia.
    • (2000) Mol. Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1
  • 36
    • 1842791361 scopus 로고    scopus 로고
    • Herp is dually regulated by both the endoplasmic reticulum stress-specific branch of the unfolded protein response and a branch that is shared with other cellular stress pathways
    • Ma, Y. & Hendershot, L. M. Herp is dually regulated by both the endoplasmic reticulum stress-specific branch of the unfolded protein response and a branch that is shared with other cellular stress pathways. J. Biol. Chem. 279, 13792-13799 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 13792-13799
    • Ma, Y.1    Hendershot, L.M.2
  • 37
    • 0842303171 scopus 로고    scopus 로고
    • HIF-1 and hypoxic response: The plot thickens
    • Poellinger, L. & Johnson, R. S. HIF-1 and hypoxic response: the plot thickens. Curr. Opin. Genet. Dev. 14, 81-85 (2004).
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 81-85
    • Poellinger, L.1    Johnson, R.S.2
  • 38
    • 0035812772 scopus 로고    scopus 로고
    • 2, and the 3 PHDs: How animal cells signal hypoxia to the nucleus
    • 2, and the 3 PHDs: how animal cells signal hypoxia to the nucleus. Cell 107, 1-3 (2001).
    • (2001) Cell , vol.107 , pp. 1-3
    • Semenza, G.L.1
  • 39
    • 0038037735 scopus 로고    scopus 로고
    • Regulation of angiogenesis by hypoxia: Role of the HIF system
    • Pugh, C. W. & Ratcliffe, P. J. Regulation of angiogenesis by hypoxia: role of the HIF system. Nature Med. 9, 677-684 (2003).
    • (2003) Nature Med. , vol.9 , pp. 677-684
    • Pugh, C.W.1    Ratcliffe, P.J.2
  • 40
    • 0036837864 scopus 로고    scopus 로고
    • Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor elF2α
    • Koumenis, C. et al. Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor elF2α. Mol. Cell. Biol. 22, 7405-7416 (2002). Demonstrated an overlap between one section of the hypoxic response and the UPR.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7405-7416
    • Koumenis, C.1
  • 41
    • 4344648874 scopus 로고    scopus 로고
    • Activating transcription factor 4 is translationally regulated by hypoxic stress
    • Blais, J. D. et al. Activating transcription factor 4 is translationally regulated by hypoxic stress. Mol. Cell. Biol. 24, 7469-7482 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7469-7482
    • Blais, J.D.1
  • 42
    • 0028268629 scopus 로고
    • Hypoxia causes the activation of nuclear factor κB through the phosphorylation of IκBα on tyrosine residues
    • Koong, A. C., Chen, E. Y. & Giaccia, A. J. Hypoxia causes the activation of nuclear factor κB through the phosphorylation of IκBα on tyrosine residues. Cancer Res. 54, 1425-1430 (1994).
    • (1994) Cancer Res. , vol.54 , pp. 1425-1430
    • Koong, A.C.1    Chen, E.Y.2    Giaccia, A.J.3
  • 43
    • 0043133837 scopus 로고    scopus 로고
    • Phosphorylation of the α subunit of eukaryotic initiation factor 2 is required for activation of NF-κB in response to diverse cellular stresses
    • Jiang, H. Y. et al. Phosphorylation of the α subunit of eukaryotic initiation factor 2 is required for activation of NF-κB in response to diverse cellular stresses. Mol. Cell. Biol. 23, 5651-5663 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5651-5663
    • Jiang, H.Y.1
  • 44
    • 0033572417 scopus 로고    scopus 로고
    • Hypoxia induces p53 accumulation through MDM2 down-regulation and inhibition of E6-mediated degradation
    • Alarcon, R., Koumenis, C., Geyer, R. K., Maki, C. G. & Giaccia, A. J. Hypoxia induces p53 accumulation through MDM2 down-regulation and inhibition of E6-mediated degradation. Cancer Res. 59, 6046-6051 (1999).
    • (1999) Cancer Res. , vol.59 , pp. 6046-6051
    • Alarcon, R.1    Koumenis, C.2    Geyer, R.K.3    Maki, C.G.4    Giaccia, A.J.5
  • 45
    • 10744232627 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induces p53 cytoplasmic localization and prevents p53-dependent apoptosis by a pathway involving glycogen synthase kinase-3β
    • Qu, L. et al. Endoplasmic reticulum stress induces p53 cytoplasmic localization and prevents p53-dependent apoptosis by a pathway involving glycogen synthase kinase-3β. Genes Dev. 18, 261-277 (2004). Showed that p53 is regulated by both the hypoxic and the ER-stress response pathways, but in opposite ways.
    • (2004) Genes Dev. , vol.18 , pp. 261-277
    • Qu, L.1
  • 46
    • 0031039243 scopus 로고    scopus 로고
    • The biology of vascular endothelial growth factor
    • Ferrara, N. & Davis-Smyth, T. The biology of vascular endothelial growth factor. Endocr. Rev. 18, 4-25 (1997).
    • (1997) Endocr. Rev. , vol.18 , pp. 4-25
    • Ferrara, N.1    Davis-Smyth, T.2
  • 47
    • 2442572249 scopus 로고    scopus 로고
    • Homocysteine increases the expression of vascular endothelial growth factor by a mechanism involving endoplasmic reticulum stress and transcription factor ATF4
    • Roybal, C. N. et al. Homocysteine increases the expression of vascular endothelial growth factor by a mechanism involving endoplasmic reticulum stress and transcription factor ATF4. J. Biol. Chem. 279, 14844-14852 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 14844-14852
    • Roybal, C.N.1
  • 48
    • 0031550259 scopus 로고    scopus 로고
    • Cloning and expression of cDNA encoding the human 150 kDa oxygen-regulated protein, ORP150
    • Ikeda, J. et al. Cloning and expression of cDNA encoding the human 150 kDa oxygen-regulated protein, ORP150. Biochem. Biophys. Res. Commun. 230, 94-99 (1997).
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 94-99
    • Ikeda, J.1
  • 49
    • 0034946944 scopus 로고    scopus 로고
    • Expression of the oxygen-regulated protein ORP 150 accelerates wound healing by modulating intracellular VEGF transport
    • Ozawa, K. et al. Expression of the oxygen-regulated protein ORP 150 accelerates wound healing by modulating intracellular VEGF transport. J. Clin. Invest. 108, 41-50 (2001).
    • (2001) J. Clin. Invest. , vol.108 , pp. 41-50
    • Ozawa, K.1
  • 51
    • 0023589208 scopus 로고
    • Breast cancer and atypia among young and middle-aged women: A study of 110 medicolegal autopsies
    • Nielsen, M., Thomsen, J. L., Primdahl, S., Dyreborg, U. & Andersen, J. A. Breast cancer and atypia among young and middle-aged women: a study of 110 medicolegal autopsies. Br. J. Cancer 56, 814-819 (1987).
    • (1987) Br. J. Cancer , vol.56 , pp. 814-819
    • Nielsen, M.1    Thomsen, J.L.2    Primdahl, S.3    Dyreborg, U.4    Andersen, J.A.5
  • 52
    • 0027468277 scopus 로고
    • Advances in diagnostic imaging and overestimations of disease prevalence and the benefits of therapy
    • Black, W. C. & Welch, H. G. Advances in diagnostic imaging and overestimations of disease prevalence and the benefits of therapy. N. Engl. J. Med. 328, 1237-1243 (1993).
    • (1993) N. Engl. J. Med. , vol.328 , pp. 1237-1243
    • Black, W.C.1    Welch, H.G.2
  • 55
    • 5644222639 scopus 로고    scopus 로고
    • GFP tagging of ERK and p38 pathways reveals novel dynamics of pathway activation during primary and metastatic growth
    • Aguirre-Ghiso, J. A., Ossowski, L. & Rosenbaum, S. GFP tagging of ERK and p38 pathways reveals novel dynamics of pathway activation during primary and metastatic growth. Cancer Res. 64, 7336-7345 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 7336-7345
    • Aguirre-Ghiso, J.A.1    Ossowski, L.2    Rosenbaum, S.3
  • 56
    • 0037106329 scopus 로고    scopus 로고
    • Requirement of the p38 mitogen-activated protein kinase signalling pathway for the induction of the 78 kDa glucose-regulated protein/immunoglobulin heavy-chain binding protein by azetidine stress: Activating transcription factor 6 as a target for stress-induced phosphorylation
    • Luo, S. & Lee, A. S. Requirement of the p38 mitogen-activated protein kinase signalling pathway for the induction of the 78 kDa glucose-regulated protein/immunoglobulin heavy-chain binding protein by azetidine stress: activating transcription factor 6 as a target for stress-induced phosphorylation. Biochem. J. 366, 787-795 (2002).
    • (2002) Biochem. J. , vol.366 , pp. 787-795
    • Luo, S.1    Lee, A.S.2
  • 57
    • 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 272, 1347-1349 (1996).
    • (1996) Science , vol.272 , pp. 1347-1349
    • Wang, X.Z.1    Ron, D.2
  • 58
    • 0033739622 scopus 로고    scopus 로고
    • PERK mediates cell-cycle exit during the mammalian unfolded protein response
    • Brewer, J. W. & Diehl, J. A. PERK mediates cell-cycle exit during the mammalian unfolded protein response. Proc. Natl Acad. Sci. USA 97, 12625-12630 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12625-12630
    • Brewer, J.W.1    Diehl, J.A.2
  • 60
    • 0037077254 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program. An Apaf-1-independent intrinsic pathway
    • Rao, R. V. et al. Coupling endoplasmic reticulum stress to the cell death program. An Apaf-1-independent intrinsic pathway. J. Biol. Chem. 277, 21836-21842 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 21836-21842
    • Rao, R.V.1
  • 61
    • 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. & 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, 439-453 (1992).
    • (1992) Genes. Dev. , vol.6 , pp. 439-453
    • Ron, D.1    Habener, J.F.2
  • 62
    • 0032054744 scopus 로고    scopus 로고
    • CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum
    • Zinszner, H. et al. CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum. Genes Dev. 12, 982-995 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 982-995
    • Zinszner, H.1
  • 63
    • 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. 21, 1249-1259 (2001).
    • (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
  • 64
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang, X. The expanding role of mitochondria in apoptosis. Genes Dev. 15, 2922-2933 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 65
    • 0037810844 scopus 로고    scopus 로고
    • Bax and Bak can localize to the endoplasmic reticulum to initiate apoptosis
    • Zong, W. X. et al. Bax and Bak can localize to the endoplasmic reticulum to initiate apoptosis. J. Cell Biol. 162, 59-69 (2003).
    • (2003) J. Cell Biol. , vol.162 , pp. 59-69
    • Zong, W.X.1
  • 66
    • 0035726625 scopus 로고    scopus 로고
    • Targeting of the C-Abl tyrosine kinase to mitochondria in endoplasmic reticulum stress-induced apoptosis
    • Ito, Y. et al. Targeting of the C-Abl tyrosine kinase to mitochondria in endoplasmic reticulum stress-induced apoptosis. Mol. Cell. Biol. 21, 6233-6242 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6233-6242
    • Ito, Y.1
  • 67
    • 0034194089 scopus 로고    scopus 로고
    • Calcium signaling in the ER: Its role in neuronal plasticity and neurodegenerative disorders
    • Mattson, M. P. et al. Calcium signaling in the ER: its role in neuronal plasticity and neurodegenerative disorders. Trends Neurosci. 23, 222-229 (2000).
    • (2000) Trends Neurosci. , vol.23 , pp. 222-229
    • Mattson, M.P.1
  • 68
    • 0030450126 scopus 로고    scopus 로고
    • Short exposures to tunicamycin induce apoptosis in SV40-transformed but not in normal human fibroblasts
    • Carlberg, M. et al. Short exposures to tunicamycin induce apoptosis in SV40-transformed but not in normal human fibroblasts. Carcinogenesis 17, 2589-2596 (1996).
    • (1996) Carcinogenesis , vol.17 , pp. 2589-2596
    • Carlberg, M.1
  • 69
    • 0033537768 scopus 로고    scopus 로고
    • 2+-induced apoptosis through calcineurin dephosphorylation of BAD
    • 2+-induced apoptosis through calcineurin dephosphorylation of BAD. Science 284, 339-343 (1999).
    • (1999) Science , vol.284 , pp. 339-343
    • Wang, H.G.1
  • 70
    • 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. 150, 887-894 (2000).
    • (2000) J. Cell Biol. , vol.150 , pp. 887-894
    • Nakagawa, T.1    Yuan, J.2
  • 71
    • 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. 277, 34287-34294 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 34287-34294
    • Morishima, N.1    Nakanishi, K.2    Takenouchi, H.3    Shibata, T.4    Yasuhiko, Y.5
  • 72
    • 0035823579 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program. Mechanism of caspase activation
    • Rao, R. V. et al. Coupling endoplasmic reticulum stress to the cell death program. Mechanism of caspase activation. J. Biol. Chem. 276, 33869-33874 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 33869-33874
    • Rao, R.V.1
  • 73
    • 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. 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, 13935-13940 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 13935-13940
    • Yoneda, T.1
  • 74
    • 3543001634 scopus 로고    scopus 로고
    • Somatic mutations of CASP3 gene in human cancers
    • Soung, Y. H. et al. Somatic mutations of CASP3 gene in human cancers. Hum. Genet. 115, 112-115 (2004).
    • (2004) Hum. Genet. , vol.115 , pp. 112-115
    • Soung, Y.H.1
  • 75
    • 2442464889 scopus 로고    scopus 로고
    • Apoptosis defects and chemotherapy resistance: Molecular interaction maps and networks
    • Pommier, Y., Sordet, O., Antony, S., Hayward, R. L. Kohn, K. W. Apoptosis defects and chemotherapy resistance: molecular interaction maps and networks. Oncogene 23, 2934-2949 (2004).
    • (2004) Oncogene , vol.23 , pp. 2934-2949
    • Pommier, Y.1    Sordet, O.2    Antony, S.3    Hayward, R.L.4    Kohn, K.W.5
  • 76
    • 0242610852 scopus 로고    scopus 로고
    • Glucose depletion enhances P-glycoprotein expression in hepatoma cells: Role of endoplasmic reticulum stress response
    • Ledoux, S., Yang, R., Friedlander, G. & Laouari, D. Glucose depletion enhances P-glycoprotein expression in hepatoma cells: role of endoplasmic reticulum stress response. Cancer Res. 63, 7284-7290 (2003). First paper to link activation of the UPR in a cultured tumour cell line to the upregulation of efflux mechanisms involved in multiple chemotherapy drug resistance.
    • (2003) Cancer Res. , vol.63 , pp. 7284-7290
    • Ledoux, S.1    Yang, R.2    Friedlander, G.3    Laouari, D.4
  • 77
    • 0030014783 scopus 로고    scopus 로고
    • DNA topoisomerases
    • Wang, J. C. DNA topoisomerases. Annu. Rev. Biochem. 65, 635-692 (1996).
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 635-692
    • Wang, J.C.1
  • 79
    • 0028174984 scopus 로고
    • DNA topoisomerases: Essential enzymes and lethal targets
    • Chen, A. Y. & Liu, L. F. DNA topoisomerases: essential enzymes and lethal targets. Annu. Rev. Pharmacol. Toxicol. 34, 191-218 (1994).
    • (1994) Annu. Rev. Pharmacol. Toxicol. , vol.34 , pp. 191-218
    • Chen, A.Y.1    Liu, L.F.2
  • 80
    • 0029944106 scopus 로고    scopus 로고
    • Antitopoisomerase drug action and resistance
    • Nitiss, J. L. & Beck, W. T. Antitopoisomerase drug action and resistance. Eur. J. Cancer 32A, 958-966 (1996).
    • (1996) Eur. J. Cancer , vol.32 A , pp. 958-966
    • Nitiss, J.L.1    Beck, W.T.2
  • 81
    • 0035029153 scopus 로고    scopus 로고
    • Tumor cell death induced by topoisomerase-targeting drugs
    • Li. T. K. & Liu, L. F. Tumor cell death induced by topoisomerase-targeting drugs. Annu. Rev. Pharmacol. Toxicol. 41, 53-77 (2001).
    • (2001) Annu. Rev. Pharmacol. Toxicol. , vol.41 , pp. 53-77
    • Li, T.K.1    Liu, L.F.2
  • 82
    • 0024315683 scopus 로고
    • Depletion of topoisomerase II in isolated nuclei during a glucose-regulated stress response
    • Shen, J. W., Subjeck, J. R., Lock, R. B. & Ross, W. E. Depletion of topoisomerase II in isolated nuclei during a glucose-regulated stress response. Mol. Cell. Biol. 9, 3284-3291 (1989).
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3284-3291
    • Shen, J.W.1    Subjeck, J.R.2    Lock, R.B.3    Ross, W.E.4
  • 83
    • 0029555619 scopus 로고
    • Glucose-regulated stresses confer resistance to VP-16 in human cancer cells through a decreased expression of DNA topoisomerase II
    • Yun, J., Tomida, A., Nagata, K. & Tsuruo, T. Glucose-regulated stresses confer resistance to VP-16 in human cancer cells through a decreased expression of DNA topoisomerase II. Oncol. Res. 7, 583-590 (1995).
    • (1995) Oncol. Res. , vol.7 , pp. 583-590
    • Yun, J.1    Tomida, A.2    Nagata, K.3    Tsuruo, T.4
  • 84
    • 0037427527 scopus 로고    scopus 로고
    • Down-regulation of topoisomerase IIα is caused by up-regulation of GRP78
    • Gosky, D. & Chatterjee, S. Down-regulation of topoisomerase IIα is caused by up-regulation of GRP78. Biochem. Biophys. Res. Commun. 300, 327-332 (2003).
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , pp. 327-332
    • Gosky, D.1    Chatterjee, S.2
  • 85
    • 18344388462 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program: Role of the ER chaperone GRP78
    • Rao, R. V. et al. Coupling endoplasmic reticulum stress to the cell death program: role of the ER chaperone GRP78. FEBS Lett. 514, 122-128 (2002).
    • (2002) FEBS Lett. , vol.514 , pp. 122-128
    • Rao, R.V.1
  • 86
    • 0038080911 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: Role of ATP binding site in suppression of caspase-7 activation
    • Reddy, R. K. et al. Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: role of ATP binding site in suppression of caspase-7 activation. J. Biol. Chem. 278, 20915-20924 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 20915-20924
    • Reddy, R.K.1
  • 87
    • 0037349338 scopus 로고    scopus 로고
    • The making of the mitotic chromosome: Modem insights into classical questions
    • Swedlow, J. R. & Hirano, T. The making of the mitotic chromosome: modem insights into classical questions. Mol. Cell 11, 557-569 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 557-569
    • Swedlow, J.R.1    Hirano, T.2
  • 88
    • 3843060266 scopus 로고    scopus 로고
    • Interaction between glucose-regulated destruction domain of DNA topoisomerase IIα and MPN domain of Jab1/CSN5
    • Yun, J., Tomida, A., Andoh, T. & Tsuruo, T. Interaction between glucose-regulated destruction domain of DNA topoisomerase IIα and MPN domain of Jab1/CSN5. J. Biol. Chem. 279, 31296-31303 (2004). Identified a sequence on topo IIα that induces its proteasome-mediated destruction in response to glucose deprivation, which activates the UPR. This might explain the increased resistance to topo-II-targeting drugs in response to ER stress.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31296-31303
    • Yun, J.1    Tomida, A.2    Andoh, T.3    Tsuruo, T.4
  • 89
    • 0032527915 scopus 로고    scopus 로고
    • Prevention of brefeldin A-induced resistance to teniposide by the proteasome inhibitor MG-132: Involvement of NF-κB activation in drug resistance
    • Lin, Z. P. et al. Prevention of brefeldin A-induced resistance to teniposide by the proteasome inhibitor MG-132: involvement of NF-κB activation in drug resistance. Cancer Res. 68, 3059-3065 (1998).
    • (1998) Cancer Res. , vol.68 , pp. 3059-3065
    • Lin, Z.P.1
  • 90
    • 0016372718 scopus 로고
    • Interactions between mammalian cell DNA and inorganic platinum compounds. I. DNA interstrand cross-linking and cytotoxic properties of platinum(II) compounds
    • Pascoe, J. M. & Roberts, J. J. Interactions between mammalian cell DNA and inorganic platinum compounds. I. DNA interstrand cross-linking and cytotoxic properties of platinum(II) compounds. Biochem. Pharmacol. 23, 1359-1365 (1974).
    • (1974) Biochem. Pharmacol. , vol.23 , pp. 1359-1365
    • Pascoe, J.M.1    Roberts, J.J.2
  • 91
    • 0032992249 scopus 로고    scopus 로고
    • Cellular sensitization to cisplatin and carboplatin with decreased removal of platinum-DNA adduct by glucose-regulated stress
    • Yamada, M. et al. Cellular sensitization to cisplatin and carboplatin with decreased removal of platinum-DNA adduct by glucose-regulated stress. Cancer Chemother. Pharmacol. 44, 59-64 (1999).
    • (1999) Cancer Chemother. Pharmacol. , vol.44 , pp. 59-64
    • Yamada, M.1
  • 92
    • 0030663711 scopus 로고    scopus 로고
    • Hypersensitivity to DNA cross-linking agents associated with up-regulation of glucose-regulated stress protein GRP78
    • Chatterjee, S., Hirota, H., Belfi, C. A., Berger, S. J. & Berger, N. A. Hypersensitivity to DNA cross-linking agents associated with up-regulation of glucose-regulated stress protein GRP78. Cancer Res. 57, 5112-5116 (1997). Demonstrated a correlation between ER stress and an increased sensitivity to DNA-crosslinking agents like melphalan, BCNU and cisplatin.
    • (1997) Cancer Res. , vol.57 , pp. 5112-5116
    • Chatterjee, S.1    Hirota, H.2    Belfi, C.A.3    Berger, S.J.4    Berger, N.A.5
  • 93
    • 0037646503 scopus 로고    scopus 로고
    • Cisplatin induces endoplasmic reticulum stress and nucleus-independent apoptotic signaling
    • Mandic, A., Hansson, J., Linder, S. & Shoshan, M. C. Cisplatin induces endoplasmic reticulum stress and nucleus-independent apoptotic signaling. J. Biol. Chem. 278, 9100-9106 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 9100-9106
    • Mandic, A.1    Hansson, J.2    Linder, S.3    Shoshan, M.C.4
  • 94
    • 0024411280 scopus 로고
    • Resistance to etoposide induced by three glucose-regulated stresses in Chinese hamster ovary cells
    • Hughes, C. S., Shen, J. W. & Subjeck, J. R. Resistance to etoposide induced by three glucose-regulated stresses in Chinese hamster ovary cells. Cancer Res. 49, 4452-4454 (1989).
    • (1989) Cancer Res. , vol.49 , pp. 4452-4454
    • Hughes, C.S.1    Shen, J.W.2    Subjeck, J.R.3
  • 95
    • 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. 12, 1812-1824 (1998). Identified the mammalian homologue of yeast Ire1 kinase, which is ubiquitously expressed, and provided the first proof that the signalling machinery of the UPR pathway is highly conserved.
    • (1998) Genes. Dev. , vol.12 , pp. 1812-1824
    • Tirasophon, W.1    Welihinda, A.A.2    Kaufman, R.J.3
  • 96
    • 0032190546 scopus 로고    scopus 로고
    • Cloning of mammalian Ire1 reveals diversity in the ER stress responses
    • Wang, X.-Z. et al. Cloning of mammalian Ire1 reveals diversity in the ER stress responses. EMBO. J. 17, 5708-5717 (1998).
    • (1998) EMBO. J. , vol.17 , pp. 5708-5717
    • Wang, X.-Z.1
  • 97
    • 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 107, 881-891 (2001).
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 98
    • 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 397, 271-274 (1999).
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 99
    • 0031755020 scopus 로고    scopus 로고
    • Identification and characterization of pancreatic eukaryotic initiation factor 2α-subunit kinase, PEK, involved in translational control
    • Shi, Y. et al. Identification and characterization of pancreatic eukaryotic initiation factor 2α-subunit kinase, PEK, involved in translational control. Mol. Cell. Biol. 18, 7499-7509 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7499-7509
    • Shi, Y.1
  • 100
    • 0041315834 scopus 로고    scopus 로고
    • Delineation of the negative feedback regulatory loop that controls protein translation during ER stress
    • Ma, Y. & Hendershot, L. M. Delineation of the negative feedback regulatory loop that controls protein translation during ER stress. J. Biol. Chem. 278, 34864-34873 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 34864-34873
    • Ma, Y.1    Hendershot, L.M.2
  • 101
    • 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. 318, 1351-1365 (2002).
    • (2002) J. Mol. Biol. , vol.318 , pp. 1351-1365
    • Ma, Y.1    Brewer, J.W.2    Diehl, J.A.3    Hendershot, L.M.4
  • 102
    • 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 10, 3787-3799(1999). Identified ATF6, a new member of the mammalian UPR pathway that is not present in yeast. It delineated the unique mechanism of activation of the ER-localized transmembrane protein during ER stress, which involves cleavage of the cytosolically disposed transcription factor domain from the ER membrane.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 103
    • 0034515724 scopus 로고    scopus 로고
    • ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs
    • Ye, J. et al. ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol. Cell 6, 1355-1364 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 1355-1364
    • Ye, J.1
  • 104
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • Calfon, M. et al. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 415, 92-96 (2002).
    • (2002) Nature , vol.415 , pp. 92-96
    • Calfon, M.1
  • 105
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
    • Nakagawa, T. et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β. Nature 403, 98-103 (2000). Identified a new ER-localized caspase family member that is selectively activated during the UPR, but not during other apoptosis-inducing stress conditions.
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1
  • 106
    • 2442432416 scopus 로고    scopus 로고
    • Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Aβ-induced cell death
    • Hitomi, J. et al. Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Aβ-induced cell death. J. Cell Biol. 165, 347-356 (2004).
    • (2004) J. Cell Biol. , vol.165 , pp. 347-356
    • Hitomi, J.1
  • 107
    • 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. Nature Cell Biol. 2, 326-332 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 108
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals
    • Shen, J., Chen, X., Hendershot, L. & Prywes, R. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev. Cell 3, 99-111 (2002).
    • (2002) Dev. Cell , vol.3 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 109
    • 3042636436 scopus 로고    scopus 로고
    • JAB1 participates in unfolded protein responses by association and dissociation with IRE1
    • Oono, K. et al. JAB1 participates in unfolded protein responses by association and dissociation with IRE1. Neurochem. Int. 45, 765-772 (2004).
    • (2004) Neurochem. Int. , vol.45 , pp. 765-772
    • Oono, K.1


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