메뉴 건너뛰기




Volumn 24, Issue 21, 2004, Pages 9456-9469

Characterization of stanniocalcin 2, a novel target of the mammalian unfolded protein response with cytoprotective properties

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; HYPOCALCIN; PROTEIN SERINE THREONINE KINASE; STANNIOCALCIN 2; THAPSIGARGIN; TRANSCRIPTION FACTOR; TUNICAMYCIN; UNCLASSIFIED DRUG;

EID: 6344282203     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.24.21.9456-9469.2004     Document Type: Article
Times cited : (156)

References (70)
  • 1
    • 0036877142 scopus 로고    scopus 로고
    • The endoplasmic reticulum: A multifunctional signaling organelle
    • Berridge, M. J. 2002. The endoplasmic reticulum: a multifunctional signaling organelle. Cell Calcium 32:235-249.
    • (2002) Cell Calcium , vol.32 , pp. 235-249
    • Berridge, M.J.1
  • 2
    • 0037134020 scopus 로고    scopus 로고
    • A system for stable expression of short interfering RNAs in mammalian cells
    • Brummelkamp, T. R., R. Bernards, and R. Agami. 2002. A system for stable expression of short interfering RNAs in mammalian cells. Science 296:550-553.
    • (2002) Science , vol.296 , pp. 550-553
    • Brummelkamp, T.R.1    Bernards, R.2    Agami, R.3
  • 4
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • Calfon, M., H. Zeng, F. Urano, J. H. Till, S. R. Hubbard, H. P. Harding, S. G. Clark, and D. Ron. 2002. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 415:92-96.
    • (2002) Nature , vol.415 , pp. 92-96
    • Calfon, M.1    Zeng, H.2    Urano, F.3    Till, J.H.4    Hubbard, S.R.5    Harding, H.P.6    Clark, S.G.7    Ron, D.8
  • 5
    • 0033637082 scopus 로고    scopus 로고
    • Degradation of proteins from the ER of Saccharomyces cerevisiae requires an intact unfolded protein response pathway
    • Casagrande, R., P. Stern, M. Diehn, C. Shamu, M. Osario, M. Zuniga, P. O. Brown, and H. Ploegh. 2000. Degradation of proteins from the ER of Saccharomyces cerevisiae requires an intact unfolded protein response pathway. Mol. Cell 5:729-735.
    • (2000) Mol. Cell , vol.5 , pp. 729-735
    • Casagrande, R.1    Stern, P.2    Diehn, M.3    Shamu, C.4    Osario, M.5    Zuniga, M.6    Brown, P.O.7    Ploegh, H.8
  • 6
    • 0039592874 scopus 로고    scopus 로고
    • The sarco/endoplasmic reticulum calcium-ATPase 2b is an endoplasmic reticulum stress-inducible protein
    • Caspersen, C., P. S. Pedersen, and M. Treiman. 2000. The sarco/endoplasmic reticulum calcium-ATPase 2b is an endoplasmic reticulum stress-inducible protein. J. Biol. Chem. 275:22363-22372.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22363-22372
    • Caspersen, C.1    Pedersen, P.S.2    Treiman, M.3
  • 8
    • 0032566015 scopus 로고    scopus 로고
    • Identification of a second stanniocalcin cDNA in mouse and human: Stanniocalcin 2
    • Chang, A. C., and R. R. Reddel. 1998. Identification of a second stanniocalcin cDNA in mouse and human: stanniocalcin 2. Mol. Cell Endocrinol. 141:95-99.
    • (1998) Mol. Cell Endocrinol. , vol.141 , pp. 95-99
    • Chang, A.C.1    Reddel, R.R.2
  • 9
    • 0032567173 scopus 로고    scopus 로고
    • Molecular cloning and characterization of stanniocalcin-related protein
    • DiMattia, G. E., R. Varghese, and G. F. Wagner. 1998. Molecular cloning and characterization of stanniocalcin-related protein. Mol. Cell Endocrinol. 146:137-140.
    • (1998) Mol. Cell Endocrinol. , vol.146 , pp. 137-140
    • DiMattia, G.E.1    Varghese, R.2    Wagner, G.F.3
  • 10
    • 0036182380 scopus 로고    scopus 로고
    • Calcium and oxidative stress: From cell signaling to cell death
    • Ermak, G., and K. J. Davies. 2002. Calcium and oxidative stress: from cell signaling to cell death. Mol. Immunol. 38:713-721.
    • (2002) Mol. Immunol. , vol.38 , pp. 713-721
    • Ermak, G.1    Davies, K.J.2
  • 11
    • 0142090441 scopus 로고    scopus 로고
    • 'Unfolding' pathways in neurodegenerative disease
    • Forman, M. S., V. M. Lee, and J. Q. Trojanowski. 2003. 'Unfolding' pathways in neurodegenerative disease. Trends Neurosci. 26:407-410.
    • (2003) Trends Neurosci. , vol.26 , pp. 407-410
    • Forman, M.S.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 12
    • 0036437307 scopus 로고    scopus 로고
    • Transcriptional and translational control in the mammalian unfolded protein response
    • Harding, H. P., M. Calfon, F. Urano, I. Novoa, and D. Ron. 2002. Transcriptional and translational control in the mammalian unfolded protein response. Annu. Rev. Cell Dev. Biol. 18:575-599.
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 575-599
    • Harding, H.P.1    Calfon, M.2    Urano, F.3    Novoa, I.4    Ron, D.5
  • 13
    • 0036895383 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the development of diabetes: A review
    • Harding, H. P., and D. Ron. 2002. Endoplasmic reticulum stress and the development of diabetes: a review. Diabetes 51(Suppl. 3):S455-S461.
    • (2002) Diabetes , vol.51 , Issue.3 SUPPL.
    • Harding, H.P.1    Ron, D.2
  • 15
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • Harding, H. P., Y. Zhang, A. Bertolotti, H. Zeng, and D. Ron. 2000. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol. Cell 5:897-904.
    • (2000) Mol. Cell , vol.5 , pp. 897-904
    • Harding, H.P.1    Zhang, Y.2    Bertolotti, A.3    Zeng, H.4    Ron, D.5
  • 16
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum- resident kinase
    • Harding, H. P., Y. Zhang, and D. Ron. 1999. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397:271-274.
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 18
    • 0028087833 scopus 로고
    • Somatic cell genetic and biochemical characterization of cell lines resulting from human genomic DNA transfections of Chinese hamster ovary cell mutants defective in sterol-dependent activation of sterol synthesis and LDL receptor expression
    • Hasan, M. T., C. C. Chang, and T. Y. Chang. 1994. Somatic cell genetic and biochemical characterization of cell lines resulting from human genomic DNA transfections of Chinese hamster ovary cell mutants defective in sterol-dependent activation of sterol synthesis and LDL receptor expression. Somat. Cell Mol. Genet. 20:183-194.
    • (1994) Somat. Cell Mol. Genet. , vol.20 , pp. 183-194
    • Hasan, M.T.1    Chang, C.C.2    Chang, T.Y.3
  • 19
    • 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., H. Yoshida, H. Yanagi, T. Yura, and K. Mori. 1999. 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) Mol. Biol. Cell , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 20
    • 0038143287 scopus 로고    scopus 로고
    • Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons
    • Holtz, W. A., and K. L. O'Malley. 2003. Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons. J. Biol. Chem. 278:19367-19377.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19367-19377
    • Holtz, W.A.1    O'Malley, K.L.2
  • 21
    • 0036083511 scopus 로고    scopus 로고
    • Prospect of a stanniocalcin endocrine/paracrine system in mammals
    • Ishibashi, K., and M. Imai. 2002. Prospect of a stanniocalcin endocrine/paracrine system in mammals. Am. J. Physiol. Renal Physiol. 282:F367-F375.
    • (2002) Am. J. Physiol. Renal Physiol. , vol.282
    • Ishibashi, K.1    Imai, M.2
  • 24
    • 0034845295 scopus 로고    scopus 로고
    • Enhanced expression of Iba1, ionized calcium-binding adapter molecule 1, after transient focal cerebral ischemia in rat brain
    • Ito, D., K. Tanaka, S. Suzuki, T. Dembo, and Y. Fukuuchi. 2001. Enhanced expression of Iba1, ionized calcium-binding adapter molecule 1, after transient focal cerebral ischemia in rat brain. Stroke 32:1208-1215.
    • (2001) Stroke , vol.32 , pp. 1208-1215
    • Ito, D.1    Tanaka, K.2    Suzuki, S.3    Dembo, T.4    Fukuuchi, Y.5
  • 25
    • 0035930366 scopus 로고    scopus 로고
    • Upregulation of the Ire1-mediated signaling molecule, Bip, in ischemic rat brain
    • Ito, D., K. Tanaka, S. Suzuki, T. Dembo, A. Kosakai, and Y. Fukuuchi. 2001. Upregulation of the Ire1-mediated signaling molecule, Bip, in ischemic rat brain. Neuroreport 12:4023-4028.
    • (2001) Neuroreport , vol.12 , pp. 4023-4028
    • Ito, D.1    Tanaka, K.2    Suzuki, S.3    Dembo, T.4    Kosakai, A.5    Fukuuchi, Y.6
  • 26
    • 0034283394 scopus 로고    scopus 로고
    • Stanniocalcin 1 and 2 are secreted as phosphoproteins from human fibrosarcoma cells
    • Jellinek, D. A., A. C. Chang, M. R. Larsen, X. Wang, P. J. Robinson, and R. R. Reddel. 2000. Stanniocalcin 1 and 2 are secreted as phosphoproteins from human fibrosarcoma cells. Biochem. J. 350(Pt. 2):453-461.
    • (2000) Biochem. J. , vol.350 , Issue.2 PART , pp. 453-461
    • Jellinek, D.A.1    Chang, A.C.2    Larsen, M.R.3    Wang, X.4    Robinson, P.J.5    Reddel, R.R.6
  • 29
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls
    • Kaufman, R. J. 1999. Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev. 13:1211-1233.
    • (1999) Genes Dev. , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 30
    • 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 eIF2α
    • Koumenis, C., C. Naczki, M. Koritzinsky, S. Rastani, A. Diehl, N. Sonenberg, A. Koromilas, and B. G. Wouters. 2002. Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2α. Mol. Cell. Biol. 22:7405-7416.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7405-7416
    • Koumenis, C.1    Naczki, C.2    Koritzinsky, M.3    Rastani, S.4    Diehl, A.5    Sonenberg, N.6    Koromilas, A.7    Wouters, B.G.8
  • 32
    • 0037386064 scopus 로고    scopus 로고
    • Dysfunction of the unfolded protein response during global brain ischemia and reperfusion
    • Kumar, R., G. S. Krause, H. Yoshida, K. Mori, and D. J. DeGracia. 2003. Dysfunction of the unfolded protein response during global brain ischemia and reperfusion. J. Cereb. Blood Flow Metab. 23:462-471.
    • (2003) J. Cereb. Blood Flow Metab. , vol.23 , pp. 462-471
    • Kumar, R.1    Krause, G.S.2    Yoshida, H.3    Mori, K.4    DeGracia, D.J.5
  • 34
    • 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., W. Tirasophon, X. Shen, M. Michalak, R. Prywes, T. Okada, H. Yoshida, K. Mori, and R. J. Kaufman. 2002. IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. Genes Dev. 16:452-466.
    • (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    Yoshida, H.7    Mori, K.8    Kaufman, R.J.9
  • 35
    • 0141890293 scopus 로고    scopus 로고
    • The role of HIF-1 alpha in transcriptional regulation of the proximal tubular epithelial cell response to hypoxia
    • Leonard, M. O., D. C. Cottell, C. Godson, H. R. Brady, and C. T. Taylor. 2003. The role of HIF-1 alpha in transcriptional regulation of the proximal tubular epithelial cell response to hypoxia. J. Biol. Chem. 278:40296-40304.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40296-40304
    • Leonard, M.O.1    Cottell, D.C.2    Godson, C.3    Brady, H.R.4    Taylor, C.T.5
  • 38
    • 0038446405 scopus 로고    scopus 로고
    • The unfolded protein response
    • Liu, C. Y., and R. J. Kaufman. 2003. The unfolded protein response. J. Cell Sci. 116:1861-1862.
    • (2003) J. Cell Sci. , vol.116 , pp. 1861-1862
    • Liu, C.Y.1    Kaufman, R.J.2
  • 39
    • 0242469289 scopus 로고    scopus 로고
    • Vascular endothelial growth factor-regulated gene expression in endothelial cells: KDR-mediated induction of Egr3 and the related nuclear receptors Nur77, Nurr1, and Nor1
    • Liu, D., H. Jia, D. I. Holmes, A. Stannard, and I. Zachary. 2003. Vascular endothelial growth factor-regulated gene expression in endothelial cells: KDR-mediated induction of Egr3 and the related nuclear receptors Nur77, Nurr1, and Nor1. Arterioscler. Thromb. Vasc. Biol. 23:2002-2007.
    • (2003) Arterioscler. Thromb. Vasc. Biol. , vol.23 , pp. 2002-2007
    • Liu, D.1    Jia, H.2    Holmes, D.I.3    Stannard, A.4    Zachary, I.5
  • 41
    • 0024494427 scopus 로고
    • Reversible middle cerebral artery occlusion without craniectomy in rats
    • Longa, E. Z., P. R. Weinstein, S. Carlson, and R. Cummins. 1989. Reversible middle cerebral artery occlusion without craniectomy in rats. Stroke 20:84-91.
    • (1989) Stroke , vol.20 , pp. 84-91
    • Longa, E.Z.1    Weinstein, P.R.2    Carlson, S.3    Cummins, R.4
  • 42
    • 0022371456 scopus 로고
    • 2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence
    • 2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence. Nature 316:696-700.
    • (1985) Nature , vol.316 , pp. 696-700
    • MacLennan, D.H.1    Brandl, C.J.2    Korczak, B.3    Green, N.M.4
  • 44
    • 0346736508 scopus 로고    scopus 로고
    • Characterization of mammalian stanniocalcin receptors. Mitochondrial targeting of ligand and receptor for regulation of cellular metabolism
    • McCudden, C. R., K. A. James, C. Hasilo, and G. F. Wagner. 2002. Characterization of mammalian stanniocalcin receptors. Mitochondrial targeting of ligand and receptor for regulation of cellular metabolism. J. Biol. Chem. 277:45249-45258.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45249-45258
    • McCudden, C.R.1    James, K.A.2    Hasilo, C.3    Wagner, G.F.4
  • 45
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa, T., H. Zhu, N. Morishima, E. Li, J. Xu, B. A. Yankner, and J. Yuan. 2000. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 403:98-103.
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 46
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh, H., A. Matsuzawa, K. Tobiume, K. Saegusa, K. Takeda, K. Inoue, S. Hori, A. Kakizuka, and H. Ichijo. 2002. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev. 16:1345-1355.
    • (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    Hori, S.7    Kakizuka, A.8    Ichijo, H.9
  • 47
    • 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., H. Yoshida, R. Akazawa, M. Negishi, and K. Mori. 2002. 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. 366:585-594.
    • (2002) Biochem. J. , vol.366 , pp. 585-594
    • Okada, T.1    Yoshida, H.2    Akazawa, R.3    Negishi, M.4    Mori, K.5
  • 48
    • 0037385160 scopus 로고    scopus 로고
    • Transient cerebral ischemia activates processing of xbp1 messenger RNA indicative of endoplasmic reticulum stress
    • Paschen, W., C. Aufenberg, S. Hotop, and T. Mengesdorf. 2003. Transient cerebral ischemia activates processing of xbp1 messenger RNA indicative of endoplasmic reticulum stress. J. Cereb. Blood Flow Metab. 23:449-461.
    • (2003) J. Cereb. Blood Flow Metab. , vol.23 , pp. 449-461
    • Paschen, W.1    Aufenberg, C.2    Hotop, S.3    Mengesdorf, T.4
  • 49
    • 0035190132 scopus 로고    scopus 로고
    • Endoplasmic reticulum dysfunction: A common denominator for cell injury in acute and degenerative diseases of the brain?
    • Paschen, W., and A. Frandsen. 2001. Endoplasmic reticulum dysfunction: a common denominator for cell injury in acute and degenerative diseases of the brain? J. Neurochem. 79:719-725.
    • (2001) J. Neurochem. , vol.79 , pp. 719-725
    • Paschen, W.1    Frandsen, A.2
  • 50
    • 0042477717 scopus 로고    scopus 로고
    • Gene expression during ER stress-induced apoptosis in neurons: Induction of the BH3-only protein Bbc3/PUMA and activation of the mitochondrial apoptosis pathway
    • Reimertz, C., D. Kogel, A. Rami, T. Chittenden, and J. H. Prehn. 2003. Gene expression during ER stress-induced apoptosis in neurons: induction of the BH3-only protein Bbc3/PUMA and activation of the mitochondrial apoptosis pathway. J. Cell Biol. 162:587-597.
    • (2003) J. Cell Biol. , vol.162 , pp. 587-597
    • Reimertz, C.1    Kogel, D.2    Rami, A.3    Chittenden, T.4    Prehn, J.H.5
  • 52
    • 0347285295 scopus 로고    scopus 로고
    • A trip to the ER: Coping with stress
    • Rutkowski, D. T., and R. J. Kaufman. 2004. A trip to the ER: coping with stress. Trends Cell Biol. 14:20-28.
    • (2004) Trends Cell Biol. , vol.14 , pp. 20-28
    • Rutkowski, D.T.1    Kaufman, R.J.2
  • 54
    • 0034062960 scopus 로고    scopus 로고
    • Regulation of stanniocalcin in MDCK cells by hypertonicity and extracellular calcium
    • Sheikh-Hamad, D., D. Rouse, and Y. Yang. 2000. Regulation of stanniocalcin in MDCK cells by hypertonicity and extracellular calcium. Am. J. Physiol. Renal Physiol. 278:F417-F424.
    • (2000) Am. J. Physiol. Renal Physiol. , vol.278
    • Sheikh-Hamad, D.1    Rouse, D.2    Yang, Y.3
  • 55
    • 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., X. Chen, L. Hendershot, and R. Prywes. 2002. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev. Cell 3:99-111.
    • (2002) Dev. Cell , vol.3 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 56
    • 18244405070 scopus 로고    scopus 로고
    • Complementary signaling pathways regulate the unfolded protein response and are required for Caenorhabditis elegans development
    • Shen, X., R. E. Ellis, K. Lee, C. Y. Liu, K. Yang, A. Solomon, H. Yoshida, R. Morimoto, D. M. Kurnit, K. Mori, and R. J. Kaufman. 2001. Complementary signaling pathways regulate the unfolded protein response and are required for Caenorhabditis elegans development. Cell 107:893-903.
    • (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    Yoshida, H.7    Morimoto, R.8    Kurnit, D.M.9    Mori, K.10    Kaufman, R.J.11
  • 57
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto, C. 2003. Unfolding the role of protein misfolding in neurodegenerative diseases. Nat. Rev. Neurosci. 4:49-60.
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 49-60
    • Soto, C.1
  • 58
    • 0004009318 scopus 로고    scopus 로고
    • Culture and biochemical analysis of cells
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Spector, D. L., R. D. Goldman, and L. A. Leinwand. 1998. Culture and biochemical analysis of cells, p. 41.1-41.4. In Cells: a laboratory manual, vol. 1. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1998) Cells: A Laboratory Manual , vol.1 , pp. 411-414
    • Spector, D.L.1    Goldman, R.D.2    Leinwand, L.A.3
  • 59
    • 0026677437 scopus 로고
    • Chum salmon (Oncorhynchus keta) stanniocalcin inhibits in vitro intestinal calcium uptake in Atlantic cod (Gadus morhua)
    • Sundell, K., B. T. Bjornsson, H. Itoh, and H. Kawauchi. 1992. Chum salmon (Oncorhynchus keta) stanniocalcin inhibits in vitro intestinal calcium uptake in Atlantic cod (Gadus morhua). J. Comp. Physiol. B 162:489-495.
    • (1992) J. Comp. Physiol. B , vol.162 , pp. 489-495
    • Sundell, K.1    Bjornsson, B.T.2    Itoh, H.3    Kawauchi, H.4
  • 60
    • 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., C. K. Patil, L. Wodicka, D. J. Lockhart, J. S. Weissman, and P. Walter. 2000. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101:249-258.
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5    Walter, P.6
  • 61
    • 0036170001 scopus 로고    scopus 로고
    • Regulation of the endoplasmic reticulum calcium storage during the unfolded protein response-significance in tissue ischemia?
    • Treiman, M. 2002. Regulation of the endoplasmic reticulum calcium storage during the unfolded protein response-significance in tissue ischemia? Trends Cardiovasc. Med. 12:57-62.
    • (2002) Trends Cardiovasc. Med. , vol.12 , pp. 57-62
    • Treiman, M.1
  • 62
    • 0033693855 scopus 로고    scopus 로고
    • IRE1 and efferent signaling from the endoplasmic reticulum
    • Urano, F., A. Bertolotti, and D. Ron. 2000. IRE1 and efferent signaling from the endoplasmic reticulum. J. Cell Sci. 113(Pt. 21):3697-3702.
    • (2000) J. Cell Sci. , vol.113 , Issue.21 PART , pp. 3697-3702
    • Urano, F.1    Bertolotti, A.2    Ron, D.3
  • 63
    • 0030665019 scopus 로고    scopus 로고
    • Neuroanatomical localization, pharmacological characterization and functions of CGRP, related peptides, and their receptors
    • van Rossum, D., U. K. Hanisch, and R. Quirion. 1997. Neuroanatomical localization, pharmacological characterization and functions of CGRP, related peptides, and their receptors. Neurosci. Biobehav. Rev. 21:649-678.
    • (1997) Neurosci. Biobehav. Rev. , vol.21 , pp. 649-678
    • Van Rossum, D.1    Hanisch, U.K.2    Quirion, R.3
  • 64
    • 0000758141 scopus 로고
    • The molecular biology of the corpuscles of stannius and regulation of stanniocalcin gene expression
    • C. Hew (ed.), Academic Press, Inc., New York, N.Y.
    • Wagner, G. F. 1994. The molecular biology of the corpuscles of stannius and regulation of stanniocalcin gene expression, p. 273-306. In C. Hew (ed.), Fish physiology, vol. 13. Academic Press, Inc., New York, N.Y.
    • (1994) Fish Physiology , vol.13 , pp. 273-306
    • Wagner, G.F.1
  • 65
    • 0022508644 scopus 로고
    • Purification, characterization, and bioassay of teleocalcin, a glycoprotein from salmon corpuscles of Stannius
    • Wagner, G. F., M. Hampong, C. M. Park, and D. H. Copp. 1986. Purification, characterization, and bioassay of teleocalcin, a glycoprotein from salmon corpuscles of Stannius. Gen. Comp. Endocrinol. 63:481-491.
    • (1986) Gen. Comp. Endocrinol. , vol.63 , pp. 481-491
    • Wagner, G.F.1    Hampong, M.2    Park, C.M.3    Copp, D.H.4
  • 67
    • 2942596347 scopus 로고    scopus 로고
    • Analysis of VEGF-responsive genes involved in the activation of endothelial cells
    • Wary, K. K., G. D. Thakker, J. O. Humtsoe, and J. Yang. 2003. Analysis of VEGF-responsive genes involved in the activation of endothelial cells. Mol. Cancer 2:25.
    • (2003) Mol. Cancer , vol.2 , pp. 25
    • Wary, K.K.1    Thakker, G.D.2    Humtsoe, J.O.3    Yang, J.4
  • 68
    • 0034515724 scopus 로고    scopus 로고
    • ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs
    • Ye, J., R. B. Rawson, R. Komuro, X. Chen, U. P. Dave, R. Prywes, M. S. Brown, and J. L. Goldstein. 2000. ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol. Cell 6:1355-1364.
    • (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    Brown, M.S.7    Goldstein, J.L.8
  • 69
    • 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., T. Matsui, A. Yamamoto, T. Okada, and K. Mori. 2001. 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) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.