메뉴 건너뛰기




Volumn 22, Issue 3, 2007, Pages 193-201

Endoplasmic reticulum stress: Signaling the unfolded protein response

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL; APOPTOSIS; CHEMISTRY; HUMAN; METABOLISM; PHYSIOLOGY; PROTEIN FOLDING; PROTEIN PROCESSING; REVIEW; ROUGH ENDOPLASMIC RETICULUM; SIGNAL TRANSDUCTION;

EID: 34447527676     PISSN: 15489213     EISSN: 15489221     Source Type: Journal    
DOI: 10.1152/physiol.00050.2006     Document Type: Review
Times cited : (423)

References (115)
  • 1
    • 33745820796 scopus 로고    scopus 로고
    • Cytoplasmic IRE1alpha-mediated XBP1 mRNA splicing in the absence of nuclear processing and endoplasmic reticulum stress
    • Back SH, Lee K, Vink E, Kaufman RJ. Cytoplasmic IRE1alpha-mediated XBP1 mRNA splicing in the absence of nuclear processing and endoplasmic reticulum stress. J Biol Chem 281: 18691-18706, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 18691-18706
    • Back, S.H.1    Lee, K.2    Vink, E.3    Kaufman, R.J.4
  • 3
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti A, Zhang Y, Hendershot LM, Harding HP, Ron D. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat Cell Biol 2: 326-332, 2000.
    • (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
  • 4
    • 0036312001 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced cell death requires mitochondrial membrane permeabilization
    • Boya P, Cohen I, Zamzami N, Vieira HL, Kroemer G. Endoplasmic reticulum stress-induced cell death requires mitochondrial membrane permeabilization. Cell Death Differ 9: 465-467, 2002.
    • (2002) Cell Death Differ , vol.9 , pp. 465-467
    • Boya, P.1    Cohen, I.2    Zamzami, N.3    Vieira, H.L.4    Kroemer, G.5
  • 6
    • 0033739622 scopus 로고    scopus 로고
    • PERK mediates cell-cycle exit during the mammalian unfolded protein response
    • Brewer JW, Diehl JA. 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
  • 8
    • 0037066741 scopus 로고    scopus 로고
    • The luminal domain of ATF6 senses endoplasmic reticulum (ER) stress and causes translocation of ATF6 from the ER to the Golgi
    • Chen X, Shen J, Prywes R. The luminal domain of ATF6 senses endoplasmic reticulum (ER) stress and causes translocation of ATF6 from the ER to the Golgi. J Biol Chem 277: 13045-13052, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 13045-13052
    • Chen, X.1    Shen, J.2    Prywes, R.3
  • 9
    • 0034786019 scopus 로고    scopus 로고
    • BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis
    • Cheng EH, Wei MC, Weiler S, Flavell RA, Mak TW, Lindsten T, Korsmeyer SJ. BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. Mol Cell 8: 705-711, 2001.
    • (2001) Mol Cell , vol.8 , pp. 705-711
    • Cheng, E.H.1    Wei, M.C.2    Weiler, S.3    Flavell, R.A.4    Mak, T.W.5    Lindsten, T.6    Korsmeyer, S.J.7
  • 10
    • 33947510911 scopus 로고    scopus 로고
    • Selective inhibition of eukaryotic translation initiation factor 2alpha dephosphorylation potentiates fatty acid-induced endoplasmic reticulum stress and causes pancreatic beta-cell dysfunction and apoptosis
    • Cnop M, Ladriere L, Hekerman P, Ortis F, Cardozo AK, Dogusan Z, Flamez D, Boyce M, Yuan J, Eizirik DL. Selective inhibition of eukaryotic translation initiation factor 2alpha dephosphorylation potentiates fatty acid-induced endoplasmic reticulum stress and causes pancreatic beta-cell dysfunction and apoptosis. J Biol Chem 282: 3989-3997, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 3989-3997
    • Cnop, M.1    Ladriere, L.2    Hekerman, P.3    Ortis, F.4    Cardozo, A.K.5    Dogusan, Z.6    Flamez, D.7    Boyce, M.8    Yuan, J.9    Eizirik, D.L.10
  • 11
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • Cox JS, Shamu CE, 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
  • 12
    • 0030297537 scopus 로고    scopus 로고
    • A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response
    • Cox JS, 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
  • 14
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton M. The mitochondrial permeability transition pore and its role in cell death. Biochem J 341: 233-249, 1999.
    • (1999) Biochem J , vol.341 , pp. 233-249
    • Crompton, M.1
  • 15
    • 0034425698 scopus 로고    scopus 로고
    • EIF-2AK3, 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 GM, Julier C. EIF-2AK3, encoding translation initiation factor 2-alpha kinase 3, is mutated in patients with Wolcott-Rallison syndrome. Nat Genet 25: 406-409, 2000.
    • (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
  • 16
    • 8644282751 scopus 로고    scopus 로고
    • Translational repression mediates activation of nuclear factor kappa B by phosphorylated translation initiation factor 2
    • Deng J, Lu PD, Zhang Y, Scheuner D, Kaufman RJ, Sonenberg N, Harding HP, Ron D. Translational repression mediates activation of nuclear factor kappa B by phosphorylated translation initiation factor 2. Mol Cell Biol 24: 10161-10168, 2004.
    • (2004) Mol Cell Biol , vol.24 , pp. 10161-10168
    • Deng, J.1    Lu, P.D.2    Zhang, Y.3    Scheuner, D.4    Kaufman, R.J.5    Sonenberg, N.6    Harding, H.P.7    Ron, D.8
  • 19
    • 0034604033 scopus 로고    scopus 로고
    • Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2
    • Hacki J, Egger L, Monney L, Conus S, Rosse T, Fellay I, Borner C. Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2. Oncogene 19: 2286-2295, 2000.
    • (2000) Oncogene , vol.19 , pp. 2286-2295
    • Hacki, J.1    Egger, L.2    Monney, L.3    Conus, S.4    Rosse, T.5    Fellay, I.6    Borner, C.7
  • 20
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding HP, Novoa I, Zhang Y, Zeng H, Wek R, Schapira M, Ron D. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol Cell 6: 1099-1108, 2000.
    • (2000) Mol Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6    Ron, D.7
  • 22
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding HP, 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
  • 23
    • 0037353039 scopus 로고    scopus 로고
    • Harding HP, Zhang Y, Zeng H, Novoa I, PDL, Calfon M, Sadri N, Yun C, Popko B, Paules R, Stojdl DF, Bell JC, Hettmann T, Leiden JM, Ron D. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol Cell 11: 619-633, 2003.
    • Harding HP, Zhang Y, Zeng H, Novoa I, PDL, Calfon M, Sadri N, Yun C, Popko B, Paules R, Stojdl DF, Bell JC, Hettmann T, Leiden JM, Ron D. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol Cell 11: 619-633, 2003.
  • 24
    • 0035310752 scopus 로고    scopus 로고
    • Identification of the G13 (cAMP-response-element-binding protein-related protein) gene product related to activating transcription factor 6 as a transcriptional activator of the mammalian unfolded protein response
    • Haze K, Okada T, Yoshida H, Yanagi H, Yura T, Negishi M, Mori K. Identification of the G13 (cAMP-response-element-binding protein-related protein) gene product related to activating transcription factor 6 as a transcriptional activator of the mammalian unfolded protein response. Biochem J 355: 19-28, 2001.
    • (2001) Biochem J , vol.355 , pp. 19-28
    • Haze, K.1    Okada, T.2    Yoshida, H.3    Yanagi, H.4    Yura, T.5    Negishi, M.6    Mori, K.7
  • 25
    • 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.
    • (1999) Mol Biol Cell , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 28
    • 33745893809 scopus 로고    scopus 로고
    • Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response
    • Hollien J, Weissman JS. Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response. Science 313: 104-107, 2006.
    • (2006) Science , vol.313 , pp. 104-107
    • Hollien, J.1    Weissman, J.S.2
  • 30
    • 0043133837 scopus 로고    scopus 로고
    • Phosphorylation of the alpha subunit of eukaryotic initiation factor 2 is required for activation of NF-kappaB in response to diverse cellular stresses
    • Jiang HY, Wek SA, McGrath BC, Scheuner D, Kaufman RJ, Cavener DR, Wek RC. Phosphorylation of the alpha subunit of eukaryotic initiation factor 2 is required for activation of NF-kappaB 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    Wek, S.A.2    McGrath, B.C.3    Scheuner, D.4    Kaufman, R.J.5    Cavener, D.R.6    Wek, R.C.7
  • 31
    • 0027465942 scopus 로고    scopus 로고
    • Kohno K, Normington K, Sambrook J, MJG, Mori K. The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum. Mol Cell Biol 13: 877-890, 1993.
    • Kohno K, Normington K, Sambrook J, MJG, Mori K. The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum. Mol Cell Biol 13: 877-890, 1993.
  • 32
    • 0035937721 scopus 로고    scopus 로고
    • Identification of ERSE-II, a new cis-acting element responsible for the ATF6-dependent mammalian unfolded protein response
    • Kokame K, Kato H, Miyata T. Identification of ERSE-II, a new cis-acting element responsible for the ATF6-dependent mammalian unfolded protein response. J Biol Chem 276: 9199-9205, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 9199-9205
    • Kokame, K.1    Kato, H.2    Miyata, T.3
  • 34
    • 0027362667 scopus 로고
    • Investigation of the subcellular distribution of the bcl-2 oncoprotein: Residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes
    • Krajewski S, Tanaka S, Takayama S, Schibler MJ, Fenton W, Reed JC. Investigation of the subcellular distribution of the bcl-2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes. Cancer Res 53: 4701-4714, 1993.
    • (1993) Cancer Res , vol.53 , pp. 4701-4714
    • Krajewski, S.1    Tanaka, S.2    Takayama, S.3    Schibler, M.J.4    Fenton, W.5    Reed, J.C.6
  • 35
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • Lee AH, Iwakoshi NN, Glimcher LH. XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol Cell Biol 23: 7448-7459, 2003.
    • (2003) Mol Cell Biol , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 36
    • 0037418238 scopus 로고    scopus 로고
    • JNK phosphorylation of Bim-related members of the Bcl2 family induces Baxdependent apoptosis
    • Lei K, Davis RJ. JNK phosphorylation of Bim-related members of the Bcl2 family induces Baxdependent apoptosis. Proc Natl Acad Sci USA 100: 2432-2437, 2003.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 2432-2437
    • Lei, K.1    Davis, R.J.2
  • 38
    • 33747849846 scopus 로고    scopus 로고
    • Regulation of insulin biosynthesis in pancreatic beta cells by an endoplasmic reticulum-resident protein kinase IRE1
    • Lipson KL, Fonseca SG, Ishigaki S, Nguyen LX, Foss E, Bortell R, Rossini AA, Urano F. Regulation of insulin biosynthesis in pancreatic beta cells by an endoplasmic reticulum-resident protein kinase IRE1. Cell Metab 4: 245-254, 2006.
    • (2006) Cell Metab , vol.4 , pp. 245-254
    • Lipson, K.L.1    Fonseca, S.G.2    Ishigaki, S.3    Nguyen, L.X.4    Foss, E.5    Bortell, R.6    Rossini, A.A.7    Urano, F.8
  • 39
    • 0034637605 scopus 로고    scopus 로고
    • Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum
    • Liu CY, Schroder M, Kaufman RJ. Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum. J Biol Chem 275: 24881-24885., 2000.
    • (2000) J Biol Chem , vol.275 , pp. 24881-24885
    • Liu, C.Y.1    Schroder, M.2    Kaufman, R.J.3
  • 40
    • 5444264022 scopus 로고    scopus 로고
    • Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response
    • Lu PD, Harding HP, Ron D. Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response. Mol Cell Biol 167: 27-33, 2004.
    • (2004) Mol Cell Biol , vol.167 , pp. 27-33
    • Lu, P.D.1    Harding, H.P.2    Ron, D.3
  • 41
    • 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 AS. 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
  • 42
    • 0036314984 scopus 로고    scopus 로고
    • Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response
    • Ma Y, Brewer JW, Diehl JA, Hendershot LM. 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
  • 43
    • 33749492425 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress signaling in disease
    • Marciniak SJ, Ron D. Endoplasmic reticulum stress signaling in disease. Physiol Rev 86: 1133-1149, 2006.
    • (2006) Physiol Rev , vol.86 , pp. 1133-1149
    • Marciniak, S.J.1    Ron, D.2
  • 45
    • 0035144493 scopus 로고    scopus 로고
    • Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state
    • McCullough KD, Martindale JL, Klotz LO, Aw TY, Holbrook NJ. 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
  • 47
    • 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 MJ, Sambrook J. A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling 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
  • 48
    • 0032540253 scopus 로고    scopus 로고
    • Palindrome with spacer of one nucleotide is characteristic of the cis-acting unfolded protein response element in Saccharomyces cerevisiae
    • Mori K, Ogawa N, Kawahara T, Yanagi H, Yura T. Palindrome with spacer of one nucleotide is characteristic of the cis-acting unfolded protein response element in Saccharomyces cerevisiae. J Biol Chem 273: 9912-9920, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 9912-9920
    • Mori, K.1    Ogawa, N.2    Kawahara, T.3    Yanagi, H.4    Yura, T.5
  • 49
    • 0026628290 scopus 로고
    • A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins
    • Mori K, Sant A, Kohno K, Normington K, Gething MJ, Sambrook JF. A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins. EMBO J 11: 2583-2593, 1992.
    • (1992) EMBO J , vol.11 , pp. 2583-2593
    • Mori, K.1    Sant, A.2    Kohno, K.3    Normington, K.4    Gething, M.J.5    Sambrook, J.F.6
  • 50
    • 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
  • 51
    • 33645107263 scopus 로고    scopus 로고
    • Cleavge of the membrane-bound transcription factor OASIS in response to endoplasmic reticulum stress
    • Murakami T, Kondo S, Ogata M, Kanemoto S, Saito A, Wanaka A, Imaizumi K. Cleavge of the membrane-bound transcription factor OASIS in response to endoplasmic reticulum stress. J Neurochem 96: 1090-1100, 2006.
    • (2006) J Neurochem , vol.96 , pp. 1090-1100
    • Murakami, T.1    Kondo, S.2    Ogata, M.3    Kanemoto, S.4    Saito, A.5    Wanaka, A.6    Imaizumi, K.7
  • 52
    • 33846223428 scopus 로고    scopus 로고
    • Role of disulfide bridges formed in the lumenal domain of ATF6 in sensing endoplasmic reticulum stress
    • Nadanaka S, Okada T, Yoshida H, Mori K. Role of disulfide bridges formed in the lumenal domain of ATF6 in sensing endoplasmic reticulum stress. Mol Cell Biol 27: 1027-1043, 2006.
    • (2006) Mol Cell Biol , vol.27 , pp. 1027-1043
    • Nadanaka, S.1    Okada, T.2    Yoshida, H.3    Mori, K.4
  • 53
    • 2542488276 scopus 로고    scopus 로고
    • Activation of mammalian unfolded protein response is compatible with the quality control system operating in the endoplasmic reticulum
    • Nadanaka S, Yoshida H, Kano F, Murata M, Mori K. Activation of mammalian unfolded protein response is compatible with the quality control system operating in the endoplasmic reticulum. Mol Biol Cell 15: 2537-2548, 2004.
    • (2004) Mol Biol Cell , vol.15 , pp. 2537-2548
    • Nadanaka, S.1    Yoshida, H.2    Kano, F.3    Murata, M.4    Mori, K.5
  • 54
    • 33846201752 scopus 로고    scopus 로고
    • Analysis of ATF6 activation in site-2 protease-deficient Chinese hamster ovary cells
    • Nadanaka S, Yoshida H, Sato R, Mori K. Analysis of ATF6 activation in site-2 protease-deficient Chinese hamster ovary cells. Cell Struct Funct 31: 109-116, 2006.
    • (2006) Cell Struct Funct , vol.31 , pp. 109-116
    • Nadanaka, S.1    Yoshida, H.2    Sato, R.3    Mori, K.4
  • 55
    • 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
  • 56
    • 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 BA, Yuan J. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 403: 98-103, 2000.
    • (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
  • 57
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh H, Matsuzawa A, Tobiume K, Saegusa K, Takeda K, Inoue K, Hori S, Kakizuka A, Ichijo H. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev 16: 1345-1355, 2002.
    • (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
  • 59
    • 0035947778 scopus 로고    scopus 로고
    • Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha
    • Novoa I, Zeng H, Harding HP, Ron D. Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha. J Cell Biol 153: 1011-1022, 2001.
    • (2001) J Cell Biol , vol.153 , pp. 1011-1022
    • Novoa, I.1    Zeng, H.2    Harding, H.P.3    Ron, D.4
  • 60
    • 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, 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: 585-594, 2002.
    • (2002) Biochem J , vol.366 , pp. 585-594
    • Okada, T.1    Yoshida, H.2    Akazawa, R.3    Negishi, M.4    Mori, K.5
  • 62
    • 0035873671 scopus 로고    scopus 로고
    • CREB-H: A novel mammalian transcription factor belonging to the CREB/ATF4 family and functioning via the box-B element with a liver-specific expression
    • Omori Y, Imai J, Wantanbe M, Komatsu T, Suzuki Y, Kataoka K, Watanabe S, Tanigami A, Sugano S. CREB-H: a novel mammalian transcription factor belonging to the CREB/ATF4 family and functioning via the box-B element with a liver-specific expression. Nucleic Acids Res 29: 2154-2162, 2001.
    • (2001) Nucleic Acids Res , vol.29 , pp. 2154-2162
    • Omori, Y.1    Imai, J.2    Wantanbe, M.3    Komatsu, T.4    Suzuki, Y.5    Kataoka, K.6    Watanabe, S.7    Tanigami, A.8    Sugano, S.9
  • 63
    • 0036175128 scopus 로고    scopus 로고
    • Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes
    • Oyadomari S, Koizumi A, Takeda K, Gotoh T, Akira S, Araki E, Mori M. Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes. J Clin Invest 109: 525-532, 2002.
    • (2002) J Clin Invest , vol.109 , pp. 525-532
    • Oyadomari, S.1    Koizumi, A.2    Takeda, K.3    Gotoh, T.4    Akira, S.5    Araki, E.6    Mori, M.7
  • 66
    • 0027729197 scopus 로고
    • Reversible phosphorylation of eukaryotic initiation factor 2 alpha in response to endoplasmic reticular signaling
    • Prostko CR, Brostrom MA, Brostrom CO. Reversible phosphorylation of eukaryotic initiation factor 2 alpha in response to endoplasmic reticular signaling. Mol Cell Biochem 128: 255-265, 1993.
    • (1993) Mol Cell Biochem , vol.128 , pp. 255-265
    • Prostko, C.R.1    Brostrom, M.A.2    Brostrom, C.O.3
  • 67
    • 0033104996 scopus 로고    scopus 로고
    • The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
    • Puthalakath H, Huang DCS, O'Reilly LA, King SM, Strasser A. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol Cell 3: 287-296, 1999.
    • (1999) Mol Cell , vol.3 , pp. 287-296
    • Puthalakath, H.1    Huang, D.C.S.2    O'Reilly, L.A.3    King, S.M.4    Strasser, A.5
  • 68
    • 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, Misra V. Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis. Mol Cell Biol 22: 5639-5649, 2002.
    • (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    Misra, V.7
  • 72
    • 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: 1383-1388, 2002.
    • (2002) J Clin Invest , vol.110 , pp. 1383-1388
    • Ron, D.1
  • 73
    • 0026546365 scopus 로고    scopus 로고
    • Ron D, Habener JF. 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.
    • Ron D, Habener JF. 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.
  • 74
    • 0035812716 scopus 로고    scopus 로고
    • Block of HAC1 mRNA translation by long-range base pairing is released by cytoplasmic splicing upon induction of the unfolded protein response
    • Ruegsegger U, Leber JH, Walter P. Block of HAC1 mRNA translation by long-range base pairing is released by cytoplasmic splicing upon induction of the unfolded protein response. Cell 107: 103-114, 2001.
    • (2001) Cell , vol.107 , pp. 103-114
    • Ruegsegger, U.1    Leber, J.H.2    Walter, P.3
  • 76
    • 33747415096 scopus 로고    scopus 로고
    • Cross-talk between two apoptotic pathways activated by endoplasmic reticulum stress: Differential contribution of caspase-12 and AIF
    • Sanges D, Marigo V. Cross-talk between two apoptotic pathways activated by endoplasmic reticulum stress: differential contribution of caspase-12 and AIF. Apoptosis 11: 1629-1641, 2006.
    • (2006) Apoptosis , vol.11 , pp. 1629-1641
    • Sanges, D.1    Marigo, V.2
  • 78
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • Schubert U, Anton LC, Gibbs J, Norbury CC, Yewdell JW, Bennink JR. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 404: 770-774, 2000.
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1    Anton, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5    Bennink, J.R.6
  • 80
    • 0029903049 scopus 로고    scopus 로고
    • Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus
    • Shamu CE, Walter P. Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J 15: 3028-3039, 1996.
    • (1996) EMBO J , vol.15 , pp. 3028-3039
    • Shamu, C.E.1    Walter, P.2
  • 81
    • 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
  • 82
    • 5644244829 scopus 로고    scopus 로고
    • Dependence of site-2 protease cleavage of ATF6 on prior site-1 protease digestion is determined by the size of the luminal domain of ATF6
    • Shen J, Prywes R. Dependence of site-2 protease cleavage of ATF6 on prior site-1 protease digestion is determined by the size of the luminal domain of ATF6. J Biol Chem 279: 43046-43051, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 43046-43051
    • Shen, J.1    Prywes, R.2
  • 83
    • 0031755020 scopus 로고    scopus 로고
    • Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control
    • Shi Y, Vattem KM, Sood R, An J, Liang J, Stramm L, Wek RC. Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-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    Vattem, K.M.2    Sood, R.3    An, J.4    Liang, J.5    Stramm, L.6    Wek, R.C.7
  • 84
    • 33748862585 scopus 로고    scopus 로고
    • BH3-only proteins: Integrated control point of apoptosis
    • Shibue T, Taniguchi T. BH3-only proteins: integrated control point of apoptosis. Int J Cancer 119: 2036-2043, 2006.
    • (2006) Int J Cancer , vol.119 , pp. 2036-2043
    • Shibue, T.1    Taniguchi, T.2
  • 85
    • 0030297538 scopus 로고    scopus 로고
    • tRNA ligase is required for regulated mRNA splicing in the unfolded protein response
    • Sidrauski C, Cox JS, Walter P. tRNA ligase is required for regulated mRNA splicing in the unfolded protein response. Cell 87: 405-413, 1996.
    • (1996) Cell , vol.87 , pp. 405-413
    • Sidrauski, C.1    Cox, J.S.2    Walter, P.3
  • 86
    • 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.
    • (1997) Cell , vol.90 , pp. 1031-1039
    • Sidrauski, C.1    Walter, P.2
  • 88
    • 30044441047 scopus 로고    scopus 로고
    • CREB4, a transmembrane bZIP transcription factor and potential new substrate for regulation and cleavage by S1P
    • Stirling J, O'Hare P. CREB4, a transmembrane bZIP transcription factor and potential new substrate for regulation and cleavage by S1P. Mol Biol Cell 17: 413-426, 2006.
    • (2006) Mol Biol Cell , vol.17 , pp. 413-426
    • Stirling, J.1    O'Hare, P.2
  • 89
    • 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 JS, Greer PA. Ubiquitous calpains promote caspase-12 and JNK activation during endoplasmic reticulum stress-induced apoptosis. J Biol Chem 281: 16016-16024, 2006.
    • (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
  • 90
    • 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 AA, Kaufman RJ. 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.
    • (1998) Genes Dev , vol.12 , pp. 1812-1824
    • Tirasophon, W.1    Welihinda, A.A.2    Kaufman, R.J.3
  • 91
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers KJ, Patil CK, Wodicka L, Lockhart DJ, Weissman JS, Walter P. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101: 249-258, 2000.
    • (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
  • 92
    • 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 HP, Ron D. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 287: 664-666, 2000.
    • (2000) Science , vol.287 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6    Ron, D.7
  • 93
    • 0032190546 scopus 로고    scopus 로고
    • Cloning of mammalian Ire1 reveals diversity in the ER stress responses
    • Wang XZ, Harding HP, Zhang Y, Jolicoeur EM, Kuroda M, Ron D. 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    Harding, H.P.2    Zhang, Y.3    Jolicoeur, E.M.4    Kuroda, M.5    Ron, D.6
  • 95
    • 0034282912 scopus 로고    scopus 로고
    • Activation of ATF6 and an ATF6 DNA binding site by the endoplasmic reticulum stress response
    • Wang Y, Shen J, Arenzana N, Tirasophon W, Kaufman RJ, Prywes R. Activation of ATF6 and an ATF6 DNA binding site by the endoplasmic reticulum stress response. J Biol Chem 275: 27013-27020, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 27013-27020
    • Wang, Y.1    Shen, J.2    Arenzana, N.3    Tirasophon, W.4    Kaufman, R.J.5    Prywes, R.6
  • 97
    • 0029892851 scopus 로고    scopus 로고
    • The unfolded protein response pathway in Saccharomyces cerevisiae. Oligomerization and trans-phosphorylation of Ire1p (Ern1p) are required for kinase activation
    • Welihinda AA, Kaufman RJ. The unfolded protein response pathway in Saccharomyces cerevisiae. Oligomerization and trans-phosphorylation of Ire1p (Ern1p) are required for kinase activation. J Biol Chem 271: 18181-18187, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 18181-18187
    • Welihinda, A.A.1    Kaufman, R.J.2
  • 98
    • 23144442469 scopus 로고    scopus 로고
    • A new pharmacology: Drugging stressed folding pathways
    • Wiseman RL, Balch WE. A new pharmacology: drugging stressed folding pathways. Trends Mol Med 11: 347-350, 2005.
    • (2005) Trends Mol Med , vol.11 , pp. 347-350
    • Wiseman, R.L.1    Balch, W.E.2
  • 99
    • 33645156429 scopus 로고    scopus 로고
    • From acute ER stress to physiological roles of the unfolded protein response
    • Wu J, Kaufman RJ. From acute ER stress to physiological roles of the unfolded protein response. Cell Death Differ 13: 374-384, 2006.
    • (2006) Cell Death Differ , vol.13 , pp. 374-384
    • Wu, J.1    Kaufman, R.J.2
  • 100
    • 0033499801 scopus 로고    scopus 로고
    • BCL-2 is phosphorylated and inactivated by an ASK1/Jun Nterminal protein kinase pathway normally activated at G(2)/M
    • Yamamoto K, Ichijo H, Korsmeyer SJ. BCL-2 is phosphorylated and inactivated by an ASK1/Jun Nterminal protein kinase pathway normally activated at G(2)/M. Mol Cell Biol 19: 8469-8478, 1999.
    • (1999) Mol Cell Biol , vol.19 , pp. 8469-8478
    • Yamamoto, K.1    Ichijo, H.2    Korsmeyer, S.J.3
  • 102
    • 33745833084 scopus 로고    scopus 로고
    • The DRiP hypothesis decennial: Support, controversy, refinement and extension
    • Yewdell JW, Nicchitta CV. The DRiP hypothesis decennial: support, controversy, refinement and extension. TRENDS Immunol 27: 368-373, 2006.
    • (2006) TRENDS Immunol , vol.27 , pp. 368-373
    • Yewdell, J.W.1    Nicchitta, C.V.2
  • 103
    • 0035957929 scopus 로고    scopus 로고
    • Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress
    • Yoneda T, Imaizumi K, Oono K, Yui D, Gomi F, Katayama T, Tohyama M. Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress. J Biol Chem 276: 13935-13940, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 13935-13940
    • Yoneda, T.1    Imaizumi, K.2    Oono, K.3    Yui, D.4    Gomi, F.5    Katayama, T.6    Tohyama, M.7
  • 104
    • 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, 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: 33741-33749, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 33741-33749
    • Yoshida, H.1    Haze, K.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 105
    • 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
  • 106
    • 0033815971 scopus 로고    scopus 로고
    • ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response
    • Yoshida H, Okada T, Haze K, Yanagi H, Yura T, Negishi M, Mori K. ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response. Mol Cell Biol 20: 6755-6767, 2000.
    • (2000) Mol Cell Biol , vol.20 , pp. 6755-6767
    • Yoshida, H.1    Okada, T.2    Haze, K.3    Yanagi, H.4    Yura, T.5    Negishi, M.6    Mori, K.7
  • 108
    • 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 DT, Back SH, Kaufman RJ. Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response. Cell 124: 587-599, 2006.
    • (2006) Cell , vol.124 , pp. 587-599
    • Zhang, K.1    Shen, X.2    Wu, J.3    Sakaki, K.4    Saunders, T.5    Rutkowski, D.T.6    Back, S.H.7    Kaufman, R.J.8
  • 109
    • 14944371187 scopus 로고    scopus 로고
    • The unfolded protein response sensor IRE1alpha is required at 2 distinct steps in B cell lymphopoiesis
    • Zhang K, Wong HN, Song B, Miller CN, Scheuner D, Kaufman RJ. The unfolded protein response sensor IRE1alpha is required at 2 distinct steps in B cell lymphopoiesis. J Clin Invest 115: 268-281, 2005.
    • (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
  • 110
    • 0036091476 scopus 로고    scopus 로고
    • The PERK eukaryotic initiation factor 2alpha kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas
    • Zhang P, McGrath B, Li S, Frank A, Zambito F, Reinert J, Gannon M, Ma K, McNaughton K, Cavener DR. The PERK eukaryotic initiation factor 2alpha kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas. Mol Cell Biol 22: 3864-3874, 2002.
    • (2002) Mol Cell Biol , vol.22 , pp. 3864-3874
    • Zhang, P.1    McGrath, B.2    Li, S.3    Frank, A.4    Zambito, F.5    Reinert, J.6    Gannon, M.7    Ma, K.8    McNaughton, K.9    Cavener, D.R.10
  • 111
    • 33751430251 scopus 로고    scopus 로고
    • Zhang W, Feng D, Li Y, Iida K, McGrath B, Cavener DR. PERK EIF2AK3 control of pancreatic b-cell differentiation and proliferation is required for postnatal glucose homeostasis. Cell Metab 4: 1-7, 2006.
    • Zhang W, Feng D, Li Y, Iida K, McGrath B, Cavener DR. PERK EIF2AK3 control of pancreatic b-cell differentiation and proliferation is required for postnatal glucose homeostasis. Cell Metab 4: 1-7, 2006.
  • 112
    • 33745844503 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in health and disease
    • Zhao L, Ackerman SL. Endoplasmic reticulum stress in health and disease. Curr Opin Cell Biol 18: 444-452, 2006.
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 444-452
    • Zhao, L.1    Ackerman, S.L.2
  • 113
    • 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 CY, Back SH, Clark RL, Peisach D, Xu Z, Kaufman RJ. 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: 14343-14348, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 14343-14348
    • Zhou, J.1    Liu, C.Y.2    Back, S.H.3    Clark, R.L.4    Peisach, D.5    Xu, Z.6    Kaufman, R.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.