메뉴 건너뛰기




Volumn 2, Issue 4, 2013, Pages 247-265

ER-stress in Alzheimer’s disease: Turning the scale?

Author keywords

Alzheimer s disease; Apoptosis; APP; Autophagy; Calcium homeostasis; Secretases; Tau; Unfolded protein response

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ACTIVATING TRANSCRIPTION FACTOR 6; ADAM10 ENDOPEPTIDASE; AMYLOID PRECURSOR PROTEIN; BETA SECRETASE 1; GLUCOSE REGULATED PROTEIN 78; GLUCOSE REGULATED PROTEIN 94; INITIATION FACTOR 2ALPHA; TAU PROTEIN; THAPSIGARGIN; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME; TUNICAMYCIN; X BOX BINDING PROTEIN 1;

EID: 84980053538     PISSN: None     EISSN: 2165591X     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (61)

References (155)
  • 1
    • 25444434458 scopus 로고    scopus 로고
    • Diagnosis and management of the cardiac amyloidoses
    • Falk RH. Diagnosis and management of the cardiac amyloidoses. Circulation 2005; 112: 2047-2060.
    • (2005) Circulation , vol.112 , pp. 2047-2060
    • Falk, R.H.1
  • 4
    • 84872559990 scopus 로고    scopus 로고
    • Molecular mechanisms of amyloid oligomers toxicity
    • Kayed R and Lasagna-Reeves CA. Molecular mechanisms of amyloid oligomers toxicity. J Alzheimers Dis 2013; 33 Suppl 1: S67-S78.
    • (2013) J Alzheimers Dis , vol.33 , pp. S67-S78
    • Kayed, R.1    Lasagna-Reeves, C.A.2
  • 5
    • 84869506145 scopus 로고    scopus 로고
    • Evidence for the accumulation of Abeta immunoreactive material in the human brain and in transgenic animal models
    • Cuello AC, Allard S and Ferretti MT. Evidence for the accumulation of Abeta immunoreactive material in the human brain and in transgenic animal models. Life Sci 2012; 91: 1141-1147.
    • (2012) Life Sci , vol.91 , pp. 1141-1147
    • Cuello, A.C.1    Allard, S.2    Ferretti, M.T.3
  • 6
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-beta in Alzheimer's disease
    • Laferla FM, Green KN and Oddo S. Intracellular amyloid-beta in Alzheimer's disease. Nat Rev Neurosci 2007; 8: 499-509.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 499-509
    • Laferla, F.M.1    Green, K.N.2    Oddo, S.3
  • 7
    • 84871922036 scopus 로고    scopus 로고
    • Deciphering the mechanism underlying late-onset Alzheimer disease
    • Krstic D and Knuesel I. Deciphering the mechanism underlying late-onset Alzheimer disease. Nat Rev Neurol 2013; 9: 25-34.
    • (2013) Nat Rev Neurol , vol.9 , pp. 25-34
    • Krstic, D.1    Knuesel, I.2
  • 9
    • 0026545684 scopus 로고
    • An alternative secretase cleavage produces soluble Alzheimer amyloid precursor protein containing a potentially amyloidogenic sequence
    • Anderson JP, Chen Y, Kim KS and Robakis NK. An alternative secretase cleavage produces soluble Alzheimer amyloid precursor protein containing a potentially amyloidogenic sequence. J Neurochem 1992; 59: 2328-2331.
    • (1992) J Neurochem , vol.59 , pp. 2328-2331
    • Anderson, J.P.1    Chen, Y.2    Kim, K.S.3    Robakis, N.K.4
  • 13
    • 0034723418 scopus 로고    scopus 로고
    • Protein kinase C-dependent alpha-secretase competes with beta-secretase for cleavage of amyloid-beta precursor protein in the trans-golgi network
    • Skovronsky DM, Moore DB, Milla ME, Doms RW and Lee VM. Protein kinase C-dependent alpha-secretase competes with beta-secretase for cleavage of amyloid-beta precursor protein in the trans-golgi network. J Biol Chem 2000; 275: 2568-2575.
    • (2000) J Biol Chem , vol.275 , pp. 2568-2575
    • Skovronsky, D.M.1    Moore, D.B.2    Milla, M.E.3    Doms, R.W.4    Lee, V.M.5
  • 14
    • 84655176404 scopus 로고    scopus 로고
    • Functions of Abeta, sAPPalpha and sAPPbeta: Similarities and differences
    • Chasseigneaux S and Allinquant B. Functions of Abeta, sAPPalpha and sAPPbeta: similarities and differences. J Neurochem 2012; 120 Suppl 1: 99-108.
    • (2012) J Neurochem , vol.120 , pp. 99-108
    • Chasseigneaux, S.1    Allinquant, B.2
  • 17
    • 84865623640 scopus 로고    scopus 로고
    • Protein secretion and the endoplasmic reticulum
    • Benham AM. Protein secretion and the endoplasmic reticulum. Cold Spring Harb Perspect Biol 2012; 4: a012872
    • (2012) Cold Spring Harb Perspect Biol , vol.4
    • Benham, A.M.1
  • 18
    • 0025273937 scopus 로고
    • Phospholipid synthesis in a membrane fraction associated with mitochondria
    • Vance JE. Phospholipid synthesis in a membrane fraction associated with mitochondria. J Biol Chem 1990; 265: 7248-7256.
    • (1990) J Biol Chem , vol.265 , pp. 7248-7256
    • Vance, J.E.1
  • 19
    • 84871726622 scopus 로고    scopus 로고
    • Where the endoplasmic reticulum and the mitochondrion tie the knot: The mitochondria-associated membrane (MAM)
    • Raturi A and Simmen T. Where the endoplasmic reticulum and the mitochondrion tie the knot: the mitochondria-associated membrane (MAM). Biochim Biophys Acta 2013; 1833: 213-224.
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 213-224
    • Raturi, A.1    Simmen, T.2
  • 20
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • de Brito OM and Scorrano L. Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 2008; 456: 605-610.
    • (2008) Nature , vol.456 , pp. 605-610
    • de Brito, O.M.1    Scorrano, L.2
  • 21
    • 3142697676 scopus 로고    scopus 로고
    • The gene product of the gp78/AMFR ubiquitin E3 ligase cDNA is selectively recognized by the 3F3A antibody within a subdomain of the endoplasmic reticulum
    • Registre M, Goetz JG, St Pierre P, Pang H, Lagacé M, Bouvier M, Le PU and Nabi IR. The gene product of the gp78/AMFR ubiquitin E3 ligase cDNA is selectively recognized by the 3F3A antibody within a subdomain of the endoplasmic reticulum. Biochem Biophys Res Commun 2004; 320: 1316-1322.
    • (2004) Biochem Biophys Res Commun , vol.320 , pp. 1316-1322
    • Registre, M.1    Goetz, J.G.2    St Pierre, P.3    Pang, H.4    Lagacé, M.5    Bouvier, M.6    Le, P.U.7    Nabi, I.R.8
  • 24
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter P and Ron D. The unfolded protein response: from stress pathway to homeostatic regulation. Science 2011; 334: 1081-1086.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 25
    • 0027332929 scopus 로고
    • Generation of beta A4 from the amyloid protein precursor and fragments thereof
    • Dyrks T, Dyrks E, Mönning U, Urmoneit B, Turner J and Beyreuther K. Generation of beta A4 from the amyloid protein precursor and fragments thereof. FEBS Lett 1993; 335: 89-93.
    • (1993) FEBS Lett , vol.335 , pp. 89-93
    • Dyrks, T.1    Dyrks, E.2    Mönning, U.3    Urmoneit, B.4    Turner, J.5    Beyreuther, K.6
  • 26
    • 0026665014 scopus 로고
    • Evidence for intracellular cleavage of the Alzheimer's amyloid precursor in PC12 cells
    • Sambamurti K, Shioi J, Anderson JP, Pappolla MA and Robakis NK. Evidence for intracellular cleavage of the Alzheimer's amyloid precursor in PC12 cells. J Neurosci Res 1992; 33: 319-329.
    • (1992) J Neurosci Res , vol.33 , pp. 319-329
    • Sambamurti, K.1    Shioi, J.2    Anderson, J.P.3    Pappolla, M.A.4    Robakis, N.K.5
  • 27
    • 84871417031 scopus 로고    scopus 로고
    • Role of mitochondrial homeostasis and dynamics in Alzheimer's disease
    • Selfridge JE, E L, Lu J and Swerdlow RH. Role of mitochondrial homeostasis and dynamics in Alzheimer's disease. Neurobiol Dis 2013; 51: 3-12.
    • (2013) Neurobiol Dis , vol.51 , pp. 3-12
    • Selfridge, J.E.E.L.1    Lu, J.2    Swerdlow, R.H.3
  • 28
    • 79960822419 scopus 로고    scopus 로고
    • Autophagy in aging and Alzheimer's disease: Pathologic or protective?
    • Barnett A and Brewer GJ. Autophagy in aging and Alzheimer's disease: pathologic or protective? J Alzheimers Dis 2011; 25: 385-394.
    • (2011) J Alzheimers Dis , vol.25 , pp. 385-394
    • Barnett, A.1    Brewer, G.J.2
  • 29
    • 79960672046 scopus 로고    scopus 로고
    • Endoplasmic reticulum Ca(2+) handling in excitable cells in health and disease
    • Stutzmann GE and Mattson MP. Endoplasmic reticulum Ca(2+) handling in excitable cells in health and disease. Pharmacol Rev 2011; 63: 700-727.
    • (2011) Pharmacol Rev , vol.63 , pp. 700-727
    • Stutzmann, G.E.1    Mattson, M.P.2
  • 30
    • 84862608221 scopus 로고    scopus 로고
    • Unfolded protein stress in the endoplasmic reticulum and mitochondria: A role in neurodegeneration
    • Bernales S, Soto MM and McCullagh E. Unfolded protein stress in the endoplasmic reticulum and mitochondria: a role in neurodegeneration. Front Aging Neurosci 2012; 4: 5
    • (2012) Front Aging Neurosci , vol.4 , pp. 5
    • Bernales, S.1    Soto, M.M.2    McCullagh, E.3
  • 31
    • 84860219621 scopus 로고    scopus 로고
    • Activation of the unfolded protein response is an early event in Alzheimer's and Parkinson's disease
    • Hoozemans JJ, van Haastert ES, Nijholt DA, Rozemuller AJ and Scheper W. Activation of the unfolded protein response is an early event in Alzheimer's and Parkinson's disease. Neurodegener Dis 2012; 10: 212-215.
    • (2012) Neurodegener Dis , vol.10 , pp. 212-215
    • Hoozemans, J.J.1    van Haastert, E.S.2    Nijholt, D.A.3    Rozemuller, A.J.4    Scheper, W.5
  • 32
    • 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 and Ron D. Cloning of mammalian Ire1 reveals diversity in the ER stress responses. EMBO J 1998; 17: 5708-5717.
    • (1998) EMBO J , vol.17 , pp. 5708-5717
    • Wang, X.Z.1    Harding, H.P.2    Zhang, Y.3    Jolicoeur, E.M.4    Kuroda, M.5    Ron, D.6
  • 33
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • Cox JS, Shamu CE and Walter P. Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 1993; 73: 1197-1206.
    • (1993) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 34
    • 0026710871 scopus 로고
    • IRE1 encodes a putative protein kinase containing a membrane-spanning domain and is required for inositol phototrophy in Saccharomyces cerevisiae
    • Nikawa J and Yamashita S. IRE1 encodes a putative protein kinase containing a membrane-spanning domain and is required for inositol phototrophy in Saccharomyces cerevisiae. Mol Microbiol 1992; 6: 1441-1446.
    • (1992) Mol Microbiol , vol.6 , pp. 1441-1446
    • Nikawa, J.1    Yamashita, S.2
  • 35
    • 0025298202 scopus 로고
    • Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon
    • Meurs E, Chong K, Galabru J, Thomas NS, Kerr IM, Williams BR and Hovanessian AG. Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon. Cell 1990; 62: 379-390.
    • (1990) Cell , vol.62 , pp. 379-390
    • Meurs, E.1    Chong, K.2    Galabru, J.3    Thomas, N.S.4    Kerr, I.M.5    Williams, B.R.6    Hovanessian, A.G.7
  • 36
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • Haze K, Yoshida H, Yanagi H, Yura T and Mori K. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Biol Cell 1999; 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
  • 37
    • 0030850013 scopus 로고    scopus 로고
    • Interaction of ATF6 and serum response factor
    • Zhu C, Johansen FE and Prywes R. Interaction of ATF6 and serum response factor. Mol Cell Biol 1997; 17: 4957-4966.
    • (1997) Mol Cell Biol , vol.17 , pp. 4957-4966
    • Zhu, C.1    Johansen, F.E.2    Prywes, R.3
  • 38
    • 0024817131 scopus 로고
    • Transcription factor ATF cDNA clones: An extensive family of leucine zipper proteins able to selectively form DNA-binding heterodimers
    • Hai TW, Liu F, Coukos WJ and Green MR. Transcription factor ATF cDNA clones: an extensive family of leucine zipper proteins able to selectively form DNA-binding heterodimers. Genes Dev 1989; 3: 2083-2090.
    • (1989) Genes Dev , vol.3 , pp. 2083-2090
    • Hai, T.W.1    Liu, F.2    Coukos, W.J.3    Green, M.R.4
  • 39
    • 84880641508 scopus 로고    scopus 로고
    • Evolution of the unfolded protein response
    • Hollien J. Evolution of the unfolded protein response. Biochim Biophys Acta 2013; 1833: 2458-2463.
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 2458-2463
    • Hollien, J.1
  • 40
    • 33846223428 scopus 로고    scopus 로고
    • Role of disulfide bridges formed in the luminal domain of ATF6 in sensing endoplasmic reticulum stress
    • Nadanaka S, Okada T, Yoshida H and Mori K. Role of disulfide bridges formed in the luminal domain of ATF6 in sensing endoplasmic reticulum stress. Mol Cell Biol 2007; 27: 1027-1043.
    • (2007) Mol Cell Biol , vol.27 , pp. 1027-1043
    • Nadanaka, S.1    Okada, T.2    Yoshida, H.3    Mori, K.4
  • 42
    • 44449101173 scopus 로고    scopus 로고
    • ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum
    • Adachi Y, Yamamoto K, Okada T, Yoshida H, Harada A and Mori K. ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum. Cell Struct Funct 2008; 33: 75-89.
    • (2008) Cell Struct Funct , vol.33 , pp. 75-89
    • Adachi, Y.1    Yamamoto, K.2    Okada, T.3    Yoshida, H.4    Harada, A.5    Mori, K.6
  • 43
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding HP, Zhang Y and Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 1999; 397: 271-274.
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 44
    • 30944458057 scopus 로고    scopus 로고
    • Activation-dependent substrate recruitment by the eukaryotic translation initiation factor 2 kinase PERK
    • Marciniak SJ, Garcia-Bonilla L, Hu J, Harding HP and Ron D. Activation-dependent substrate recruitment by the eukaryotic translation initiation factor 2 kinase PERK. J Cell Biol 2006; 172: 201-209.
    • (2006) J Cell Biol , vol.172 , pp. 201-209
    • Marciniak, S.J.1    Garcia-Bonilla, L.2    Hu, J.3    Harding, H.P.4    Ron, D.5
  • 45
    • 0034163483 scopus 로고    scopus 로고
    • Pancreatic eukaryotic initiation factor-2alpha kinase (PEK) homologues in humans, Drosophila melanogaster and Caenorhabditis elegans that mediate translational control in response to endoplasmic reticulum stress
    • Sood R, Porter AC, Ma K, Quilliam LA and Wek RC. Pancreatic eukaryotic initiation factor-2alpha kinase (PEK) homologues in humans, Drosophila melanogaster and Caenorhabditis elegans that mediate translational control in response to endoplasmic reticulum stress. Biochem J 2000; 346: 281-293.
    • (2000) Biochem J , vol.346 , pp. 281-293
    • Sood, R.1    Porter, A.C.2    Ma, K.3    Quilliam, L.A.4    Wek, R.C.5
  • 46
    • 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 and Ron D. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol Cell 2000; 6: 1099-1108.
    • (2000) Mol Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6    Ron, D.7
  • 47
    • 0344784185 scopus 로고
    • Inhibition of protein synthesis initiation by oxidized glutathione: Activation of a protein kinase that phosphorylates the alpha subunit of eukaryotic initiation factor 2
    • Ernst V, Levin DH and London IM. Inhibition of protein synthesis initiation by oxidized glutathione: activation of a protein kinase that phosphorylates the alpha subunit of eukaryotic initiation factor 2. Proc Natl Acad Sci U S A 1978; 75: 4110-4114.
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 4110-4114
    • Ernst, V.1    Levin, D.H.2    London, I.M.3
  • 48
    • 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 and Hendershot LM. Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response. J Mol Biol 2002; 318: 1351-1365.
    • (2002) J Mol Biol , vol.318 , pp. 1351-1365
    • Ma, Y.1    Brewer, J.W.2    Diehl, J.A.3    Hendershot, L.M.4
  • 49
    • 65449141379 scopus 로고    scopus 로고
    • An upstream open reading frame regulates translation of GADD34 during cellular stresses that induce eIF2alpha phosphorylation
    • Lee YY, Cevallos RC and Jan E. An upstream open reading frame regulates translation of GADD34 during cellular stresses that induce eIF2alpha phosphorylation. J Biol Chem 2009; 284: 6661-6673.
    • (2009) J Biol Chem , vol.284 , pp. 6661-6673
    • Lee, Y.Y.1    Cevallos, R.C.2    Jan, E.3
  • 50
    • 79952264011 scopus 로고    scopus 로고
    • Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
    • Tabas I and Ron D. Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress. Nat Cell Biol 2011; 13: 184-190.
    • (2011) Nat Cell Biol , vol.13 , pp. 184-190
    • Tabas, I.1    Ron, D.2
  • 51
    • 0035947778 scopus 로고    scopus 로고
    • Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha
    • Novoa I, Zeng H, Harding HP and Ron D. Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha. J Cell Biol 2001; 153: 1011-1022.
    • (2001) J Cell Biol , vol.153 , pp. 1011-1022
    • Novoa, I.1    Zeng, H.2    Harding, H.P.3    Ron, D.4
  • 52
    • 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, Schröder M and Kaufman RJ. Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum. J Biol Chem 2000; 275: 24881-24885.
    • (2000) J Biol Chem , vol.275 , pp. 24881-24885
    • Liu, C.Y.1    Schröder, M.2    Kaufman, R.J.3
  • 53
    • 0034312290 scopus 로고    scopus 로고
    • The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein response
    • Tirasophon W, Lee K, Callaghan B, Welihinda A and Kaufman RJ. The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein response. Genes Dev 2000; 14: 2725-2736.
    • (2000) Genes Dev , vol.14 , pp. 2725-2736
    • Tirasophon, W.1    Lee, K.2    Callaghan, B.3    Welihinda, A.4    Kaufman, R.J.5
  • 55
    • 84878233437 scopus 로고    scopus 로고
    • An ire1-phk1 chimera reveals a dispensable role of autokinase activity in endoplasmic reticulum stress response
    • Mannan MA, Shadrick WR, Biener G, Shin BS, Anshu A, Raicu V, Frick DN and Dey M. An ire1-phk1 chimera reveals a dispensable role of autokinase activity in endoplasmic reticulum stress response. J Mol Biol 2013; 425: 2083-2099.
    • (2013) J Mol Biol , vol.425 , pp. 2083-2099
    • Mannan, M.A.1    Shadrick, W.R.2    Biener, G.3    Shin, B.S.4    Anshu, A.5    Raicu, V.6    Frick, D.N.7    Dey, M.8
  • 57
    • 33846217495 scopus 로고    scopus 로고
    • XBP1 is critical to protect cells from endoplasmic reticulum stress: Evidence from Site-2 protease-deficient Chinese hamster ovary cells
    • Yoshida H, Nadanaka S, Sato R and Mori K. XBP1 is critical to protect cells from endoplasmic reticulum stress: evidence from Site-2 protease-deficient Chinese hamster ovary cells. Cell Struct Funct 2006; 31: 117-125.
    • (2006) Cell Struct Funct , vol.31 , pp. 117-125
    • Yoshida, H.1    Nadanaka, S.2    Sato, R.3    Mori, K.4
  • 58
    • 53549098817 scopus 로고    scopus 로고
    • Human HRD1 promoter carries a functional unfolded protein response element to which XBP1 but not ATF6 directly binds
    • Yamamoto K, Suzuki N, Wada T, Okada T, Yoshida H, Kaufman RJ and Mori K. Human HRD1 promoter carries a functional unfolded protein response element to which XBP1 but not ATF6 directly binds. J Biochem 2008; 144: 477-486.
    • (2008) J Biochem , vol.144 , pp. 477-486
    • Yamamoto, K.1    Suzuki, N.2    Wada, T.3    Okada, T.4    Yoshida, H.5    Kaufman, R.J.6    Mori, K.7
  • 59
    • 84867063735 scopus 로고    scopus 로고
    • IRE1alpha-XBP1s induces PDI expression to increase MTP activity for hepatic VLDL assembly and lipid homeostasis
    • Wang S, Chen Z, Lam V, Han J, Hassler J, Finck BN, Davidson NO and Kaufman RJ. IRE1alpha-XBP1s induces PDI expression to increase MTP activity for hepatic VLDL assembly and lipid homeostasis. Cell Metab 2012; 16: 473-486.
    • (2012) Cell Metab , vol.16 , pp. 473-486
    • Wang, S.1    Chen, Z.2    Lam, V.3    Han, J.4    Hassler, J.5    Finck, B.N.6    Davidson, N.O.7    Kaufman, R.J.8
  • 60
    • 18844440910 scopus 로고    scopus 로고
    • XBP1 activates the transcription of its target genes via an ACGT core sequence under ER stress
    • Kanemoto S, Kondo S, Ogata M, Murakami T, Urano F and Imaizumi K. XBP1 activates the transcription of its target genes via an ACGT core sequence under ER stress. Biochem Biophys Res Commun 2005; 331: 1146-1153.
    • (2005) Biochem Biophys Res Commun , vol.331 , pp. 1146-1153
    • Kanemoto, S.1    Kondo, S.2    Ogata, M.3    Murakami, T.4    Urano, F.5    Imaizumi, K.6
  • 61
    • 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 and Ron D. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 2000; 287: 664-666.
    • (2000) Science , vol.287 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6    Ron, D.7
  • 63
    • 0037385313 scopus 로고    scopus 로고
    • Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-1
    • Iwakoshi NN, Lee AH, Vallabhajosyula P, Otipoby KL, Rajewsky K and Glimcher LH. Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-1. Nat Immunol 2003; 4: 321-329.
    • (2003) Nat Immunol , vol.4 , pp. 321-329
    • Iwakoshi, N.N.1    Lee, A.H.2    Vallabhajosyula, P.3    Otipoby, K.L.4    Rajewsky, K.5    Glimcher, L.H.6
  • 65
    • 81755184374 scopus 로고    scopus 로고
    • The eIF2 kinase PERK and the integrated stress response facilitate activation of ATF6 during endoplasmic reticulum stress
    • Teske BF, Wek SA, Bunpo P, Cundiff JK, McClintick JN, Anthony TG and Wek RC. The eIF2 kinase PERK and the integrated stress response facilitate activation of ATF6 during endoplasmic reticulum stress. Mol Biol Cell 2011; 22: 4390-4405.
    • (2011) Mol Biol Cell , vol.22 , pp. 4390-4405
    • Teske, B.F.1    Wek, S.A.2    Bunpo, P.3    Cundiff, J.K.4    McClintick, J.N.5    Anthony, T.G.6    Wek, R.C.7
  • 66
    • 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 and Prywes R. Activation of ATF6 and an ATF6 DNA binding site by the endoplasmic reticulum stress response. J Biol Chem 2000; 275: 27013-27020.
    • (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
  • 67
    • 9144228073 scopus 로고    scopus 로고
    • Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE and ERSE-II
    • Yamamoto K, Yoshida H, Kokame K, Kaufman RJ and Mori K. Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE and ERSE-II. J Biochem 2004; 136: 343-350.
    • (2004) J Biochem , vol.136 , pp. 343-350
    • Yamamoto, K.1    Yoshida, H.2    Kokame, K.3    Kaufman, R.J.4    Mori, K.5
  • 68
    • 0033559493 scopus 로고    scopus 로고
    • The mammalian endoplasmic reticulum stress response element consists of an evolutionarily conserved tripartite structure and interacts with a novel stress-inducible complex
    • Roy B and Lee AS. The mammalian endoplasmic reticulum stress response element consists of an evolutionarily conserved tripartite structure and interacts with a novel stress-inducible complex. Nucleic Acids Res 1999; 27: 1437-1443.
    • (1999) Nucleic Acids Res , vol.27 , pp. 1437-1443
    • Roy, B.1    Lee, A.S.2
  • 69
    • 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 and Miyata T. Identification of ERSE-II, a new cis-acting element responsible for the ATF6-dependent mammalian unfolded protein response. J Biol Chem 2001; 276: 9199-9205.
    • (2001) J Biol Chem , vol.276 , pp. 9199-9205
    • Kokame, K.1    Kato, H.2    Miyata, T.3
  • 70
    • 0035141230 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced formation of transcription factor complex ERSF including NF-Y (CBF) and activating transcription factors 6alpha and 6beta that activates the mammalian unfolded protein response
    • Yoshida H, Okada T, Haze K, Yanagi H, Yura T, Negishi M and Mori K. Endoplasmic reticulum stress-induced formation of transcription factor complex ERSF including NF-Y (CBF) and activating transcription factors 6alpha and 6beta that activates the mammalian unfolded protein response. Mol Cell Biol 2001; 21: 1239-1248.
    • (2001) Mol Cell Biol , vol.21 , pp. 1239-1248
    • Yoshida, H.1    Okada, T.2    Haze, K.3    Yanagi, H.4    Yura, T.5    Negishi, M.6    Mori, K.7
  • 71
    • 84880075534 scopus 로고    scopus 로고
    • Identification of a Novel Endoplasmic Reticulum Stress Response Element Regulated by XBP1
    • Misiewicz M, Déry MA, Foveau B, Jodoin J, Ruths D and le Blanc AC. Identification of a Novel Endoplasmic Reticulum Stress Response Element Regulated by XBP1. J Biol Chem 2013; 288: 20378-20391.
    • (2013) J Biol Chem , vol.288 , pp. 20378-20391
    • Misiewicz, M.1    Déry, M.A.2    Foveau, B.3    Jodoin, J.4    Ruths, D.5    Le Blanc, A.C.6
  • 72
    • 0032509216 scopus 로고    scopus 로고
    • Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors
    • Yoshida H, Haze K, Yanagi H, Yura T and Mori K. Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors. J Biol Chem 1998; 273: 33741-33749.
    • (1998) J Biol Chem , vol.273 , pp. 33741-33749
    • Yoshida, H.1    Haze, K.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 74
    • 0026788147 scopus 로고
    • Phosphorylation of eukaryotic initiation factor (eIF) 2 alpha and inhibition of eIF-2B in GH3 pituitary cells by perturbants of early protein processing that induce GRP78
    • Prostko CR, Brostrom MA, Malara EM and Brostrom CO. Phosphorylation of eukaryotic initiation factor (eIF) 2 alpha and inhibition of eIF-2B in GH3 pituitary cells by perturbants of early protein processing that induce GRP78. J Biol Chem 1992; 267: 16751-16754.
    • (1992) J Biol Chem , vol.267 , pp. 16751-16754
    • Prostko, C.R.1    Brostrom, M.A.2    Malara, E.M.3    Brostrom, C.O.4
  • 75
    • 84878784750 scopus 로고    scopus 로고
    • Comparative analysis of the expression patterns of UPR-target genes caused by UPR-inducing compounds
    • Shinjo S, Mizotani Y, Tashiro E and Imoto M. Comparative analysis of the expression patterns of UPR-target genes caused by UPR-inducing compounds. Biosci Biotechnol Biochem 2013; 77: 729-735.
    • (2013) Biosci Biotechnol Biochem , vol.77 , pp. 729-735
    • Shinjo, S.1    Mizotani, Y.2    Tashiro, E.3    Imoto, M.4
  • 77
    • 0033598996 scopus 로고    scopus 로고
    • A role for presenilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response
    • Niwa M, Sidrauski C, Kaufman RJ and Walter P. A role for presenilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response. Cell 1999; 99: 691-702.
    • (1999) Cell , vol.99 , pp. 691-702
    • Niwa, M.1    Sidrauski, C.2    Kaufman, R.J.3    Walter, P.4
  • 78
    • 0034871249 scopus 로고    scopus 로고
    • Endoproteolysis of the ER stress transducer ATF6 in the presence of functionally inactive presenilins
    • Steiner H, Winkler E, Shearman MS, Prywes R and Haass C. Endoproteolysis of the ER stress transducer ATF6 in the presence of functionally inactive presenilins. Neurobiol Dis 2001; 8: 717-722.
    • (2001) Neurobiol Dis , vol.8 , pp. 717-722
    • Steiner, H.1    Winkler, E.2    Shearman, M.S.3    Prywes, R.4    Haass, C.5
  • 79
    • 79959636033 scopus 로고    scopus 로고
    • The many substrates of presenilin/gamma-secretase
    • Haapasalo A and Kovacs DM. The many substrates of presenilin/gamma-secretase. J Alzheimers Dis 2011; 25: 3-28.
    • (2011) J Alzheimers Dis , vol.25 , pp. 3-28
    • Haapasalo, A.1    Kovacs, D.M.2
  • 81
    • 1542784578 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle
    • Vattemi G, Engel WK, McFerrin J and Askanas V. Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle. Am J Pathol 2004; 164: 1-7.
    • (2004) Am J Pathol , vol.164 , pp. 1-7
    • Vattemi, G.1    Engel, W.K.2    McFerrin, J.3    Askanas, V.4
  • 83
    • 10644290831 scopus 로고    scopus 로고
    • Intracellularly generated amyloid-beta peptide counteracts the antiapoptotic function of its precursor protein and primes proapoptotic pathways for activation by other insults in neuroblastoma cells
    • Esposito L, Gan L, Yu GQ, Essrich C and Mucke L. Intracellularly generated amyloid-beta peptide counteracts the antiapoptotic function of its precursor protein and primes proapoptotic pathways for activation by other insults in neuroblastoma cells. J Neurochem 2004; 91: 1260-1274.
    • (2004) J Neurochem , vol.91 , pp. 1260-1274
    • Esposito, L.1    Gan, L.2    Yu, G.Q.3    Essrich, C.4    Mucke, L.5
  • 84
    • 84886388885 scopus 로고    scopus 로고
    • Treadmill exercise represses neuronal cell death and inflammation during Abeta-induced ER stress by regulating unfolded protein response in aged presenilin 2 mutant mice
    • Kang EB, Kwon IS, Koo JH, Kim EJ, Kim CH, Lee J, Yang CH, Lee YI, Cho IH and Cho JY. Treadmill exercise represses neuronal cell death and inflammation during Abeta-induced ER stress by regulating unfolded protein response in aged presenilin 2 mutant mice. Apoptosis 2013; 18: 1332-1347.
    • (2013) Apoptosis , vol.18 , pp. 1332-1347
    • Kang, E.B.1    Kwon, I.S.2    Koo, J.H.3    Kim, E.J.4    Kim, C.H.5    Lee, J.6    Yang, C.H.7    Lee, Y.I.8    Cho, I.H.9    Cho, J.Y.10
  • 85
    • 84874612520 scopus 로고    scopus 로고
    • Unfolded protein response and activated degradative pathways regulation in GNE myopathy
    • Li H, Chen Q, Liu F, Zhang X, Li W, Liu S, Zhao Y, Gong Y and Yan C. Unfolded protein response and activated degradative pathways regulation in GNE myopathy. PLoS One 2013; 8: e58116.
    • (2013) PLoS One , vol.8
    • Li, H.1    Chen, Q.2    Liu, F.3    Zhang, X.4    Li, W.5    Liu, S.6    Zhao, Y.7    Gong, Y.8    Yan, C.9
  • 86
    • 84870349573 scopus 로고    scopus 로고
    • Inhibition of mitochondrial cytochrome c oxidase potentiates Abeta-induced ER stress and cell death in cortical neurons
    • Costa RO, Ferreiro E, Oliveira CR and Pereira CM. Inhibition of mitochondrial cytochrome c oxidase potentiates Abeta-induced ER stress and cell death in cortical neurons. Mol Cell Neurosci 2013; 52: 1-8.
    • (2013) Mol Cell Neurosci , vol.52 , pp. 1-8
    • Costa, R.O.1    Ferreiro, E.2    Oliveira, C.R.3    Pereira, C.M.4
  • 87
    • 77953485026 scopus 로고    scopus 로고
    • Induction of the unfolded protein response and cell death pathway in Alzheimer's disease, but not in aged Tg2576 mice
    • Lee JH, Won SM, Suh J, Son SJ, Moon GJ, Park UJ and Gwag BJ. Induction of the unfolded protein response and cell death pathway in Alzheimer's disease, but not in aged Tg2576 mice. Exp Mol Med 2010; 42: 386-394.
    • (2010) Exp Mol Med , vol.42 , pp. 386-394
    • Lee, J.H.1    Won, S.M.2    Suh, J.3    Son, S.J.4    Moon, G.J.5    Park, U.J.6    Gwag, B.J.7
  • 88
    • 33745019916 scopus 로고    scopus 로고
    • Beta-amyloid peptides induces neuronal apoptosis via a mechanism independent of unfolded protein responses
    • Yu MS, Suen KC, Kwok NS, So KF, Hugon J and Chang RC. Beta-amyloid peptides induces neuronal apoptosis via a mechanism independent of unfolded protein responses. Apoptosis 2006; 11: 687-700.
    • (2006) Apoptosis , vol.11 , pp. 687-700
    • Yu, M.S.1    Suen, K.C.2    Kwok, N.S.3    So, K.F.4    Hugon, J.5    Chang, R.C.6
  • 89
    • 35848951621 scopus 로고    scopus 로고
    • Abeta 1-42 induces mild endoplasmic reticulum stress in an aggregation state-dependent manner
    • Chafekar SM, Hoozemans JJ, Zwart R, Baas F and Scheper W. Abeta 1-42 induces mild endoplasmic reticulum stress in an aggregation state-dependent manner. Antioxid Redox Signal 2007; 9: 2245-2254.
    • (2007) Antioxid Redox Signal , vol.9 , pp. 2245-2254
    • Chafekar, S.M.1    Hoozemans, J.J.2    Zwart, R.3    Baas, F.4    Scheper, W.5
  • 93
    • 84655166492 scopus 로고    scopus 로고
    • The physiology of the beta-amyloid precursor protein intracellular domain AICD
    • Pardossi-Piquard R and Checler F. The physiology of the beta-amyloid precursor protein intracellular domain AICD. J Neurochem 2012; 120 Suppl 1: 109-124.
    • (2012) J Neurochem , vol.120 , pp. 109-124
    • Pardossi-Piquard, R.1    Checler, F.2
  • 94
    • 65549138530 scopus 로고    scopus 로고
    • Amyloid precursor protein promotes endoplasmic reticulum stress-induced cell death via C/EBP homologous protein-mediated pathway
    • Takahashi K, Niidome T, Akaike A, Kihara T and Sugimoto H. Amyloid precursor protein promotes endoplasmic reticulum stress-induced cell death via C/EBP homologous protein-mediated pathway. J Neurochem 2009; 109: 1324-1337.
    • (2009) J Neurochem , vol.109 , pp. 1324-1337
    • Takahashi, K.1    Niidome, T.2    Akaike, A.3    Kihara, T.4    Sugimoto, H.5
  • 96
    • 0032524319 scopus 로고    scopus 로고
    • Secreted beta-amyloid precursor protein counteracts the proapoptotic action of mutant presenilin-1 by activation of NF-kappaB and stabilization of calcium homeostasis
    • Guo Q, Robinson N and Mattson MP. Secreted beta-amyloid precursor protein counteracts the proapoptotic action of mutant presenilin-1 by activation of NF-kappaB and stabilization of calcium homeostasis. J Biol Chem 1998; 273: 12341-12351.
    • (1998) J Biol Chem , vol.273 , pp. 12341-12351
    • Guo, Q.1    Robinson, N.2    Mattson, M.P.3
  • 100
    • 84858000638 scopus 로고    scopus 로고
    • The unfolded protein response is associated with early tau pathology in the hippocampus of tauopathies
    • Nijholt DA, van Haastert ES, Rozemuller AJ, Scheper W and Hoozemans JJ. The unfolded protein response is associated with early tau pathology in the hippocampus of tauopathies. J Pathol 2012; 226: 693-702.
    • (2012) J Pathol , vol.226 , pp. 693-702
    • Nijholt, D.A.1    van Haastert, E.S.2    Rozemuller, A.J.3    Scheper, W.4    Hoozemans, J.J.5
  • 101
    • 84863242250 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induces tau pathology and forms a vicious cycle: Implication in Alzheimer's disease pathogenesis
    • Ho YS, Yang X, Lau JC, Hung CH, Wuwongse S, Zhang Q, Wang J, Baum L, So KF and Chang RC. Endoplasmic reticulum stress induces tau pathology and forms a vicious cycle: implication in Alzheimer's disease pathogenesis. J Alzheimers Dis 2012; 28: 839-854.
    • (2012) J Alzheimers Dis , vol.28 , pp. 839-854
    • Ho, Y.S.1    Yang, X.2    Lau, J.C.3    Hung, C.H.4    Wuwongse, S.5    Zhang, Q.6    Wang, J.7    Baum, L.8    So, K.F.9    Chang, R.C.10
  • 102
    • 77953516041 scopus 로고    scopus 로고
    • Transgenic mouse and cell culture models demonstrate a lack of mechanistic connection between endoplasmic reticulum stress and tau dysfunction
    • Spatara ML and Robinson AS. Transgenic mouse and cell culture models demonstrate a lack of mechanistic connection between endoplasmic reticulum stress and tau dysfunction. J Neurosci Res 2010; 88: 1951-1961.
    • (2010) J Neurosci Res , vol.88 , pp. 1951-1961
    • Spatara, M.L.1    Robinson, A.S.2
  • 104
    • 78650469377 scopus 로고    scopus 로고
    • LiCl attenuates thapsigargin-induced tau hyperphosphorylation by inhibiting GSK-3beta in vivo and in vitro
    • Fu ZQ, Yang Y, Song J, Jiang Q, Lin ZC, Wang Q, Zhu LQ, Wang JZ and Tian Q. LiCl attenuates thapsigargin-induced tau hyperphosphorylation by inhibiting GSK-3beta in vivo and in vitro. J Alzheimers Dis 2010; 21: 1107-1117.
    • (2010) J Alzheimers Dis , vol.21 , pp. 1107-1117
    • Fu, Z.Q.1    Yang, Y.2    Song, J.3    Jiang, Q.4    Lin, Z.C.5    Wang, Q.6    Zhu, L.Q.7    Wang, J.Z.8    Tian, Q.9
  • 106
    • 48249157930 scopus 로고    scopus 로고
    • ER stress is involved in Abeta-induced GSK-3beta activation and tau phosphorylation
    • Resende R, Ferreiro E, Pereira C and Oliveira CR. ER stress is involved in Abeta-induced GSK-3beta activation and tau phosphorylation. J Neurosci Res 2008; 86: 2091-2099.
    • (2008) J Neurosci Res , vol.86 , pp. 2091-2099
    • Resende, R.1    Ferreiro, E.2    Pereira, C.3    Oliveira, C.R.4
  • 108
    • 77951499020 scopus 로고    scopus 로고
    • Increased BACE1 mRNA and noncoding BACE1-antisense transcript in sporadic inclusion-body myositis muscle fibers--possibly caused by endoplasmic reticulum stress
    • Nogalska A, Engel WK and Askanas V. Increased BACE1 mRNA and noncoding BACE1-antisense transcript in sporadic inclusion-body myositis muscle fibers--possibly caused by endoplasmic reticulum stress. Neurosci Lett 2010; 474: 140-143.
    • (2010) Neurosci Lett , vol.474 , pp. 140-143
    • Nogalska, A.1    Engel, W.K.2    Askanas, V.3
  • 112
    • 4344681535 scopus 로고    scopus 로고
    • Expression of the Alzheimer protease BACE1 is suppressed via its 5'-untranslated region
    • Lammich S, Schöbel S, Zimmer AK, Lichtenthaler SF and Haass C. Expression of the Alzheimer protease BACE1 is suppressed via its 5'-untranslated region. EMBO Rep 2004; 5: 620-625.
    • (2004) EMBO Rep , vol.5 , pp. 620-625
    • Lammich, S.1    Schöbel, S.2    Zimmer, A.K.3    Lichtenthaler, S.F.4    Haass, C.5
  • 118
    • 79955470772 scopus 로고    scopus 로고
    • The "A Disintegrin And Metalloproteases" ADAM10 and ADAM17: Novel drug targets with therapeutic potential?
    • Saftig P and Reiss K. The "A Disintegrin And Metalloproteases" ADAM10 and ADAM17: novel drug targets with therapeutic potential? Eur J Cell Biol 2011; 90: 527-535.
    • (2011) Eur J Cell Biol , vol.90 , pp. 527-535
    • Saftig, P.1    Reiss, K.2
  • 119
    • 84864865373 scopus 로고    scopus 로고
    • The unfolded protein response controls induction and activation of ADAM17/TACE by severe hypoxia and ER stress
    • Rzymski T, Petry A, Kračun D, Riess F, Pike L, Harris AL and Görlach A. The unfolded protein response controls induction and activation of ADAM17/TACE by severe hypoxia and ER stress. Oncogene 2012; 31: 3621-3634.
    • (2012) Oncogene , vol.31 , pp. 3621-3634
    • Rzymski, T.1    Petry, A.2    Kračun, D.3    Riess, F.4    Pike, L.5    Harris, A.L.6    Görlach, A.7
  • 120
    • 84907447652 scopus 로고    scopus 로고
    • Unfolded protein response signaling by transcription factor XBP-1 regulates ADAM10 and is affected in Alzheimer's disease
    • [Epub ahead of print]
    • Reinhardt S, Schuck F, Grösgen S, Riemenschneider M, Hartmann T, Postina R, Grimm M and Endres K. Unfolded protein response signaling by transcription factor XBP-1 regulates ADAM10 and is affected in Alzheimer's disease. FASEB J 2013; [Epub ahead of print].
    • (2013) FASEB J
    • Reinhardt, S.1    Schuck, F.2    Grösgen, S.3    Riemenschneider, M.4    Hartmann, T.5    Postina, R.6    Grimm, M.7    Endres, K.8
  • 123
    • 84864534874 scopus 로고    scopus 로고
    • ADAM10 regulates transcription factor expression required for plasma cell function
    • Chaimowitz NS, Kang DJ, Dean LM and Conrad DH. ADAM10 regulates transcription factor expression required for plasma cell function. PLoS One 2012; 7: e42694.
    • (2012) PLoS One , vol.7
    • Chaimowitz, N.S.1    Kang, D.J.2    Dean, L.M.3    Conrad, D.H.4
  • 128
    • 33749521100 scopus 로고    scopus 로고
    • Intraneuronal beta-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: Potential factors in amyloid plaque formation
    • Oakley H, Cole SL, Logan S, Maus E, Shao P, Craft J, Guillozet-Bongaarts A, Ohno M, Disterhoft J, van Eldik L, Berry R and Vassar R. Intraneuronal beta-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: potential factors in amyloid plaque formation. J Neurosci 2006; 26: 10129-10140.
    • (2006) J Neurosci , vol.26 , pp. 10129-10140
    • Oakley, H.1    Cole, S.L.2    Logan, S.3    Maus, E.4    Shao, P.5    Craft, J.6    Guillozet-Bongaarts, A.7    Ohno, M.8    Disterhoft, J.9    van Eldik, L.10    Berry, R.11    Vassar, R.12
  • 132
    • 84881076550 scopus 로고    scopus 로고
    • CHOP induces activating transcription factor 5 (ATF5) to trigger apoptosis in response to perturbations in protein homeostasis
    • Teske BF, Fusakio ME, Zhou D, Shan J, McClintick JN, Kilberg MS and Wek RC. CHOP induces activating transcription factor 5 (ATF5) to trigger apoptosis in response to perturbations in protein homeostasis. Mol Biol Cell 2013; 24: 2477-2490.
    • (2013) Mol Biol Cell , vol.24 , pp. 2477-2490
    • Teske, B.F.1    Fusakio, M.E.2    Zhou, D.3    Shan, J.4    McClintick, J.N.5    Kilberg, M.S.6    Wek, R.C.7
  • 134
    • 34547464672 scopus 로고    scopus 로고
    • Genetically augmenting tau levels does not modulate the onset or progression of Abeta pathology in transgenic mice
    • Oddo S, Caccamo A, Cheng D, Jouleh B, Torp R and Laferla FM. Genetically augmenting tau levels does not modulate the onset or progression of Abeta pathology in transgenic mice. J Neurochem 2007; 102: 1053-1063.
    • (2007) J Neurochem , vol.102 , pp. 1053-1063
    • Oddo, S.1    Caccamo, A.2    Cheng, D.3    Jouleh, B.4    Torp, R.5    Laferla, F.M.6
  • 135
    • 79955601720 scopus 로고    scopus 로고
    • Intraneuronal amyloid beta oligomers cause cell death via endoplasmic reticulum stress, endosomal/lysosomal leakage, and mitochondrial dysfunction in vivo
    • Umeda T, Tomiyama T, Sakama N, Tanaka S, Lambert MP, Klein WL and Mori H. Intraneuronal amyloid beta oligomers cause cell death via endoplasmic reticulum stress, endosomal/lysosomal leakage, and mitochondrial dysfunction in vivo. J Neurosci Res 2011; 89: 1031-1042.
    • (2011) J Neurosci Res , vol.89 , pp. 1031-1042
    • Umeda, T.1    Tomiyama, T.2    Sakama, N.3    Tanaka, S.4    Lambert, M.P.5    Klein, W.L.6    Mori, H.7
  • 137
    • 84862892661 scopus 로고    scopus 로고
    • Dysfunctional pro-ceramide, ER stress and insulin/IGF signaling networks with progression of Alzheimer's disease
    • de La Monte SM, Re E, Longato L and Tong M. Dysfunctional pro-ceramide, ER stress and insulin/IGF signaling networks with progression of Alzheimer's disease. J Alzheimers Dis 2012; 30 Suppl 2: S217-S229.
    • (2012) J Alzheimers Dis , vol.30 , pp. S217-S229
    • de La Monte, S.M.1    Re, E.2    Longato, L.3    Tong, M.4
  • 139
    • 77955653927 scopus 로고    scopus 로고
    • Protein disulfide isomerase-immunopositive inclusions in patients with Alzheimer disease
    • Honjo Y, Ito H, Horibe T, Takahashi R and Kawakami K. Protein disulfide isomerase-immunopositive inclusions in patients with Alzheimer disease. Brain Res 2010; 1349: 90-96.
    • (2010) Brain Res , vol.1349 , pp. 90-96
    • Honjo, Y.1    Ito, H.2    Horibe, T.3    Takahashi, R.4    Kawakami, K.5
  • 140
    • 77949764687 scopus 로고    scopus 로고
    • Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-beta generation
    • Kaneko M, Koike H, Saito R, Kitamura Y, Okuma Y and Nomura Y. Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-beta generation. J Neurosci 2010; 30: 3924-3932.
    • (2010) J Neurosci , vol.30 , pp. 3924-3932
    • Kaneko, M.1    Koike, H.2    Saito, R.3    Kitamura, Y.4    Okuma, Y.5    Nomura, Y.6
  • 141
    • 84885456003 scopus 로고    scopus 로고
    • The ire-1 ER stress-response pathway is required for normal secretory-protein metabolism in C. elegans
    • Safra M, Ben-Hamo S, Kenyon C and Henis-Korenblit S. The ire-1 ER stress-response pathway is required for normal secretory-protein metabolism in C. elegans. J Cell Sci 2013; 126: 4136-4146.
    • (2013) J Cell Sci , vol.126 , pp. 4136-4146
    • Safra, M.1    Ben-Hamo, S.2    Kenyon, C.3    Henis-Korenblit, S.4
  • 142
    • 84879343155 scopus 로고    scopus 로고
    • XBP-1 is a cell-nonautonomous regulator of stress resistance and longevity
    • Taylor RC and Dillin A. XBP-1 is a cell-nonautonomous regulator of stress resistance and longevity. Cell 2013; 153: 1435-1447.
    • (2013) Cell , vol.153 , pp. 1435-1447
    • Taylor, R.C.1    Dillin, A.2
  • 143
    • 84886581781 scopus 로고    scopus 로고
    • Targeting the unfolded protein response in neurodegeneration: A new approach to therapy
    • Halliday M and Mallucci GR. Targeting the unfolded protein response in neurodegeneration: A new approach to therapy. Neuropharmacology 2014; 76: 169-174.
    • (2014) Neuropharmacology , vol.76 , pp. 169-174
    • Halliday, M.1    Mallucci, G.R.2
  • 144
    • 84856448928 scopus 로고    scopus 로고
    • Therapeutic targeting of the endoplasmic reticulum in Alzheimer's disease
    • Chadwick W, Mitchell N, Martin B and Maudsley S. Therapeutic targeting of the endoplasmic reticulum in Alzheimer's disease. Curr Alzheimer Res 2012; 9: 110-119.
    • (2012) Curr Alzheimer Res , vol.9 , pp. 110-119
    • Chadwick, W.1    Mitchell, N.2    Martin, B.3    Maudsley, S.4
  • 145
    • 34547126694 scopus 로고    scopus 로고
    • Novel therapeutic strategies for the treatment of protein-misfolding diseases
    • Rochet JC. Novel therapeutic strategies for the treatment of protein-misfolding diseases. Expert Rev Mol Med 2007; 9: 1-34.
    • (2007) Expert Rev Mol Med , vol.9 , pp. 1-34
    • Rochet, J.C.1
  • 146
    • 84879128268 scopus 로고    scopus 로고
    • Modulation of 5-lipoxygenase in proteotoxicity and Alzheimer's disease
    • Valera E, Dargusch R, Maher PA and Schubert D. Modulation of 5-lipoxygenase in proteotoxicity and Alzheimer's disease. J Neurosci 2013; 33: 10512-10525.
    • (2013) J Neurosci , vol.33 , pp. 10512-10525
    • Valera, E.1    Dargusch, R.2    Maher, P.A.3    Schubert, D.4
  • 147
    • 29244491657 scopus 로고    scopus 로고
    • P300 modulates ATF4 stability and transcriptional activity independently of its acetyltransferase domain
    • Lassot I, Estrabaud E, Emiliani S, Benkirane M, Benarous R and Margottin-Goguet F. p300 modulates ATF4 stability and transcriptional activity independently of its acetyltransferase domain. J Biol Chem 2005; 280: 41537-41545.
    • (2005) J Biol Chem , vol.280 , pp. 41537-41545
    • Lassot, I.1    Estrabaud, E.2    Emiliani, S.3    Benkirane, M.4    Benarous, R.5    Margottin-Goguet, F.6
  • 148
    • 84876355956 scopus 로고    scopus 로고
    • UBC9 regulates the stability of XBP1, a key transcription factor controlling the ER stress response
    • Uemura A, Taniguchi M, Matsuo Y, Oku M, Wakabayashi S and Yoshida H. UBC9 regulates the stability of XBP1, a key transcription factor controlling the ER stress response. Cell Struct Funct 2013; 38: 67-79.
    • (2013) Cell Struct Funct , vol.38 , pp. 67-79
    • Uemura, A.1    Taniguchi, M.2    Matsuo, Y.3    Oku, M.4    Wakabayashi, S.5    Yoshida, H.6
  • 149
    • 77950523710 scopus 로고    scopus 로고
    • The regulatory subunits of PI3K, p85alpha and p85beta, interact with XBP-1 and increase its nuclear translocation
    • Park SW, Zhou Y, Lee J, Lu A, Sun C, Chung J, Ueki K and Ozcan U. The regulatory subunits of PI3K, p85alpha and p85beta, interact with XBP-1 and increase its nuclear translocation. Nat Med 2010; 16: 429-437.
    • (2010) Nat Med , vol.16 , pp. 429-437
    • Park, S.W.1    Zhou, Y.2    Lee, J.3    Lu, A.4    Sun, C.5    Chung, J.6    Ueki, K.7    Ozcan, U.8
  • 150
    • 77950537400 scopus 로고    scopus 로고
    • A regulatory subunit of phosphoinositide 3-kinase increases the nuclear accumulation of X-box-binding protein-1 to modulate the unfolded protein response
    • Winnay JN, Boucher J, Mori MA, Ueki K and Kahn CR. A regulatory subunit of phosphoinositide 3-kinase increases the nuclear accumulation of X-box-binding protein-1 to modulate the unfolded protein response. Nat Med 2010; 16: 438-445.
    • (2010) Nat Med , vol.16 , pp. 438-445
    • Winnay, J.N.1    Boucher, J.2    Mori, M.A.3    Ueki, K.4    Kahn, C.R.5
  • 151
    • 84875534184 scopus 로고    scopus 로고
    • UPR Signal Activation by Luminal Sensor Domains
    • Carrara M, Prischi F and Ali MM. UPR Signal Activation by Luminal Sensor Domains. Int J Mol Sci 2013; 14: 6454-6466.
    • (2013) Int J Mol Sci , vol.14 , pp. 6454-6466
    • Carrara, M.1    Prischi, F.2    Ali, M.M.3
  • 152
    • 3843117589 scopus 로고    scopus 로고
    • Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells
    • Vattem KM and Wek RC. Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells. Proc Natl Acad Sci U S A 2004; 101: 11269-11274.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 11269-11274
    • Vattem, K.M.1    Wek, R.C.2
  • 153
    • 0025878233 scopus 로고
    • Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity
    • Hai T and Curran T. Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity. Proc Natl Acad Sci U S A 1991; 88: 3720-3724.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 3720-3724
    • Hai, T.1    Curran, T.2
  • 155
    • 0032079899 scopus 로고    scopus 로고
    • Post-translational processing and turnover kinetics of presynaptically targeted amyloid precursor superfamily proteins in the central nervous system
    • Lyckman AW, Confaloni AM, Thinakaran G, Sisodia SS and Moya KL. Post-translational processing and turnover kinetics of presynaptically targeted amyloid precursor superfamily proteins in the central nervous system. J Biol Chem 1998; 273: 11100-11106.
    • (1998) J Biol Chem , vol.273 , pp. 11100-11106
    • Lyckman, A.W.1    Confaloni, A.M.2    Thinakaran, G.3    Sisodia, S.S.4    Moya, K.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.