메뉴 건너뛰기




Volumn 34, Issue 1, 2013, Pages 115-131

Impaired transcription in Alzheimer's disease: Key role in mitochondrial dysfunction and oxidative stress

Author keywords

Antioxidant defenses; CREB; intranuclear A ; mitochondrial biogenesis; Nrf2; PGC 1 ; transcription factors

Indexed keywords

ADVANCED GLYCATION END PRODUCT RECEPTOR; AMYLOID BETA PROTEIN; BETA SECRETASE; BUNGAROTOXIN RECEPTOR; CRE RECOMBINASE; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; GAMMA SECRETASE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR A; TRANSCRIPTION FACTOR NRF2; UNCLASSIFIED DRUG;

EID: 84874303866     PISSN: 13872877     EISSN: 18758908     Source Type: Journal    
DOI: 10.3233/JAD-121444     Document Type: Review
Times cited : (62)

References (169)
  • 1
    • 17044439021 scopus 로고    scopus 로고
    • Alzheimer's disease: Abeta, tau and synaptic dysfunction
    • LaFerla FM, Oddo S (2005) Alzheimer's disease: Abeta, tau and synaptic dysfunction. Trends Mol Med 11, 170-176.
    • (2005) Trends Mol Med , vol.11 , pp. 170-176
    • Laferla, F.M.1    Oddo, S.2
  • 2
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-beta in Alzheimer's disease
    • LaFerla FM, Green KN, Oddo S (2007) Intracellular amyloid-beta in Alzheimer's disease. Nat Rev Neurosci 8, 499-509.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 499-509
    • Laferla, F.M.1    Green, K.N.2    Oddo, S.3
  • 3
    • 0001181116 scopus 로고    scopus 로고
    • Alzheimer's Disease: Molecular Understanding Predicts Amyloid-Based Therapeutics
    • DOI 10.1146/annurev.pharmtox.43.100901.140248
    • Selkoe DJ, Schenk D (2003) Alzheimer's disease: Molecular understanding predicts amyloid-based therapeutics. Annu Rev Pharmacol Toxicol 43, 545-584. (Pubitemid 37372653)
    • (2003) Annual Review of Pharmacology and Toxicology , vol.43 , pp. 545-584
    • Selkoe, D.J.1    Schenk, D.2
  • 4
    • 79957604912 scopus 로고    scopus 로고
    • Genetics of Alzheimer's disease: New evidences for an old hypothesis?
    • Lambert JC, Amouyel P (2011) Genetics of Alzheimer's disease: New evidences for an old hypothesis? Curr Opin Genet Dev 21, 295-301.
    • (2011) Curr Opin Genet Dev , vol.21 , pp. 295-301
    • Lambert, J.C.1    Amouyel, P.2
  • 6
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe DJ (2001) Alzheimer's disease: Genes, proteins, and therapy. Physiol Rev 81, 741-766. (Pubitemid 32267077)
    • (2001) Physiological Reviews , vol.81 , Issue.2 , pp. 741-766
    • Selkoe, D.J.1
  • 8
    • 71549170836 scopus 로고    scopus 로고
    • Mitochondria and reactive oxygen and nitrogen species in neurological disorders and stroke: Therapeutic implications
    • Bolanos JP, Moro MA, Lizasoain I, Almeida A (2009) Mitochondria and reactive oxygen and nitrogen species in neurological disorders and stroke: Therapeutic implications. Adv Drug Deliv Rev 61, 1299-1315.
    • (2009) Adv Drug Deliv Rev , vol.61 , pp. 1299-1315
    • Bolanos, J.P.1    Ma, M.2    Lizasoain, I.3    Almeida, A.4
  • 10
    • 33846021307 scopus 로고    scopus 로고
    • Apolipoprotein E and low density lipoprotein receptor-related protein facilitate intraneuronal Aβ42 accumulation in amyloid model mice
    • DOI 10.1074/jbc.M604436200
    • Zerbinatti CV, Wahrle SE, Kim H, Cam JA, Bales K, Paul SM, Holtzman DM, Bu G (2006) Apolipoprotein E and low density lipoprotein receptor-related protein facilitate intraneuronal Abeta42 accumulation in amyloid model mice. J Biol Chem 281, 36180-36186. (Pubitemid 46041352)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.47 , pp. 36180-36186
    • Zerbinatti, C.V.1    Wahrle, S.E.2    Kim, H.3    Cam, J.A.4    Bales, K.5    Paul, S.M.6    Holtzman, D.M.7    Bu, G.8
  • 11
    • 0037345672 scopus 로고    scopus 로고
    • Expanding the association between the APOE gene and the risk of Alzheimer's disease: Possible roles for APOE promoter polymorphisms and alterations in APOE transcription
    • DOI 10.1046/j.1471-4159.2003.01615.x
    • Laws SM, Hone E, Gandy S, Martins RN (2003) Expanding the association between the APOE gene and the risk of Alzheimer's disease: Possible roles for APOE promoter polymorphisms and alterations in APOE transcription. J Neurochem 84, 1215-1236. (Pubitemid 36343589)
    • (2003) Journal of Neurochemistry , vol.84 , Issue.6 , pp. 1215-1236
    • Laws, S.M.1    Hone, E.2    Gandy, S.3    Martins, R.N.4
  • 16
    • 0024550204 scopus 로고
    • Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein
    • DOI 10.1016/0092-8674(89)90177-3
    • Weidemann A, Konig G, Bunke D, Fischer P, Salbaum JM, Masters CL, Beyreuther K (1989) Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein. Cell 57, 115-126. (Pubitemid 19098873)
    • (1989) Cell , vol.57 , Issue.1 , pp. 115-126
    • Weidemann, A.1    Konig, G.2    Bunke, D.3    Fischer, P.4    Salbaum, J.M.5    Masters, C.L.6    Beyreuther, K.7
  • 17
    • 0027212769 scopus 로고
    • Identification and transport of full-length amyloid precursor proteins in rat peripheral nervous system
    • Sisodia SS, Koo EH, Hoffman PN, Perry G, Price DL (1993) Identification and transport of full-length amyloid precursor proteins in rat peripheral nervous system. J Neurosci 13, 3136-3142. (Pubitemid 23199238)
    • (1993) Journal of Neuroscience , vol.13 , Issue.7 , pp. 3136-3142
    • Sisodia, S.S.1    Koo, E.H.2    Hoffman, P.N.3    Perry, G.4    Price, D.L.5
  • 18
    • 0033609449 scopus 로고    scopus 로고
    • Cleavage of Alzheimer's amyloid precursor protein by alpha-secretase occurs at the surface of neuronal cells
    • Parvathy S, Hussain I, Karran EH, Turner AJ, Hooper NM (1999) Cleavage of Alzheimer's amyloid precursor protein by alpha-secretase occurs at the surface of neuronal cells. Biochemistry 38, 9728-9734.
    • (1999) Biochemistry , vol.38 , pp. 9728-9734
    • Parvathy, S.1    Hussain, I.2    Karran, E.H.3    Turner, A.J.4    Hooper, N.M.5
  • 24
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • DOI 10.1038/nrm2101, PII NRM2101
    • Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 8, 101-112. (Pubitemid 46432529)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 25
    • 0242361783 scopus 로고    scopus 로고
    • Identity and function of gamma-secretase
    • Kimberly WT, Wolfe MS (2003) Identity and function of gamma-secretase. J Neurosci Res 74, 353-360.
    • (2003) J Neurosci Res , vol.74 , pp. 353-360
    • Kimberly, W.T.1    Wolfe, M.S.2
  • 28
    • 49249118742 scopus 로고    scopus 로고
    • Neurotoxic effect of oligomeric and fibrillar species of amyloid-beta peptide 1-42: Involvement of endoplasmic reticulum calcium release in oligomer-induced cell death
    • Resende R, Ferreiro E, Pereira C, Resende de Oliveira C (2008) Neurotoxic effect of oligomeric and fibrillar species of amyloid-beta peptide 1-42: Involvement of endoplasmic reticulum calcium release in oligomer-induced cell death. Neuroscience 155, 725-737.
    • (2008) Neuroscience , vol.155 , pp. 725-737
    • Resende, R.1    Ferreiro, E.2    Pereira, C.3    Resende De Oliveira, C.4
  • 30
    • 0030064140 scopus 로고    scopus 로고
    • Amyloid β protein deposition in normal aging has the same characteristics as that in Alzheimer's disease: Predominance of Aβ42(43) and association of Aβ40 with cored plaques
    • Fukumoto H, Asami-Odaka A, Suzuki N, Shimada H, Ihara Y, Iwatsubo T (1996) Amyloid beta protein deposition in normal aging has the same characteristics as that in Alzheimer's disease. Predominance of A beta 42 (43) and association of A beta 40 with cored plaques. Am J Pathol 148, 259-265. (Pubitemid 26019660)
    • (1996) American Journal of Pathology , vol.148 , Issue.1 , pp. 259-265
    • Fukumoto, H.1    Asami-Odaka, A.2    Suzuki, N.3    Shimada, H.4    Ihara, Y.5    Iwatsubo, T.6
  • 32
    • 67649367548 scopus 로고    scopus 로고
    • Amyloid beta-protein stimulates trafficking of cholesterol and caveolin-1 from the plasma membrane to the Golgi complex in mouse primary astrocytes
    • Igbavboa U, Sun GY, Weisman GA, He Y, Wood WG (2009) Amyloid beta-protein stimulates trafficking of cholesterol and caveolin-1 from the plasma membrane to the Golgi complex in mouse primary astrocytes. Neuroscience 162, 328-338.
    • (2009) Neuroscience , vol.162 , pp. 328-338
    • Igbavboa, U.1    Sun, G.Y.2    Weisman, G.A.3    He, Y.4    Wood, W.G.5
  • 33
    • 0037096251 scopus 로고    scopus 로고
    • A Novel Function of Monomeric Amyloid β-Protein Serving as an Antioxidant Molecule against Metal-Induced Oxidative Damage
    • Zou K, Gong JS, Yanagisawa K, Michikawa M (2002) A novel function of monomeric amyloid beta-protein serving as an antioxidant molecule against metal-induced oxidative damage. J Neurosci 22, 4833-4841. (Pubitemid 37465598)
    • (2002) Journal of Neuroscience , vol.22 , Issue.12 , pp. 4833-4841
    • Zou, K.1    Gong, J.-S.2    Yanagisawa, K.3    Michikawa, M.4
  • 34
    • 0037195546 scopus 로고    scopus 로고
    • Consistent immunohistochemical detection of intracellular β-amyloid42 in pyramidal neurons of Alzheimer's disease entorhinal cortex
    • DOI 10.1016/S0304-3940(02)00875-3, PII S0304394002008753
    • D'Andrea MR, Nagele RG, Wang HY, Lee DH (2002) Consistent immunohistochemical detection of intracellular beta-amyloid42 in pyramidal neurons of Alzheimer's disease entorhinal cortex. Neurosci Lett 333, 163-166. (Pubitemid 35335768)
    • (2002) Neuroscience Letters , vol.333 , Issue.3 , pp. 163-166
    • D'Andrea, M.R.1    Nagele, R.G.2    Wang, H.-Y.3    Lee, D.H.S.4
  • 38
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer's Disease with plaques and tangles: Intracellular Aβ and synaptic dysfunction
    • DOI 10.1016/S0896-6273(03)00434-3
    • Oddo S, Caccamo A, Shepherd JD, Murphy MP, Golde TE, Kayed R, Metherate R, Mattson MP, Akbari Y, LaFerla FM (2003) Triple-transgenic model of Alzheimer's disease with plaques and tangles: Intracellular Abeta and synaptic dysfunction. Neuron 39, 409-421. (Pubitemid 36937044)
    • (2003) Neuron , vol.39 , Issue.3 , pp. 409-421
    • Oddo, S.1    Caccamo, A.2    Shepherd, J.D.3    Murphy, M.P.4    Golde, T.E.5    Kayed, R.6    Metherate, R.7    Mattson, M.P.8    Akbari, Y.9    LaFerla, F.M.10
  • 39
    • 0037066072 scopus 로고    scopus 로고
    • 1-42 in neurons is facilitated by the α7 nicotinic acetylcholine receptor in Alzheimer's disease
    • DOI 10.1016/S0306-4522(01)00460-2, PII S0306452201004602
    • Nagele RG, D'Andrea MR, Anderson WJ, Wang HY (2002) Intracellular accumulation of beta-amyloid (1-42) in neurons is facilitated by the alpha 7 nicotinic acetylcholine receptor in Alzheimer's disease. Neuroscience 110, 199-211. (Pubitemid 34214939)
    • (2002) Neuroscience , vol.110 , Issue.2 , pp. 199-211
    • Nagele, R.G.1    D'Andrea, M.R.2    Anderson, W.J.3    Wang, H.-Y.4
  • 40
    • 79955454688 scopus 로고    scopus 로고
    • Amyloid-Beta interaction with mitochondria
    • Pagani L, Eckert A (2011) Amyloid-Beta interaction with mitochondria. Int J Alzheimers Dis 2011, 925050.
    • (2011) Int J Alzheimers Dis , vol.2011 , pp. 925050
    • Pagani, L.1    Eckert, A.2
  • 41
    • 0034888054 scopus 로고    scopus 로고
    • Immunohistochemical and ultrastructural study of basophilic inclusions in adult-onset motor neuron disease
    • Sasaki S, Toi S, Shirata A, Yamane K, Sakuma H, Iwata M (2001) Immunohistochemical and ultrastructural study of basophilic inclusions in adult-onset motor neuron disease. Acta Neuropathol 102, 200-206. (Pubitemid 32771671)
    • (2001) Acta Neuropathologica , vol.102 , Issue.2 , pp. 200-206
    • Sasaki, S.1    Toi, S.2    Shirata, A.3    Yamane, K.4    Sakuma, H.5    Iwata, M.6
  • 43
    • 0031918250 scopus 로고    scopus 로고
    • Receptors for advanced glycosylation endproducts in human brain: Role in brain homeostasis
    • Li JJ, Dickson D, Hof PR, Vlassara H (1998) Receptors for advanced glycosylation endproducts in human brain: Role in brain homeostasis. Mol Med 4, 46-60. (Pubitemid 28134332)
    • (1998) Molecular Medicine , vol.4 , Issue.1 , pp. 46-60
    • Li, J.J.1    Dickson, D.2    Hof, P.R.3    Vlassara, H.4
  • 44
    • 0035847269 scopus 로고    scopus 로고
    • Immunohistochemical distribution of the receptor for advanced glycation end products in neurons and astrocytes in Alzheimer's disease
    • DOI 10.1016/S0006-8993(00)03075-4, PII S0006899300030754
    • Sasaki N, Toki S, Chowei H, Saito T, Nakano N, Hayashi Y, Takeuchi M, Makita Z (2001) Immunohistochemical distribution of the receptor for advanced glycation end products in neurons and astrocytes in Alzheimer's disease. Brain Res 888, 256-262. (Pubitemid 32058790)
    • (2001) Brain Research , vol.888 , Issue.2 , pp. 256-262
    • Sasaki, N.1    Toki, S.2    Chowei, H.3    Saito, T.4    Nakano, N.5    Hayashi, Y.6    Takeuchi, M.7    Makita, Z.8
  • 46
    • 0037135272 scopus 로고    scopus 로고
    • Uptake and pathogenic effects of amyloid beta peptide 1-42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists
    • DOI 10.1016/S0306-4522(02)00132-X, PII S030645220200132X
    • Bi X, Gall CM, Zhou J, Lynch G (2002) Uptake and pathogenic effects of amyloid beta peptide 1-42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists. Neuroscience 112, 827-840. (Pubitemid 34667047)
    • (2002) Neuroscience , vol.112 , Issue.4 , pp. 827-840
    • Bi, X.1    Gall, C.M.2    Zhou, J.3    Lynch, G.4
  • 47
    • 84856958510 scopus 로고    scopus 로고
    • Amyloid beta peptide 1-42 disturbs intracellular calcium homeostasis through activation of GluN2B-containing N-methyl-d-aspartate receptors in cortical cultures
    • Ferreira IL, Bajouco LM, Mota SI, Auberson YP, Oliveira CR, Rego AC (2012) Amyloid beta peptide 1-42 disturbs intracellular calcium homeostasis through activation of GluN2B-containing N-methyl-d-aspartate receptors in cortical cultures. Cell Calcium 51, 95-106.
    • (2012) Cell Calcium , vol.51 , pp. 95-106
    • Ferreira, I.L.1    Bajouco, L.M.2    Mota, S.I.3    Auberson, Y.P.4    Oliveira, C.R.5    Rego, A.C.6
  • 50
    • 0032551528 scopus 로고    scopus 로고
    • Amyloid β protein is internalized selectively by hippocampal field CA1 and causes neurons to accumulate amyloidogenic carboxyterminal fragments of the amyloid precursor protein
    • DOI 10.1002/(SICI)1096-9861(19980720)397:1<139::AID-CNE10>3.0.CO;2- K
    • Bahr BA, Hoffman KB, Yang AJ, Hess US, Glabe CG, Lynch G (1998) Amyloid beta protein is internalized selectively by hippocampal field CA1 and causes neurons to accumulate amyloidogenic carboxyterminal fragments of the amyloid precursor protein. J Comp Neurol 397, 139-147. (Pubitemid 28304057)
    • (1998) Journal of Comparative Neurology , vol.397 , Issue.1 , pp. 139-147
    • Bahr, B.A.1    Hoffman, K.B.2    Yang, A.J.3    Hess, U.S.4    Glabe, C.G.5    Lynch, G.6
  • 51
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers
    • Lauren J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM (2009) Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature 457, 1128-1132.
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Lauren, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 53
    • 14644442872 scopus 로고    scopus 로고
    • Intraneuronal Aβ causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice
    • DOI 10.1016/j.neuron.2005.01.040
    • Billings LM, Oddo S, Green KN, McGaugh JL, LaFerla FM (2005) Intraneuronal Abeta causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice. Neuron 45, 675-688. (Pubitemid 40320703)
    • (2005) Neuron , vol.45 , Issue.5 , pp. 675-688
    • Billings, L.M.1    Oddo, S.2    Green, K.N.3    McGaugh, J.L.4    LaFerla, F.M.5
  • 55
    • 4644238084 scopus 로고    scopus 로고
    • Early changes in neurons of the hippocampus and neocortex in transgenic rats expressing intracellular human a-β
    • Lopez EM, Bell KF, Ribeiro-da-Silva A, Cuello AC (2004) Early changes in neurons of the hippocampus and neocortex in transgenic rats expressing intracellular human a-beta. J Alzheimers Dis 6, 421-431; discussion 443-9. (Pubitemid 39287255)
    • (2004) Journal of Alzheimer's Disease , vol.6 , Issue.4 , pp. 421-431
    • Lopez, E.M.1    Bell, K.F.S.2    Ribeiro-Da-Silva, A.3    Cuello, A.C.4
  • 56
    • 0037017399 scopus 로고    scopus 로고
    • 1-42 through p53 and Bax in cultured primary human neurons
    • DOI 10.1083/jcb.200110119
    • Zhang Y, McLaughlin R, Goodyer C, LeBlanc A (2002) Selective cytotoxicity of intracellular amyloid beta peptide1-42 through p53 and Bax in cultured primary human neurons. J Cell Biol 156, 519-529. (Pubitemid 34839899)
    • (2002) Journal of Cell Biology , vol.156 , Issue.3 , pp. 519-529
    • Zhang, Y.1    McLaughlin, R.2    Goodyer, C.3    LeBlanc, A.4
  • 60
    • 79957653811 scopus 로고    scopus 로고
    • Intraneuronal APP not free Abeta peptides in 3xTg-AD mice: Implications for tau versus Abeta-mediated Alzheimer neurodegeneration
    • Winton MJ, Lee EB, Sun E, Wong MM, Leight S, Zhang B, Trojanowski JQ, Lee VM (2011) Intraneuronal APP, not free Abeta peptides in 3xTg-AD mice: Implications for tau versus Abeta-mediated Alzheimer neurodegeneration. J Neurosci 31, 7691-7699.
    • (2011) J Neurosci , vol.31 , pp. 7691-7699
    • Winton, M.J.1    Lee, E.B.2    Sun, E.3    Wong, M.M.4    Leight, S.5    Zhang, B.6    Trojanowski, J.Q.7    Lee, V.M.8
  • 62
    • 84858022369 scopus 로고    scopus 로고
    • AbetaPP accumulation and/or intraneuronal amyloid-beta accumulation? the 3xTg-AD mouse model revisited
    • Wirths O, Dins A, Bayer TA (2012) AbetaPP accumulation and/or intraneuronal amyloid-beta accumulation? The 3xTg-AD mouse model revisited. J Alzheimers Dis 28, 897-904.
    • (2012) J Alzheimers Dis , vol.28 , pp. 897-904
    • Wirths, O.1    Dins, A.2    Bayer, T.A.3
  • 63
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of A beta accumulation in Alzheimer's disease neurons: Implications for free radical generation and oxidative damage in disease progression
    • Manczak M, Anekonda TS, Henson E, Park BS, Quinn J, Reddy PH (2006) Mitochondria are a direct site of A beta accumulation in Alzheimer's disease neurons: Implications for free radical generation and oxidative damage in disease progression. Hum Mol Genet 15, 1437-1449.
    • (2006) Hum Mol Genet , vol.15 , pp. 1437-1449
    • Manczak, M.1    Anekonda, T.S.2    Henson, E.3    Park, B.S.4    Quinn, J.5    Reddy, P.H.6
  • 66
    • 79251584617 scopus 로고    scopus 로고
    • Mitochondrial gammasecretase participates in the metabolism of mitochondriaassociated amyloid precursor protein
    • Pavlov PF, Wiehager B, Sakai J, Frykman S, Behbahani H, Winblad B, Ankarcrona M (2011) Mitochondrial gammasecretase participates in the metabolism of mitochondriaassociated amyloid precursor protein. FASEB J 25, 78-88.
    • (2011) FASEB J , vol.25 , pp. 78-88
    • Pavlov, P.F.1    Wiehager, B.2    Sakai, J.3    Frykman, S.4    Behbahani, H.5    Winblad, B.6    Ankarcrona, M.7
  • 67
    • 0037192120 scopus 로고    scopus 로고
    • Differential effects of proteases involved in intracellular degradation of amyloid β-protein between detergent-soluble and -insoluble pools in CHO-695 cells
    • DOI 10.1021/bi011193l
    • Sudoh S, Frosch MP, Wolf BA (2002) Differential effects of proteases involved in intracellular degradation of amyloid beta-protein between detergent-soluble and -insoluble pools in CHO-695 cells. Biochemistry 41, 1091-1099. (Pubitemid 34083761)
    • (2002) Biochemistry , vol.41 , Issue.4 , pp. 1091-1099
    • Sudoh, S.1    Frosch, M.P.2    Wolf, B.A.3
  • 69
    • 0037186457 scopus 로고    scopus 로고
    • Abundant type 10 17β-hydroxysteroid dehydrogenase in the hippocampus of mouse Alzheimer's disease model
    • DOI 10.1016/S0169-328X(02)00102-X, PII S0169328X0200102X
    • He XY, Wen GY, Merz G, Lin D, Yang YZ, Mehta P, Schulz H, Yang SY (2002) Abundant type 10 17 beta-hydroxysteroid dehydrogenase in the hippocampus of mouse Alzheimer's disease model. Brain Res Mol Brain Res 99, 46-53. (Pubitemid 34178500)
    • (2002) Molecular Brain Research , vol.99 , Issue.1 , pp. 46-53
    • He, X.-Y.1    Wen, G.-Y.2    Merz, G.3    Lin, D.4    Yang, Y.-Z.5    Mehta, P.6    Schulz, H.7    Yang, S.-Y.8
  • 71
    • 36248991348 scopus 로고    scopus 로고
    • Chronic exposure to sub-lethal beta-amyloid (Aβ) inhibits the import of nuclear-encoded proteins to mitochondria in differentiated PC12 cells
    • DOI 10.1111/j.1471-4159.2007.04907.x
    • Sirk D, Zhu Z, Wadia JS, Shulyakova N, Phan N, Fong J, Mills LR (2007) Chronic exposure to sub-lethal betaamyloid (Abeta) inhibits the import of nuclear-encoded proteins to mitochondria in differentiated PC12 cells. J Neurochem 103, 1989-2003. (Pubitemid 350126630)
    • (2007) Journal of Neurochemistry , vol.103 , Issue.5 , pp. 1989-2003
    • Sirk, D.1    Zhu, Z.2    Wadia, J.S.3    Shulyakova, N.4    Phan, N.5    Fong, J.6    Mills, L.R.7
  • 74
    • 34447498864 scopus 로고    scopus 로고
    • High cyclophilin D content of synaptic mitochondria results in increased vulnerability to permeability transition
    • DOI 10.1523/JNEUROSCI.0646-07.2007
    • Naga KK, Sullivan PG, Geddes JW (2007) High cyclophilin D content of synaptic mitochondria results in increased vulnerability to permeability transition. J Neurosci 27, 7469-7475. (Pubitemid 47066566)
    • (2007) Journal of Neuroscience , vol.27 , Issue.28 , pp. 7469-7475
    • Naga, K.K.1    Sullivan, P.G.2    Geddes, J.W.3
  • 75
    • 0028110234 scopus 로고
    • Cortical cytochrome oxidase activity is reduced in Alzheimer's disease
    • Mutisya EM, Bowling AC, Beal MF (1994) Cortical cytochrome oxidase activity is reduced in Alzheimer's disease. J Neurochem 63, 2179-2184. (Pubitemid 24369993)
    • (1994) Journal of Neurochemistry , vol.63 , Issue.6 , pp. 2179-2184
    • Mutisya, E.M.1    Bowling, A.C.2    Beal, M.F.3
  • 77
    • 77749326636 scopus 로고    scopus 로고
    • Mitochondrial dynamics in Alzheimer's disease: Opportunities for future treatment strategies
    • Bonda DJ, Wang X, Perry G, Smith MA, Zhu X (2010) Mitochondrial dynamics in Alzheimer's disease: Opportunities for future treatment strategies. Drugs Aging 27, 181-192.
    • (2010) Drugs Aging , vol.27 , pp. 181-192
    • Bonda, D.J.1    Wang, X.2    Perry, G.3    Smith, M.A.4    Zhu, X.5
  • 78
    • 58049218922 scopus 로고    scopus 로고
    • Amyloid-beta overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins
    • Wang X, Su B, Siedlak SL, Moreira PI, Fujioka H, Wang Y, Casadesus G, Zhu X (2008) Amyloid-beta overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins. Proc Natl Acad Sci U S A 105, 19318-19323.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 19318-19323
    • Wang, X.1    Su, B.2    Siedlak, S.L.3    Moreira, P.I.4    Fujioka, H.5    Wang, Y.6    Casadesus, G.7    Zhu, X.8
  • 80
    • 68849110235 scopus 로고    scopus 로고
    • Reduction of oxidative stress, amyloid deposition, and memory deficit by manganese superoxide dismutase overexpression in a transgenic mouse model of Alzheimer's disease
    • Dumont M, Wille E, Stack C, Calingasan NY, Beal MF, Lin MT (2009) Reduction of oxidative stress, amyloid deposition, and memory deficit by manganese superoxide dismutase overexpression in a transgenic mouse model of Alzheimer's disease. FASEB J 23, 2459-2466.
    • (2009) FASEB J , vol.23 , pp. 2459-2466
    • Dumont, M.1    Wille, E.2    Stack, C.3    Calingasan, N.Y.4    Beal, M.F.5    Lin, M.T.6
  • 82
    • 80053384785 scopus 로고    scopus 로고
    • Functional activity of the novel Alzheimer's amyloid beta-peptide interacting domain (AbetaID) in the APP and BACE1 promoter sequences and implications in activating apoptotic genes and in amyloidogenesis
    • Bailey JA, MaloneyB, GeYW, Lahiri DK (2011) Functional activity of the novel Alzheimer's amyloid beta-peptide interacting domain (AbetaID) in the APP and BACE1 promoter sequences and implications in activating apoptotic genes and in amyloidogenesis. Gene 488, 13-22.
    • (2011) Gene , vol.488 , pp. 13-22
    • Bailey, J.A.1    Maloney, B.2    Ge, Y.W.3    Lahiri, D.K.4
  • 83
    • 16344379032 scopus 로고    scopus 로고
    • Characterization of the APP proximal promoter and 5′-untranslated regions: Identification or cell type-specific domains and implications in APP gene expression and Alzheimer's disease
    • DOI 10.1096/fj.04-2900fje
    • Lahiri DK, Ge YW, Maloney B (2005) Characterization of the APP proximal promoter and 5β-untranslated regions: Identification of cell type-specific domains and implications in APP gene expression and Alzheimer's disease. FASEB J 19, 653-655. (Pubitemid 40471275)
    • (2005) FASEB Journal , vol.19 , Issue.6 , pp. 653-655
    • Lahiri, D.K.1    Ge, Y.-W.2    Maloney, B.3
  • 84
    • 80053385335 scopus 로고    scopus 로고
    • The Alzheimer's amyloid beta-peptide (Abeta) binds a specific DNA Abetainteracting domain (AbetaID) in the APP, BACE1, and APOE promoters in a sequence-specific manner: Characterizing a new regulatory motif
    • Maloney B, Lahiri DK (2011) The Alzheimer's amyloid beta-peptide (Abeta) binds a specific DNA Abetainteracting domain (AbetaID) in the APP, BACE1, and APOE promoters in a sequence-specific manner: Characterizing a new regulatory motif. Gene 488, 1-12.
    • (2011) Gene , vol.488 , pp. 1-12
    • Maloney, B.1    Lahiri, D.K.2
  • 86
    • 79959265543 scopus 로고    scopus 로고
    • Bioinformatics identification of modules of transcription factor binding sites in Alzheimer's disease-related genes by in silico promoter analysis and microarrays
    • Augustin R, Lichtenthaler SF, GreeffM, Hansen J, WurstW, Trumbach D (2011) Bioinformatics identification of modules of transcription factor binding sites in Alzheimer's disease-related genes by in silico promoter analysis and microarrays. Int J Alzheimers Dis 2011, 154325.
    • (2011) Int J Alzheimers Dis , vol.2011 , pp. 154325
    • Augustin, R.1    Lichtenthaler, S.F.2    Greeff, M.3    Hansen, J.4    Wurst, W.5    Trumbach, D.6
  • 87
    • 79251644774 scopus 로고    scopus 로고
    • Whole transcriptome sequencing reveals gene expression and splicing differences in brain regions affected by Alzheimer's disease
    • Twine NA, Janitz K, Wilkins MR, Janitz M (2011) Whole transcriptome sequencing reveals gene expression and splicing differences in brain regions affected by Alzheimer's disease. PLoS One 6, e16266.
    • (2011) PLoS One , vol.6
    • Twine, N.A.1    Janitz, K.2    Wilkins, M.R.3    Janitz, M.4
  • 90
    • 77956869250 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid beta converting left-handed Z-DNA back to righthanded B-form
    • Geng J, Zhao C, Ren J, Qu X (2010) Alzheimer's disease amyloid beta converting left-handed Z-DNA back to righthanded B-form. Chem Commun (Camb) 46, 7187-7189.
    • (2010) Chem Commun (Camb) , vol.46 , pp. 7187-7189
    • Geng, J.1    Zhao, C.2    Ren, J.3    Qu, X.4
  • 91
    • 57749120460 scopus 로고    scopus 로고
    • Nrf1 and Nrf2 play distinct roles in activation of antioxidant response element-dependent genes
    • Ohtsuji M, Katsuoka F, Kobayashi A, Aburatani H, Hayes JD, Yamamoto M (2008) Nrf1 and Nrf2 play distinct roles in activation of antioxidant response element-dependent genes. J Biol Chem 283, 33554-33562.
    • (2008) J Biol Chem , vol.283 , pp. 33554-33562
    • Ohtsuji, M.1    Katsuoka, F.2    Kobayashi, A.3    Aburatani, H.4    Hayes, J.D.5    Yamamoto, M.6
  • 92
    • 0039726828 scopus 로고    scopus 로고
    • TheCNCbasic leucine zipper factor, Nrf1, is essential for cell survival in response to oxidative stress-inducing agents. Role for Nrf1 in gammagcs (l) and gss expression in mouse fibroblasts
    • Kwong M, KanYW, Chan JY (1999) TheCNCbasic leucine zipper factor, Nrf1, is essential for cell survival in response to oxidative stress-inducing agents. Role for Nrf1 in gammagcs (l) and gss expression in mouse fibroblasts. J Biol Chem 274, 37491-37498.
    • (1999) J Biol Chem , vol.274 , pp. 37491-37498
    • Kwong, M.1    Kan, Y.W.2    Chan, J.Y.3
  • 93
    • 36749013169 scopus 로고    scopus 로고
    • The NHB1 (N-terminal homology box 1) sequence in transcription factor Nrf1 is required to anchor it to the endoplasmic reticulum and also to enable its asparagine-glycosylation
    • DOI 10.1042/BJ20070761
    • Zhang Y, Lucocq JM, Yamamoto M, Hayes JD (2007) The NHB1 (N-terminal homology box 1) sequence in transcription factor Nrf1 is required to anchor it to the endoplasmic reticulum and also to enable its asparagine-glycosylation. Biochem J 408, 161-172. (Pubitemid 350206339)
    • (2007) Biochemical Journal , vol.408 , Issue.2 , pp. 161-172
    • Zhang, Y.1    Lucocq, J.M.2    Yamamoto, M.3    Hayes, J.D.4
  • 94
    • 33745807575 scopus 로고    scopus 로고
    • Nrf1 is targeted to the endoplasmic reticulum membrane by an N-terminal transmembrane domain: Inhibition of nuclear translocation and transacting function
    • DOI 10.1074/jbc.M602802200
    • Wang W, Chan JY (2006) Nrf1 is targeted to the endoplasmic reticulum membrane by an N-terminal transmembrane domain. Inhibition of nuclear translocation and transacting function. J Biol Chem 281, 19676-19687. (Pubitemid 44035470)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.28 , pp. 19676-19687
    • Wang, W.1    Chan, J.Y.2
  • 95
    • 1942520367 scopus 로고    scopus 로고
    • Nrf2 signaling in coordinated activation of antioxidant gene expression
    • DOI 10.1016/j.freeradbiomed.2004.02.074, PII S0891584904001923
    • Jaiswal AK (2004) Nrf2 signaling in coordinated activation of antioxidant gene expression. Free Radic Biol Med 36, 1199-1207. (Pubitemid 38526313)
    • (2004) Free Radical Biology and Medicine , vol.36 , Issue.10 , pp. 1199-1207
    • Jaiswal, A.K.1
  • 96
    • 3142570440 scopus 로고    scopus 로고
    • The pathways and molecular mechanisms regulating Nrf2 activation in response to chemical stress
    • DOI 10.1016/j.freeradbiomed.2004.04.033, PII S089158490400379X
    • Nguyen T, Yang CS, Pickett CB (2004) The pathways and molecular mechanisms regulating Nrf2 activation in response to chemical stress. Free Radic Biol Med 37, 433-441. (Pubitemid 38901076)
    • (2004) Free Radical Biology and Medicine , vol.37 , Issue.4 , pp. 433-441
    • Nguyen, T.1    Yang, C.S.2    Pickett, C.B.3
  • 97
    • 0034752461 scopus 로고    scopus 로고
    • Two domains of Nrf2 cooperatively bind CBP, a CREB binding protein, and synergistically activate transcription
    • DOI 10.1046/j.1365-2443.2001.00469.x
    • Katoh Y, Itoh K, Yoshida E, Miyagishi M, Fukamizu A, Yamamoto M (2001) Two domains of Nrf2 cooperatively bind CBP, a CREB binding protein, and synergistically activate transcription. Genes Cells 6, 857-868. (Pubitemid 33019739)
    • (2001) Genes to Cells , vol.6 , Issue.10 , pp. 857-868
    • Katoh, Y.1    Itoh, K.2    Yoshida, E.3    Miyagishi, M.4    Fukamizu, A.5    Yamamoto, M.6
  • 98
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh K, Wakabayashi N, Katoh Y, Ishii T, Igarashi K, Engel JD, Yamamoto M (1999)Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev 13, 76-86. (Pubitemid 29045117)
    • (1999) Genes and Development , vol.13 , Issue.1 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 100
    • 0036854702 scopus 로고    scopus 로고
    • The transcriptional activation of the human copper/zinc superoxide dismutase gene by 2,3,7,8-tetrachlorodibenzo-p-dioxin through two different regulator sites, the antioxidant responsive element and xenobiotic responsive element
    • DOI 10.1023/A:1020600509965
    • Park EY, Rho HM (2002) The transcriptional activation of the human copper/zinc superoxide dismutase gene by 2, 3, 7, 8-tetrachlorodibenzo-p-dioxin through two different regulator sites, the antioxidant responsive element and xenobiotic responsive element. Mol Cell Biochem 240, 47-55. (Pubitemid 35385819)
    • (2002) Molecular and Cellular Biochemistry , vol.240 , Issue.1-2 , pp. 47-55
    • Park, E.Y.1    Rho, H.M.2
  • 102
    • 0033543566 scopus 로고    scopus 로고
    • Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene
    • Alam J, Stewart D, Touchard C, Boinapally S, Choi AM, Cook JL (1999) Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene. J Biol Chem 274, 26071-26078.
    • (1999) J Biol Chem , vol.274 , pp. 26071-26078
    • Alam, J.1    Stewart, D.2    Touchard, C.3    Boinapally, S.4    Choi, A.M.5    Cook, J.L.6
  • 104
    • 1642535318 scopus 로고    scopus 로고
    • Induction of murine NAD(P)H:quinone oxidoreductase by 2,3,7,8- tetrachlorodibenzo-p-dioxin requires the CNC (cap 'n' collar) basic leucine zipper transcription factor Nrf2 (nuclear factor erythroid 2-related factor 2): Cross-interaction between AhR (aryl hydrocarbon receptor) and Nrf2 signal transduction
    • DOI 10.1042/BJ20031123
    • Ma Q, Kinneer K, Bi Y, Chan JY, Kan YW (2004) Induction of murine NAD (P)H:quinone oxidoreductase by 2, 3, 7, 8-tetrachlorodibenzo-p-dioxin requires the CNC (cap 'n' collar) basic leucine zipper transcription factor Nrf2 (nuclear factor erythroid 2-related factor 2): Crossinteraction between AhR (aryl hydrocarbon receptor) and Nrf2 signal transduction. Biochem J 377, 205-213. (Pubitemid 38114447)
    • (2004) Biochemical Journal , vol.377 , Issue.1 , pp. 205-213
    • Ma, Q.1    Kinneer, K.2    Bi, Y.3    Chan, J.Y.4    Kan, Y.W.5
  • 106
    • 0033731182 scopus 로고    scopus 로고
    • Regulation of the antioxidant response element by protein kinase C-mediated phosphorylation of NF-E2-related factor 2
    • Huang HC, Nguyen T, Pickett CB (2000) Regulation of the antioxidant response element by protein kinase C-mediated phosphorylation of NF-E2-related factor 2. Proc Natl Acad Sci U S A 97, 12475-12480.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 12475-12480
    • Huang, H.C.1    Nguyen, T.2    Pickett, C.B.3
  • 107
    • 33748358379 scopus 로고    scopus 로고
    • Mechanism of action of isothiocyanates: The induction of ARE-regulated genes is associated with activation of ERK and JNK and the phosphorylation and nuclear translocation of Nrf2
    • DOI 10.1158/1535-7163.MCT-05-0497
    • Xu C, Yuan X, Pan Z, Shen G, Kim JH, Yu S, Khor TO, Li W, Ma J, Kong AN (2006) Mechanism of action of isothiocyanates: The induction of ARE-regulated genes is associated with activation of ERK and JNK and the phosphorylation and nuclear translocation of Nrf2. Mol Cancer Ther 5, 1918-1926. (Pubitemid 44336562)
    • (2006) Molecular Cancer Therapeutics , vol.5 , Issue.8 , pp. 1918-1926
    • Xu, C.1    Yuan, X.2    Pan, Z.3    Shen, G.4    Kim, J.-H.5    Yu, S.6    Khor, T.O.7    Li, W.8    Ma, J.9    Kong, A.-N.T.10
  • 108
    • 56249106571 scopus 로고    scopus 로고
    • Nrf2 as a master redox switch in turning on the cellular signaling involved in the induction of cytoprotective genes by some chemopreventive phytochemicals
    • Surh YJ, Kundu JK, Na HK (2008) Nrf2 as a master redox switch in turning on the cellular signaling involved in the induction of cytoprotective genes by some chemopreventive phytochemicals. Planta Med 74, 1526-1539.
    • (2008) Planta Med , vol.74 , pp. 1526-1539
    • Surh, Y.J.1    Kundu, J.K.2    Na, H.K.3
  • 109
    • 33744950387 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3β inhibits the xenobiotic and antioxidant cell response by direct phosphorylation and nuclear exclusion of the transcription factor Nrf2
    • DOI 10.1074/jbc.M513737200
    • Salazar M, Rojo AI, Velasco D, de Sagarra RM, CuadradoA (2006) Glycogen synthase kinase-3beta inhibits the xenobiotic and antioxidant cell response by direct phosphorylation and nuclear exclusion of the transcription factor Nrf2. J Biol Chem 281, 14841-14851. (Pubitemid 43855189)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.21 , pp. 14841-14851
    • Salazar, M.1    Rojo, A.I.2    Velasco, D.3    De Sagarra, R.M.4    Cuadrado, A.5
  • 110
    • 34447526197 scopus 로고    scopus 로고
    • GSK-3β acts upstream of Fyn kinase in regulation of nuclear export and degradation of NF-E2 related factor 2
    • DOI 10.1074/jbc.M611336200
    • Jain AK, Jaiswal AK (2007) GSK-3beta acts upstream of Fyn kinase in regulation of nuclear export and degradation of NF-E2 related factor 2. J Biol Chem 282, 16502-16510. (Pubitemid 47100395)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.22 , pp. 16502-16510
    • Jain, A.K.1    Jaiswal, A.K.2
  • 111
    • 33744953050 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 568 controls nuclear export of Nrf2
    • DOI 10.1074/jbc.M511198200
    • Jain AK, Jaiswal AK (2006) Phosphorylation of tyrosine 568 controls nuclear export of Nrf2. J Biol Chem 281, 12132-12142. (Pubitemid 43855477)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.17 , pp. 12132-12142
    • Jain, A.K.1    Jaiswal, A.K.2
  • 112
    • 79952658955 scopus 로고    scopus 로고
    • The Nrf2-inducible antioxidant defense in astrocytes can be both up-and down-regulated by activated microglia: Involvement of p38 MAPK
    • Correa F, Ljunggren E, Mallard C, Nilsson M, Weber SG, Sandberg M (2011) The Nrf2-inducible antioxidant defense in astrocytes can be both up-and down-regulated by activated microglia: Involvement of p38 MAPK. Glia 59, 785-799.
    • (2011) Glia , vol.59 , pp. 785-799
    • Correa, F.1    Ljunggren, E.2    Mallard, C.3    Nilsson, M.4    Weber, S.G.5    Sandberg, M.6
  • 115
    • 0034814057 scopus 로고    scopus 로고
    • Interleukin-1 promotion of MAPK-p38 overexpression in experimental animals and in Alzheimer's disease: Potential significance for tau protein phosphorylation
    • DOI 10.1016/S0197-0186(01)00041-9, PII S0197018601000419
    • Sheng JG, Jones RA, Zhou XQ, McGinness JM, Van Eldik LJ, Mrak RE, Griffin WS (2001) Interleukin-1 promotion of MAPK-p38 overexpression in experimental animals and in Alzheimer's disease: Potential significance for tau protein phosphorylation. Neurochem Int 39, 341-348. (Pubitemid 32907398)
    • (2001) Neurochemistry International , vol.39 , Issue.5-6 , pp. 341-348
    • Sheng, J.G.1    Jones, R.A.2    Zhou, X.Q.3    McGinness, J.M.4    Van Eldik, L.J.5    Mrak, R.E.6    Griffin, W.S.T.7
  • 118
    • 0036284021 scopus 로고    scopus 로고
    • Early accumulation of p62 in neurofibrillary tangles in alzheimer's disease: Possible role in tangle formation
    • DOI 10.1046/j.1365-2990.2002.00394.x
    • Kuusisto E, Salminen A, Alafuzoff I (2002) Early accumulation of p62 in neurofibrillary tangles in Alzheimer's disease: Possible role in tangle formation. Neuropathol Appl Neurobiol 28, 228-237. (Pubitemid 34639445)
    • (2002) Neuropathology and Applied Neurobiology , vol.28 , Issue.3 , pp. 228-237
    • Kuusisto, E.1    Salminen, A.2    Alafuzoff, I.3
  • 120
    • 77649272440 scopus 로고    scopus 로고
    • Stabilization of transcription factor Nrf2 by tBHQ prevents oxidative stress-induced amyloid beta formation in NT2N neurons
    • Eftekharzadeh B, Maghsoudi N, Khodagholi F (2010) Stabilization of transcription factor Nrf2 by tBHQ prevents oxidative stress-induced amyloid beta formation in NT2N neurons. Biochimie 92, 245-253.
    • (2010) Biochimie , vol.92 , pp. 245-253
    • Eftekharzadeh, B.1    Maghsoudi, N.2    Khodagholi, F.3
  • 121
    • 79953803997 scopus 로고    scopus 로고
    • 2-Ethoxy-4, 5-diphenyl-1, 3-oxazine-6-one activates the Nrf2/HO-1 axis and protects against oxidative stress-induced neuronal death
    • Ansari N, Khodagholi F, Amini M (2011) 2-Ethoxy-4, 5-diphenyl-1, 3-oxazine-6-one activates the Nrf2/HO-1 axis and protects against oxidative stress-induced neuronal death. Eur J Pharmacol 658, 84-90.
    • (2011) Eur J Pharmacol , vol.658 , pp. 84-90
    • Ansari, N.1    Khodagholi, F.2    Amini, M.3
  • 122
    • 80051791713 scopus 로고    scopus 로고
    • Downregulation of CREB expression in Alzheimer's brain and in Abeta-treated rat hippocampal neurons
    • Pugazhenthi S, Wang M, Pham S, Sze CI, Eckman CB (2011) Downregulation of CREB expression in Alzheimer's brain and in Abeta-treated rat hippocampal neurons. Mol Neurodegener 6, 60.
    • (2011) Mol Neurodegener , vol.6 , pp. 60
    • Pugazhenthi, S.1    Wang, M.2    Pham, S.3    Sze, C.I.4    Eckman, C.B.5
  • 123
    • 0037101970 scopus 로고    scopus 로고
    • Function and regulation of CREB family transcription factors in the nervous system
    • DOI 10.1016/S0896-6273(02)00828-0
    • Lonze BE, Ginty DD (2002) Function and regulation of CREB family transcription factors in the nervous system. Neuron 35, 605-623. (Pubitemid 35229980)
    • (2002) Neuron , vol.35 , Issue.4 , pp. 605-623
    • Lonze, B.E.1    Ginty, D.D.2
  • 124
    • 0043037252 scopus 로고    scopus 로고
    • 2+/CREB/CBP-dependent gene regulation: A shared mechanism critical in long-term synaptic plasticity and neuronal survival
    • DOI 10.1016/S0143-4160(03)00140-4
    • Bito H, Takemoto-Kimura S (2003) Ca (2+)/CREB/CBPdependent gene regulation: A shared mechanism critical in long-term synaptic plasticity and neuronal survival. Cell Calcium 34, 425-430. (Pubitemid 37021234)
    • (2003) Cell Calcium , vol.34 , Issue.4-5 , pp. 425-430
    • Bito, H.1    Takemoto-Kimura, S.2
  • 126
    • 21744460229 scopus 로고    scopus 로고
    • Potential role of cAMP response element-binding protein in ethanol-induced N-methyl-D-aspartate receptor 2B subunit gene transcription in fetal mouse cortical cells
    • DOI 10.1124/mol.104.007872
    • Rani CS, Qiang M, Ticku MK (2005) Potential role ofcAMP response element-binding protein in ethanol-induced Nmethyl-D-aspartate receptor 2B subunit gene transcription in fetal mouse cortical cells. Mol Pharmacol 67, 2126-2136. (Pubitemid 41007793)
    • (2005) Molecular Pharmacology , vol.67 , Issue.6 , pp. 2126-2136
    • Rani, C.S.S.1    Qiang, M.2    Ticku, M.K.3
  • 127
    • 0942298555 scopus 로고    scopus 로고
    • Up-regulation of NMDAR1 subunit gene expression in cortical neurons via a PKA-dependent pathway
    • DOI 10.1046/j.1471-4159.2003.02156.x
    • Lau GC, Saha S, Faris R, Russek SJ (2004) Up-regulation of NMDAR1 subunit gene expression in cortical neurons via a PKA-dependent pathway. J Neurochem 88, 564-575. (Pubitemid 38140201)
    • (2004) Journal of Neurochemistry , vol.88 , Issue.3 , pp. 564-575
    • Lau, G.C.1    Saha, S.2    Faris, R.3    Russek, S.J.4
  • 128
    • 4444280871 scopus 로고    scopus 로고
    • What turns CREB on?
    • DOI 10.1016/j.cellsig.2004.05.001, PII S0898656804000804
    • Johannessen M, Delghandi MP, Moens U (2004) What turns CREB on? Cell Signal 16, 1211-1227. (Pubitemid 39165450)
    • (2004) Cellular Signalling , vol.16 , Issue.11 , pp. 1211-1227
    • Johannessen, M.1    Delghandi, M.P.2    Moens, U.3
  • 129
    • 0024445798 scopus 로고
    • Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at serine 133
    • DOI 10.1016/0092-8674(89)90013-5
    • Gonzalez GA, Montminy MR (1989) Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at serine 133. Cell 59, 675-680. (Pubitemid 19282874)
    • (1989) Cell , vol.59 , Issue.4 , pp. 675-680
    • Gonzalez, G.A.1    Montminy, M.R.2
  • 130
    • 0037333584 scopus 로고    scopus 로고
    • Cyclic AMP inhibition of tumor necrosis factor α production induced by amyloidogenic C-terminal peptide of Alzheimer's amyloid precursor protein in macrophages: Involvement of multiple intracellular pathways and cyclic AMP response element binding protein
    • DOI 10.1124/mol.63.3.690
    • Chong YH, Shin YJ, Suh YH (2003) Cyclic AMP inhibition of tumor necrosis factor alpha production induced by amyloidogenic C-terminal peptide of Alzheimer's amyloid precursor protein in macrophages: Involvement of multiple intracellular pathways and cyclic AMP response element binding protein. Mol Pharmacol 63, 690-698. (Pubitemid 36297342)
    • (2003) Molecular Pharmacology , vol.63 , Issue.3 , pp. 690-698
    • Chong, Y.H.1    Shin, Y.J.2    Suh, Y.-H.3
  • 133
    • 84856562824 scopus 로고    scopus 로고
    • Increased EID1 nuclear translocation impairs synaptic plasticity and memory function associated with pathogenesis of Alzheimer's disease
    • Liu R, Lei JX, Luo C, Lan X, Chi L, Deng P, Lei S, Ghribi O, Liu QY (2012) Increased EID1 nuclear translocation impairs synaptic plasticity and memory function associated with pathogenesis of Alzheimer's disease. Neurobiol Dis 45, 902-912.
    • (2012) Neurobiol Dis , vol.45 , pp. 902-912
    • Liu, R.1    Lei, J.X.2    Luo, C.3    Lan, X.4    Chi, L.5    Deng, P.6    Lei, S.7    Ghribi, O.8    Liu, Q.Y.9
  • 134
    • 84860217099 scopus 로고    scopus 로고
    • CREB-regulated transcription coactivator 1-dependent transcription in Alzheimer's disease mice
    • Saura CA (2012) CREB-regulated transcription coactivator 1-dependent transcription in Alzheimer's disease mice. Neurodegener Dis 10, 250-252.
    • (2012) Neurodegener Dis , vol.10 , pp. 250-252
    • Saura, C.A.1
  • 135
    • 0035907325 scopus 로고    scopus 로고
    • Beta -amyloid-(1-42) impairs activity-dependent cAMP-response element-binding protein signaling in neurons at concentrations in which cell survival Is not compromised
    • Tong L, Thornton PL, Balazs R, Cotman CW (2001) Beta -amyloid-(1-42) impairs activity-dependent cAMP-response element-binding protein signaling in neurons at concentrations in which cell survival Is not compromised. J Biol Chem 276, 17301-17306.
    • (2001) J Biol Chem , vol.276 , pp. 17301-17306
    • Tong, L.1    Thornton, P.L.2    Balazs, R.3    Cotman, C.W.4
  • 136
    • 79954573504 scopus 로고    scopus 로고
    • The role of CREB signaling in Alzheimer's disease and other cognitive disorders
    • Saura CA, Valero J (2011) The role of CREB signaling in Alzheimer's disease and other cognitive disorders. Rev Neurosci 22, 153-169.
    • (2011) Rev Neurosci , vol.22 , pp. 153-169
    • Saura, C.A.1    Valero, J.2
  • 137
    • 77249122985 scopus 로고    scopus 로고
    • Molecular network analysis suggests aberrant CREB-mediated gene regulation in the Alzheimer disease hippocampus
    • Satoh J, Tabunoki H, Arima K (2009) Molecular network analysis suggests aberrant CREB-mediated gene regulation in the Alzheimer disease hippocampus. Dis Markers 27, 239-252.
    • (2009) Dis Markers , vol.27 , pp. 239-252
    • Satoh, J.1    Tabunoki, H.2    Arima, K.3
  • 138
    • 33846633238 scopus 로고    scopus 로고
    • P300 activation by Presenilin 1 but not by its M146L mutant
    • DOI 10.1016/j.neulet.2006.11.036, PII S0304394006012523
    • Francis YI, Diss JK, Kariti M, Stephanou A, Latchman DS (2007) p300 activation by Presenilin 1 but not by its M146L mutant. Neurosci Lett 413, 137-140. (Pubitemid 46177396)
    • (2007) Neuroscience Letters , vol.413 , Issue.2 , pp. 137-140
    • Francis, Y.I.1    Diss, J.K.J.2    Kariti, M.3    Stephanou, A.4    Latchman, D.S.5
  • 139
    • 33745048523 scopus 로고    scopus 로고
    • CREB-binding protein activation by presenilin 1 but not by its M146L mutant
    • DOI 10.1097/01.wnr.0000220137.06542.a0, PII 0000175620060626000014
    • Francis YI, Stephanou A, Latchman DS (2006) CREBbinding protein activation by presenilin 1 but not by its M146L mutant. Neuroreport 17, 917-921. (Pubitemid 43869959)
    • (2006) NeuroReport , vol.17 , Issue.9 , pp. 917-921
    • Francis, Y.I.1    Stephanou, A.2    Latchman, D.S.3
  • 140
    • 78651072485 scopus 로고    scopus 로고
    • CBP gene transfer increasesBDNFlevels and ameliorates learning and memory deficits in a mouse model of Alzheimer's disease
    • Caccamo A, MaldonadoMA, BokovAF, Majumder S, Oddo S (2010) CBP gene transfer increasesBDNFlevels and ameliorates learning and memory deficits in a mouse model of Alzheimer's disease. Proc Natl Acad Sci U S A 107, 22687-22692.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 22687-22692
    • Caccamo, A.1    Maldonado, M.A.2    Bokov, A.F.3    Majumder, S.4    Oddo, S.5
  • 142
    • 78651079796 scopus 로고    scopus 로고
    • Mitochondrial transcription factor A (TFAM) polymorphisms and risk of late-onset Alzheimer's disease in Han Chinese
    • Zhang Q, Yu JT, Wang P, Chen W, Wu ZC, Jiang H, Tan L (2011) Mitochondrial transcription factor A (TFAM) polymorphisms and risk of late-onset Alzheimer's disease in Han Chinese. Brain Res 1368, 355-360.
    • (2011) Brain Res , vol.1368 , pp. 355-360
    • Zhang, Q.1    Yu, J.T.2    Wang, P.3    Chen, W.4    Wu, Z.C.5    Jiang, H.6    Tan, L.7
  • 144
    • 0037193673 scopus 로고    scopus 로고
    • Human mitochondrial transcription factor A (mtTFA): Gene structure and characterization of related pseudogenes
    • DOI 10.1016/S0378-1119(02)00600-5, PII S0378111902006005
    • Reyes A, Mezzina M, Gadaleta G (2002) Human mitochondrial transcription factor A (mtTFA): Gene structure and characterization of related pseudogenes. Gene 291, 223-232. (Pubitemid 34722392)
    • (2002) Gene , vol.291 , Issue.1-2 , pp. 223-232
    • Reyes, A.1    Mezzina, M.2    Gadaleta, G.3
  • 145
    • 28244486156 scopus 로고    scopus 로고
    • History of the Tfam gene in primates
    • DOI 10.1016/j.gene.2005.07.007, PII S0378111905003835
    • D'Errico I, Dinardo MM, Capozzi O, De Virgilio C, Gadaleta G (2005) History of the Tfam gene in primates. Gene 362, 125-132. (Pubitemid 41711192)
    • (2005) Gene , vol.362 , Issue.1-2 , pp. 125-132
    • D'Errico, I.1    Dinardo, M.M.2    Capozzi, O.3    De Virgilio, C.4    Gadaleta, G.5
  • 147
    • 78649464413 scopus 로고    scopus 로고
    • Human mitochondrial transcription factor A is required for the segregation of mitochondrial DNA in cultured cells
    • Kasashima K, Sumitani M, Endo H (2011) Human mitochondrial transcription factor A is required for the segregation of mitochondrial DNA in cultured cells. Exp Cell Res 317, 210-220.
    • (2011) Exp Cell Res , vol.317 , pp. 210-220
    • Kasashima, K.1    Sumitani, M.2    Endo, H.3
  • 149
    • 45549087482 scopus 로고    scopus 로고
    • Nuclear respiratory factor 1 controls myocyte enhancer factor 2A transcription to provide a mechanism for coordinate expression of respiratory chain subunits
    • Ramachandran B, Yu G, Gulick T (2008) Nuclear respiratory factor 1 controls myocyte enhancer factor 2A transcription to provide a mechanism for coordinate expression of respiratory chain subunits. J Biol Chem 283, 11935-11946.
    • (2008) J Biol Chem , vol.283 , pp. 11935-11946
    • Ramachandran, B.1    Yu, G.2    Gulick, T.3
  • 150
    • 69949102009 scopus 로고    scopus 로고
    • PGC-1alpha in aging and anti-aging interventions
    • Anderson R, Prolla T (2009) PGC-1alpha in aging and anti-aging interventions. Biochim Biophys Acta 1790, 1059-1066.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 1059-1066
    • Anderson, R.1    Prolla, T.2
  • 153
    • 84855687153 scopus 로고    scopus 로고
    • Impaired mitochondrial biogenesis contributes to mitochondrial dysfunction in Alzheimer's disease
    • Sheng B, Wang X, Su B, Lee HG, Casadesus G, Perry G, Zhu X (2012) Impaired mitochondrial biogenesis contributes to mitochondrial dysfunction in Alzheimer's disease. J Neurochem 120, 419-429.
    • (2012) J Neurochem , vol.120 , pp. 419-429
    • Sheng, B.1    Wang, X.2    Su, B.3    Lee, H.G.4    Casadesus, G.5    Perry, G.6    Zhu, X.7
  • 154
    • 0037326196 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-γ coactivator 1α (PGC-1α): Transcriptional coactivator and metabolic regulator
    • DOI 10.1210/er.2002-0012
    • Puigserver P, Spiegelman BM (2003) Peroxisome proliferator-activated receptor-gamma coactivator 1 alpha (PGC-1 alpha): Transcriptional coactivator and metabolic regulator. Endocr Rev 24, 78-90. (Pubitemid 36223280)
    • (2003) Endocrine Reviews , vol.24 , Issue.1 , pp. 78-90
    • Puigserver, P.1    Spiegelman, B.M.2
  • 155
    • 33644660537 scopus 로고    scopus 로고
    • PGC-1 coactivators: Inducible regulators of energy metabolism in health and disease
    • DOI 10.1172/JCI27794
    • Finck BN, Kelly DP (2006) PGC-1 coactivators: Inducible regulators of energy metabolism in health and disease. J Clin Invest 116, 615-622. (Pubitemid 43326866)
    • (2006) Journal of Clinical Investigation , vol.116 , Issue.3 , pp. 615-622
    • Finck, B.N.1    Kelly, D.P.2
  • 156
    • 33744905787 scopus 로고    scopus 로고
    • PGC-1α: A potent transcriptional cofactor involved in the pathogenesis of type 2 diabetes
    • DOI 10.1007/s00125-006-0268-6
    • Soyal S, Krempler F, Oberkofler H, Patsch W (2006) PGC-1alpha: A potent transcriptional cofactor involved in the pathogenesis of type 2 diabetes. Diabetologia 49, 1477-1488. (Pubitemid 43848083)
    • (2006) Diabetologia , vol.49 , Issue.7 , pp. 1477-1488
    • Soyal, S.1    Krempler, F.2    Oberkofler, H.3    Patsch, W.4
  • 157
    • 79957960940 scopus 로고    scopus 로고
    • Metabolic control of mitochondrial biogenesis through the PGC-1 family regulatory network
    • Scarpulla RC (2011) Metabolic control of mitochondrial biogenesis through the PGC-1 family regulatory network. Biochim Biophys Acta 1813, 1269-1278.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 1269-1278
    • Scarpulla, R.C.1
  • 162
    • 0036386911 scopus 로고    scopus 로고
    • Effects of low-intensity prolonged exercise on PGC-1 mRNA expression in rat epitrochlearis muscle
    • Terada S, Goto M, Kato M, Kawanaka K, Shimokawa T, Tabata I (2002) Effects of low-intensity prolonged exercise on PGC-1 mRNA expression in rat epitrochlearis muscle. Biochem Biophys Res Commun 296, 350-354.
    • (2002) Biochem Biophys Res Commun , vol.296 , pp. 350-354
    • Terada, S.1    Goto, M.2    Kato, M.3    Kawanaka, K.4    Shimokawa, T.5    Tabata, I.6
  • 163
    • 18144411313 scopus 로고    scopus 로고
    • SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1α
    • DOI 10.1074/jbc.M501485200
    • Nemoto S, Fergusson MM, Finkel T (2005) SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1alpha. J Biol Chem 280, 16456-16460. (Pubitemid 40616776)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.16 , pp. 16456-16460
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 164
    • 33744534726 scopus 로고    scopus 로고
    • GCN5 acetyltransferase complex controls glucose metabolism through transcriptional repression of PGC-1α
    • DOI 10.1016/j.cmet.2006.04.013, PII S1550413106001537
    • Lerin C, Rodgers JT, Kalume DE, Kim SH, Pandey A, Puigserver P (2006) GCN5 acetyltransferase complex controls glucose metabolism through transcriptional repression of PGC-1alpha. Cell Metab 3, 429-438. (Pubitemid 43811779)
    • (2006) Cell Metabolism , vol.3 , Issue.6 , pp. 429-438
    • Lerin, C.1    Rodgers, J.T.2    Kalume, D.E.3    Kim, S.-h.4    Pandey, A.5    Puigserver, P.6
  • 165
    • 0032549811 scopus 로고    scopus 로고
    • A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis
    • DOI 10.1016/S0092-8674(00)81410-5
    • Puigserver P, Wu Z, ParkCW, Graves R, Wright M, Spiegelman BM (1998) A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis. Cell 92, 829-839. (Pubitemid 28155321)
    • (1998) Cell , vol.92 , Issue.6 , pp. 829-839
    • Puigserver, P.1    Wu, Z.2    Park, C.W.3    Graves, R.4    Wright, M.5    Spiegelman, B.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.