메뉴 건너뛰기




Volumn , Issue , 2012, Pages

Mitochondrial- and endoplasmic reticulum-associated oxidative stress in alzheimers disease: From pathogenesis to biomarkers

Author keywords

[No Author keywords available]

Indexed keywords

4 HYDROXYNONENAL; 4 PHENYLBUTYRIC ACID; ACETYL LEVO CARNITINE CARNITINE; ALPHA TOCOPHEROL; ALPHA TOCOPHEROL PLUS TRIPHENYLPHOSPHONIUM; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; ANTIOXIDANT; BIOLOGICAL MARKER; CALCIUM; CATALASE; DANTROLENE; DIMEBON; DIZOCILPINE; GLUTATHIONE; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; IFENPRODIL; ISOPROSTANE DERIVATIVE; MALONALDEHYDE; MEMANTINE; MITOCHONDRIAL PROTEIN; MITOQUINONE MESYLATE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; REACTIVE OXYGEN METABOLITE; SCHILLER PEPTIDE; SUPEROXIDE DISMUTASE; UNCLASSIFIED DRUG; XESTOSPONGIN C;

EID: 84863688106     PISSN: 16878876     EISSN: 16878884     Source Type: Journal    
DOI: 10.1155/2012/735206     Document Type: Review
Times cited : (128)

References (292)
  • 1
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy J., Selkoe D. J., The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics Science 2002 297 5580 353 356 (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 2
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer's Disease with plaques and tangles: Intracellular A and synaptic dysfunction
    • DOI 10.1016/S0896-6273(03)00434-3
    • Oddo S., Caccamo A., Shepherd J. D., Murphy M. P., Golde T. E., Kayed R., Metherate R., Mattson M. P., Akbari Y., LaFerla F. M., Triple-transgenic model of Alzheimer's Disease with plaques and tangles: intracellular A and synaptic dysfunction Neuron 2003 39 3 409 421 (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
  • 3
    • 80053892506 scopus 로고    scopus 로고
    • Brain aging, Alzheimer's disease, and mitochondria
    • Swerdlow R. H., Brain aging, Alzheimer's disease, and mitochondria Biochimica et Biophysica Acta 2011 1812 12 1630 1639
    • (2011) Biochimica et Biophysica Acta , vol.1812 , Issue.12 , pp. 1630-1639
    • Swerdlow, R.H.1
  • 5
    • 84860868174 scopus 로고    scopus 로고
    • Role of WWOX/WOX1 in Alzheimer's disease pathology and in cell death signaling
    • Teng C. C., Yang Y. T., Chen Y. C., Kuo Y. M., Sze C. I., Role of WWOX/WOX1 in Alzheimer's disease pathology and in cell death signaling Frontiers in Bioscience 2012 4 1951 1965
    • (2012) Frontiers in Bioscience , vol.4 , pp. 1951-1965
    • Teng, C.C.1    Yang, Y.T.2    Chen, Y.C.3    Kuo, Y.M.4    Sze, C.I.5
  • 6
    • 0033954991 scopus 로고    scopus 로고
    • Oxidative stress and Alzheimer disease
    • Christen Y., Oxidative stress and Alzheimer disease American Journal of Clinical Nutrition 2000 71 2 621S 629S (Pubitemid 30061247)
    • (2000) American Journal of Clinical Nutrition , vol.71 , Issue.2
    • Christen, Y.1
  • 7
    • 33846243745 scopus 로고    scopus 로고
    • An integrated view of oxidative stress in aging: Basic mechanisms, functional effects, and pathological considerations
    • Kregel K. C., Zhang H. J., An integrated view of oxidative stress in aging: basic mechanisms, functional effects, and pathological considerations American Journal of Physiology 2007 292 1 R18 R36
    • (2007) American Journal of Physiology , vol.292 , Issue.1
    • Kregel, K.C.1    Zhang, H.J.2
  • 9
    • 3042513691 scopus 로고    scopus 로고
    • Mitochondria dysfunction of Alzheimer's disease cybrids enhances A toxicity
    • DOI 10.1111/j.1471-4159.2004.02438.x
    • Cardoso S. M., Santana I., Swerdlow R. H., Oliveira C. R., Mitochondria dysfunction of Alzheimer's disease cybrids enhances A toxicity Journal of Neurochemistry 2004 89 6 1417 1426 (Pubitemid 38802663)
    • (2004) Journal of Neurochemistry , vol.89 , Issue.6 , pp. 1417-1426
    • Cardoso, S.M.1    Santana, I.2    Swerdlow, R.H.3    Oliveira, C.R.4
  • 11
    • 0029073455 scopus 로고
    • Elevated thiobarbituric acid-reactive substances and antioxidant enzyme activity in the brain in Alzheimer's disease
    • Lovell M. A., Ehmann W. D., Butler S. M., Markesbery W. R., Elevated thiobarbituric acid-reactive substances and antioxidant enzyme activity in the brain in Alzheimer's disease Neurology 1995 45 8 1594 1601
    • (1995) Neurology , vol.45 , Issue.8 , pp. 1594-1601
    • Lovell, M.A.1    Ehmann, W.D.2    Butler, S.M.3    Markesbery, W.R.4
  • 15
    • 0031980065 scopus 로고    scopus 로고
    • Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease
    • DOI 10.1016/S0197-4580(98)00009-8, PII S0197458098000098
    • Markesbery W. R., Lovell M. A., Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease Neurobiology of Aging 1998 19 1 33 36 (Pubitemid 28167792)
    • (1998) Neurobiology of Aging , vol.19 , Issue.1 , pp. 33-36
    • Markesbery, W.R.1    Lovell, M.A.2
  • 16
    • 0031028437 scopus 로고    scopus 로고
    • Immunohistochemical detection of 4-hydroxy-2-nonenal adducts in Alzheimer's disease is associated with inheritance of APOE4
    • Montine K. S., Oison S. J., Amarnath V., Whetsell W. O., Graham D. G., Montine T. J., Immunohistochemical detection of 4-hydroxy-2-nonenal adducts in Alzheimer's disease is associated with inheritance of APOE4 American Journal of Pathology 1997 150 2 437 443 (Pubitemid 27073773)
    • (1997) American Journal of Pathology , vol.150 , Issue.2 , pp. 437-443
    • Montine, K.S.1    Oison, S.J.2    Amarnath, V.3    Whetsell Jr., W.O.4    Graham, D.G.5    Montine, T.J.6
  • 17
    • 33644987632 scopus 로고    scopus 로고
    • Elevated protein-bound levels of the lipid peroxidation product, 4-hydroxy-2-nonenal, in brain from persons with mild cognitive impairment
    • Butterfield D. A., Reed T., Perluigi M., De Marco C., Coccia R., Cini C., Sultana R., Elevated protein-bound levels of the lipid peroxidation product, 4-hydroxy-2-nonenal, in brain from persons with mild cognitive impairment Neuroscience Letters 2006 397 3 170 173
    • (2006) Neuroscience Letters , vol.397 , Issue.3 , pp. 170-173
    • Butterfield, D.A.1    Reed, T.2    Perluigi, M.3    De Marco, C.4    Coccia, R.5    Cini, C.6    Sultana, R.7
  • 18
    • 33646144212 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: Insights into the development of Alzheimer's disease
    • Butterfield D. A., Poon H. F., Clair D. S., Keller J. N., Pierce W. M., Klein J. B., Markesbery W. R., Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: insights into the development of Alzheimer's disease Neurobiology of Disease 2006 22 2 223 232
    • (2006) Neurobiology of Disease , vol.22 , Issue.2 , pp. 223-232
    • Butterfield, D.A.1    Poon, H.F.2    Clair, D.S.3    Keller, J.N.4    Pierce, W.M.5    Klein, J.B.6    Markesbery, W.R.7
  • 19
    • 33744935554 scopus 로고    scopus 로고
    • Increased levels of 4-hydroxynonenal and acrolein, neurotoxic markers of lipid peroxidation, in the brain in Mild Cognitive Impairment and early Alzheimer's disease
    • DOI 10.1016/j.neurobiolaging.2005.06.004, PII S0197458005001740
    • Williams T. I., Lynn B. C., Markesbery W. R., Lovell M. A., Increased levels of 4-hydroxynonenal and acrolein, neurotoxic markers of lipid peroxidation, in the brain in Mild Cognitive Impairment and early Alzheimer's disease Neurobiology of Aging 2006 27 8 1094 1099 (Pubitemid 43850642)
    • (2006) Neurobiology of Aging , vol.27 , Issue.8 , pp. 1094-1099
    • Williams, T.I.1    Lynn, B.C.2    Markesbery, W.R.3    Lovell, M.A.4
  • 20
    • 0032238783 scopus 로고    scopus 로고
    • 2-isoprostanes in Alzheimer's disease: Evidence for enhanced lipid peroxidation in vivo
    • Pratic D., Lee V. M. Y., Trojanowski J. Q., Rokach J., Fitzgerald G. A., Increased F2-isoprostanes in Alzheimer's disease: evidence for enhanced lipid peroxidation in vivo The FASEB Journal 1998 12 15 1777 1783 (Pubitemid 28553673)
    • (1998) FASEB Journal , vol.12 , Issue.15 , pp. 1777-1783
    • Pratico, D.1    Lee, V.M.-Y.2    Trojanowski, J.Q.3    Rokach, J.4    Fitzgerald, G.A.5
  • 22
    • 0035144956 scopus 로고    scopus 로고
    • Brain regional quantification of F-ring and D-/E-ring isoprostanes and neuroprostanes in Alzheimer's disease
    • Reich E. E., Markesbery W. R., Roberts L. J., Swift L. L., Morrow J. D., Montine T. J., Brain regional quantification of F-ring and D-/E-ring isoprostanes and neuroprostanes in Alzheimer's disease American Journal of Pathology 2001 158 1 293 297 (Pubitemid 32096495)
    • (2001) American Journal of Pathology , vol.158 , Issue.1 , pp. 293-297
    • Reich, E.E.1    Markesbery, W.R.2    Roberts II, L.J.3    Swift, L.L.4    Morrow, J.D.5    Montine, T.J.6
  • 23
    • 27644446857 scopus 로고    scopus 로고
    • Lipid peroxidation is an early event in the brain in amnestic mild cognitive impairment
    • DOI 10.1002/ana.20629
    • Markesbery W. R., Kryscio R. J., Lovell M. A., Morrow J. D., Lipid peroxidation is an early event in the brain in amnestic mild cognitive impairment Annals of Neurology 2005 58 5 730 735 (Pubitemid 41552548)
    • (2005) Annals of Neurology , vol.58 , Issue.5 , pp. 730-735
    • Markesbery, W.R.1    Kryscio, R.J.2    Lovell, M.A.3    Morrow, J.D.4
  • 24
    • 33947503437 scopus 로고    scopus 로고
    • Cortical biochemistry in MCI and Alzheimer disease: Lack of correlation with clinical diagnosis
    • DOI 10.1212/01.wnl.0000256373.39415.b1, PII 0000611420070306000012
    • Forman M. S., Mufson E. J., Leurgans S., Pratico D., Joyce S., Leight S., Lee V. M. Y., Trojanowski J. Q., Cortical biochemistry in MCI and Alzheimer disease: lack of correlation with clinical diagnosis Neurology 2007 68 10 757 763 (Pubitemid 46667901)
    • (2007) Neurology , vol.68 , Issue.10 , pp. 757-763
    • Forman, M.S.1    Mufson, E.J.2    Leurgans, S.3    Pratico, D.4    Joyce, S.5    Leight, S.6    Lee, V.M.-Y.7    Trojanowski, J.Q.8
  • 26
    • 0030898724 scopus 로고    scopus 로고
    • An assessment of oxidative damage to proteins, lipids, and DNA in brain from patients with Alzheimer's disease
    • Lyras L., Cairns N. J., Jenner A., Jenner P., Halliwell B., An assessment of oxidative damage to proteins, lipids, and DNA in brain from patients with Alzheimer's disease Journal of Neurochemistry 1997 68 5 2061 2069 (Pubitemid 27176143)
    • (1997) Journal of Neurochemistry , vol.68 , Issue.5 , pp. 2061-2069
    • Lyras, L.1    Cairns, N.J.2    Jenner, A.3    Jenner, P.4    Halliwell, B.5
  • 28
    • 34247142905 scopus 로고    scopus 로고
    • Elevated levels of 3-nitrotyrosine in brain from subjects with amnestic mild cognitive impairment: Implications for the role of nitration in the progression of Alzheimer's disease
    • DOI 10.1016/j.brainres.2007.02.084, PII S0006899307004222
    • Butterfield D. A., Reed T. T., Perluigi M., De Marco C., Coccia R., Keller J. N., Markesbery W. R., Sultana R., Elevated levels of 3-nitrotyrosine in brain from subjects with amnestic mild cognitive impairment: implications for the role of nitration in the progression of Alzheimer's disease Brain Research 2007 1148 1 243 248 (Pubitemid 46602178)
    • (2007) Brain Research , vol.1148 , Issue.1 , pp. 243-248
    • Butterfield, D.A.1    Reed, T.T.2    Perluigi, M.3    De Marco, C.4    Coccia, R.5    Keller, J.N.6    Markesbery, W.R.7    Sultana, R.8
  • 29
    • 70449411818 scopus 로고    scopus 로고
    • Oxidatively modified, mitochondria-relevant brain proteins in subjects with Alzheimer disease and mild cognitive impairment
    • Sultana R., Butterfield D. A., Oxidatively modified, mitochondria- relevant brain proteins in subjects with Alzheimer disease and mild cognitive impairment Journal of Bioenergetics and Biomembranes 2009 41 5 441 446
    • (2009) Journal of Bioenergetics and Biomembranes , vol.41 , Issue.5 , pp. 441-446
    • Sultana, R.1    Butterfield, D.A.2
  • 31
    • 33748423353 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidized proteins in Alzheimer's disease hippocampus and cerebellum: An approach to understand pathological and biochemical alterations in AD
    • DOI 10.1016/j.neurobiolaging.2005.09.021, PII S0197458005002915
    • Sultana R., Boyd-Kimball D., Poon H. F., Cai J., Pierce W. M., Klein J. B., Merchant M., Markesbery W. R., Butterfield D. A., Redox proteomics identification of oxidized proteins in Alzheimer's disease hippocampus and cerebellum: an approach to understand pathological and biochemical alterations in AD Neurobiology of Aging 2006 27 11 1564 1576 (Pubitemid 44344840)
    • (2006) Neurobiology of Aging , vol.27 , Issue.11 , pp. 1564-1576
    • Sultana, R.1    Boyd-Kimball, D.2    Poon, H.F.3    Cai, J.4    Pierce, W.M.5    Klein, J.B.6    Merchant, M.7    Markesbery, W.R.8    Butterfield, D.A.9
  • 32
    • 40849120274 scopus 로고    scopus 로고
    • Redox proteomic identification of 4-Hydroxy-2-nonenal-modified brain proteins in amnestic mild cognitive impairment: Insight into the role of lipid peroxidation in the progression and pathogenesis of Alzheimer's disease
    • Reed T., Perluigi M., Sultana R., Pierce W. M., Klein J. B., Turner D. M., Coccia R., Markesbery W. R., Butterfield D. A., Redox proteomic identification of 4-Hydroxy-2-nonenal-modified brain proteins in amnestic mild cognitive impairment: insight into the role of lipid peroxidation in the progression and pathogenesis of Alzheimer's disease Neurobiology of Disease 2008 30 1 107 120
    • (2008) Neurobiology of Disease , vol.30 , Issue.1 , pp. 107-120
    • Reed, T.1    Perluigi, M.2    Sultana, R.3    Pierce, W.M.4    Klein, J.B.5    Turner, D.M.6    Coccia, R.7    Markesbery, W.R.8    Butterfield, D.A.9
  • 33
    • 0029976253 scopus 로고    scopus 로고
    • DNA damage and apoptosis in Alzheimer's disease: Colocalization with c-Jun immunoreactivity, relationship to brain area, and effect of postmortem delay
    • Anderson A. J., Su J. H., Cotman C. W., DNA damage and apoptosis in Alzheimer's disease: colocalization with c-Jun immunoreactivity, relationship to brain area, and effect of postmortem delay Journal of Neuroscience 1996 16 5 1710 1719
    • (1996) Journal of Neuroscience , vol.16 , Issue.5 , pp. 1710-1719
    • Anderson, A.J.1    Su, J.H.2    Cotman, C.W.3
  • 34
    • 0041846404 scopus 로고    scopus 로고
    • Quantitative assessment of DNA fragmentation and beta-amyloid deposition in insular cortex and midfrontal gyrus from patients with Alzheimer's disease
    • DOI 10.1016/S0024-3205(03)00512-5
    • Colurso G. J., Nilson J. E., Vervoort L. G., Quantitative assessment of DNA fragmentation and beta-amyloid deposition in insular cortex and midfrontal gyrus from patients with Alzheimer's disease Life Sciences 2003 73 14 1795 1803 (Pubitemid 36897740)
    • (2003) Life Sciences , vol.73 , Issue.14 , pp. 1795-1803
    • Colurso, G.J.1    Nilson, J.E.2    Vervoort, L.G.3
  • 35
    • 0030806869 scopus 로고    scopus 로고
    • DNA damage distribution in the human brain as shown by in situ end labeling; area-specific differences in aging and Alzheimer disease in the absence of apoptotic morphology
    • Lucassen P. J., Chung W. C. J., Kamphorst W., Swaab D. F., DNA damage distribution in the human brain as shown by in situ end labeling; area-specific differences in aging and Alzheimer disease in the absence of apoptotic morphology Journal of Neuropathology and Experimental Neurology 1997 56 8 887 900 (Pubitemid 27329110)
    • (1997) Journal of Neuropathology and Experimental Neurology , vol.56 , Issue.8 , pp. 887-900
    • Lucassen, P.J.1    Chung, W.C.J.2    Kamphorst, W.3    Swaab, D.F.4
  • 36
    • 0032734510 scopus 로고    scopus 로고
    • DNA strand breaks in Alzheimer's disease
    • Adamec E., Vonsattel J. P., Nixon R. A., DNA strand breaks in Alzheimer's disease Brain Research 1999 849 1-2 67 77
    • (1999) Brain Research , vol.849 , Issue.12 , pp. 67-77
    • Adamec, E.1    Vonsattel, J.P.2    Nixon, R.A.3
  • 37
    • 0028152717 scopus 로고
    • Oxidative damage to mitochondrial DNA is increased in Alzheimer's disease
    • DOI 10.1002/ana.410360510
    • Mecocci P., MacGarvey U., Beal M. F., Oxidative damage to mitochondrial DNA is increased in Alzheimer's disease Annals of Neurology 1994 36 5 747 751 (Pubitemid 24337634)
    • (1994) Annals of Neurology , vol.36 , Issue.5 , pp. 747-751
    • Mecocci, P.1    MacGarvey, U.2    Beal, M.F.3
  • 39
    • 33645106680 scopus 로고    scopus 로고
    • Increased oxidative damage in nuclear and mitochondrial DNA in mild cognitive impairment
    • Wang J., Markesbery W. R., Lovell M. A., Increased oxidative damage in nuclear and mitochondrial DNA in mild cognitive impairment Journal of Neurochemistry 2006 96 3 825 832
    • (2006) Journal of Neurochemistry , vol.96 , Issue.3 , pp. 825-832
    • Wang, J.1    Markesbery, W.R.2    Lovell, M.A.3
  • 41
    • 0038417076 scopus 로고    scopus 로고
    • The identification and characterization of oxidized RNAs in Alzheimer's disease
    • Shan X., Tashiro H., Lin C. L. G., The identification and characterization of oxidized RNAs in Alzheimer's disease Journal of Neuroscience 2003 23 12 4913 4921 (Pubitemid 36793217)
    • (2003) Journal of Neuroscience , vol.23 , Issue.12 , pp. 4913-4921
    • Shan, X.1    Tashiro, H.2    Lin, C.-L.G.3
  • 42
    • 33645961571 scopus 로고    scopus 로고
    • Quantification of oxidized RNAs in Alzheimer's disease
    • Shan X., Lin C. L. G., Quantification of oxidized RNAs in Alzheimer's disease Neurobiology of Aging 2006 27 5 657 662
    • (2006) Neurobiology of Aging , vol.27 , Issue.5 , pp. 657-662
    • Shan, X.1    Lin, C.L.G.2
  • 43
    • 38149087424 scopus 로고    scopus 로고
    • Oxidatively modified RNA in mild cognitive impairment
    • Lovell M. A., Markesbery W. R., Oxidatively modified RNA in mild cognitive impairment Neurobiology of Disease 2008 29 2 169 175
    • (2008) Neurobiology of Disease , vol.29 , Issue.2 , pp. 169-175
    • Lovell, M.A.1    Markesbery, W.R.2
  • 44
    • 75949121583 scopus 로고    scopus 로고
    • Oxidative stress in the progression of alzheimer disease in the frontal cortex
    • Ansari M. A., Scheff S. W., Oxidative stress in the progression of alzheimer disease in the frontal cortex Journal of Neuropathology and Experimental Neurology 2010 69 2 155 167
    • (2010) Journal of Neuropathology and Experimental Neurology , vol.69 , Issue.2 , pp. 155-167
    • Ansari, M.A.1    Scheff, S.W.2
  • 45
    • 79957935719 scopus 로고    scopus 로고
    • NADPH-oxidase activation and cognition in Alzheimer disease progression
    • Ansari M. A., Scheff S. W., NADPH-oxidase activation and cognition in Alzheimer disease progression Free Radical Biology and Medicine 2011 51 1 171 178
    • (2011) Free Radical Biology and Medicine , vol.51 , Issue.1 , pp. 171-178
    • Ansari, M.A.1    Scheff, S.W.2
  • 46
    • 56349091788 scopus 로고    scopus 로고
    • Protein levels and activity of some antioxidant enzymes in hippocampus of subjects with amnestic mild cognitive impairment
    • Sultana R., Piroddi M., Galli F., Butterfield D. A., Protein levels and activity of some antioxidant enzymes in hippocampus of subjects with amnestic mild cognitive impairment Neurochemical Research 2008 33 12 2540 2546
    • (2008) Neurochemical Research , vol.33 , Issue.12 , pp. 2540-2546
    • Sultana, R.1    Piroddi, M.2    Galli, F.3    Butterfield, D.A.4
  • 48
    • 84857922100 scopus 로고    scopus 로고
    • Cytochrome c oxidase and nitric oxide in action: Molecular mechanisms and pathophysiological implications
    • Sarti P., Forte E., Mastronicola D., Giuffre A., Arese M., Cytochrome c oxidase and nitric oxide in action: molecular mechanisms and pathophysiological implications Biochimica et Biophysica Acta 2012 1817 4 610 619
    • (2012) Biochimica et Biophysica Acta , vol.1817 , Issue.4 , pp. 610-619
    • Sarti, P.1    Forte, E.2    Mastronicola, D.3    Giuffre, A.4    Arese, M.5
  • 49
    • 81855204961 scopus 로고    scopus 로고
    • Oxidative stress in health and disease: The therapeutic potential of Nrf2 activation
    • Hybertson B. M., Gao B., Bose S. K., McCord J. M., Oxidative stress in health and disease: the therapeutic potential of Nrf2 activation Molecular Aspects of Medicine 2011 32 46 234 246
    • (2011) Molecular Aspects of Medicine , vol.32 , Issue.46 , pp. 234-246
    • Hybertson, B.M.1    Gao, B.2    Bose, S.K.3    McCord, J.M.4
  • 51
    • 7244236841 scopus 로고    scopus 로고
    • A modified -amyloid hypothesis: Intraneuronal accumulation of the -amyloid peptide - The first step of a fatal cascade
    • DOI 10.1111/j.1471-4159.2004.02737.x
    • Wirths O., Multhaup G., Bayer T. A., A modified -amyloid hypothesis: intraneuronal accumulation of the -amyloid peptidethe first step of a fatal cascade Journal of Neurochemistry 2004 91 3 513 520 (Pubitemid 39431147)
    • (2004) Journal of Neurochemistry , vol.91 , Issue.3 , pp. 513-520
    • Wirths, O.1    Multhaup, G.2    Bayer, T.A.3
  • 52
    • 0037066072 scopus 로고    scopus 로고
    • 1-42 in neurons is facilitated by the 7 nicotinic acetylcholine receptor in Alzheimer's disease
    • DOI 10.1016/S0306-4522(01)00460-2, PII S0306452201004602
    • Nagele R. G., D'Andrea M. R., Anderson W. J., Wang H. Y., Intracellular accumulation of -amyloid142 in neurons is facilitated by the 7 nicotinic acetylcholine receptor in Alzheimer's disease Neuroscience 2002 110 2 199 211 (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
  • 53
    • 28744449206 scopus 로고    scopus 로고
    • Mitochondrial A: A potential focal point for neuronal metabolic dysfunction in Alzheimer's disease
    • DOI 10.1096/fj.05-3735fje
    • Caspersen C., Wang N., Yao J., Sosunov A., Chen X., Lustbader J. W., Xu H. W., Stern D., McKhann G., Yan S. D., Mitochondrial A : a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease The FASEB Journal 2005 19 14 2040 2041 (Pubitemid 41759758)
    • (2005) FASEB Journal , vol.19 , Issue.14 , pp. 2040-2041
    • Caspersen, C.1    Wang, N.2    Yao, J.3    Sosunov, A.4    Chen, X.5    Lustbader, J.W.6    Xu, H.W.7    Stern, D.8    McKhann, G.9    Yan, S.D.10
  • 56
    • 0032917662 scopus 로고    scopus 로고
    • The activity of the pentose phosphate pathway is increased in response to oxidative stress in Alzheimer's disease
    • DOI 10.1007/s007020050161
    • Palmer A. M., The activity of the pentose phosphate pathway is increased in response to oxidative stress in Alzheimer's disease Journal of Neural Transmission 1999 106 3-4 317 328 (Pubitemid 29196935)
    • (1999) Journal of Neural Transmission , vol.106 , Issue.3-4 , pp. 317-328
    • Palmer, A.M.1
  • 57
    • 0348111546 scopus 로고    scopus 로고
    • Cytochrome c oxidase is decreased in Alzheimer's disease platelets
    • DOI 10.1016/S0197-4580(03)00033-2
    • Cardoso S. M., Proena M. T., Santos S., Santana I., Oliveira C. R., Cytochrome c oxidase is decreased in Alzheimer's disease platelets Neurobiology of Aging 2004 25 1 105 110 (Pubitemid 37522198)
    • (2004) Neurobiology of Aging , vol.25 , Issue.1 , pp. 105-110
    • Cardoso, S.M.1    Proenca, M.T.2    Santos, S.3    Santana, I.4    Oliveira, C.R.5
  • 58
    • 0027340729 scopus 로고
    • 3-sensitive channels that are sensed by neighboring mitochondria
    • Rizzuto R., Brini M., Murgia M., Pozzan T., Microdomains with high Ca 2+ close to IP 3 -sensitive channels that are sensed by neighboring mitochondria Science 1993 262 5134 744 747 (Pubitemid 23350694)
    • (1993) Science , vol.262 , Issue.5134 , pp. 744-747
    • Rizzuto, R.1    Brini, M.2    Murgia, M.3    Pozzan, T.4
  • 61
    • 84863653832 scopus 로고    scopus 로고
    • The interface between cytoskeletal aberrations and mitochondrial dysfunction in Alzheimer's disease and related disorders
    • Kang D. E., Roh S. E., Woo J. A., Liu T., Bu J. H., Jung A. R., Lim Y., The interface between cytoskeletal aberrations and mitochondrial dysfunction in Alzheimer's disease and related disorders Experimental Neurobiology 2011 20 2 67 80
    • (2011) Experimental Neurobiology , vol.20 , Issue.2 , pp. 67-80
    • Kang, D.E.1    Roh, S.E.2    Woo, J.A.3    Liu, T.4    Bu, J.H.5    Jung, A.R.6    Lim, Y.7
  • 62
    • 80155148269 scopus 로고    scopus 로고
    • The mitochondria-targeted antioxidant MitoQ prevents loss of spatial memory retention and early neuropathology in a transgenic mouse model of Alzheimer's disease
    • McManus M. J., Murphy M. P., Franklin J. L., The mitochondria-targeted antioxidant MitoQ prevents loss of spatial memory retention and early neuropathology in a transgenic mouse model of Alzheimer's disease The Journal of Neuroscience 2011 31 44 15703 15715
    • (2011) The Journal of Neuroscience , vol.31 , Issue.44 , pp. 15703-15715
    • McManus, M.J.1    Murphy, M.P.2    Franklin, J.L.3
  • 63
    • 77953024447 scopus 로고    scopus 로고
    • Analysis of microdissected human neurons by a sensitive ELISA reveals a correlation between elevated intracellular concentrations of A 42 and Alzheimer's disease neuropathology
    • Hashimoto M., Bogdanovic N., Volkmann I., Aoki M., Winblad B., Tjernberg L. O., Analysis of microdissected human neurons by a sensitive ELISA reveals a correlation between elevated intracellular concentrations of A 42 and Alzheimer's disease neuropathology Acta Neuropathologica 2010 119 5 543 554
    • (2010) Acta Neuropathologica , vol.119 , Issue.5 , pp. 543-554
    • Hashimoto, M.1    Bogdanovic, N.2    Volkmann, I.3    Aoki, M.4    Winblad, B.5    Tjernberg, L.O.6
  • 64
    • 0035780141 scopus 로고    scopus 로고
    • Amyloid -peptide promotes permeability transition pore in brain mitochondria
    • Moreira P. I., Santos M. S., Moreno A., Oliveira C., Amyloid -peptide promotes permeability transition pore in brain mitochondria Bioscience Reports 2001 21 6 789 800
    • (2001) Bioscience Reports , vol.21 , Issue.6 , pp. 789-800
    • Moreira, P.I.1    Santos, M.S.2    Moreno, A.3    Oliveira, C.4
  • 65
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of A accumulation in Alzheimer's disease neurons: Implications for free radical generation and oxidative damage in disease progression
    • Manczak M., Anekonda T. S., Henson E., Park B. S., Quinn J., Reddy P. H., Mitochondria are a direct site of A accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression Human Molecular Genetics 2006 15 9 1437 1449
    • (2006) Human Molecular Genetics , vol.15 , Issue.9 , 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
    • 0036272650 scopus 로고    scopus 로고
    • Amyloid inhibits integrated mitochondrial respiration and key enzyme activities
    • DOI 10.1046/j.0022-3042.2001.00681.x
    • Casley C. S., Canevari L., Land J. M., Clark J. B., Sharpe M. A., -Amyloid inhibits integrated mitochondrial respiration and key enzyme activities Journal of Neurochemistry 2002 80 1 91 100 (Pubitemid 34614581)
    • (2002) Journal of Neurochemistry , vol.80 , Issue.1 , pp. 91-100
    • Casley, C.S.1    Canevari, L.2    Land, J.M.3    Clark, J.B.4    Sharpe, M.A.5
  • 67
    • 67650732998 scopus 로고    scopus 로고
    • Impaired balance of mitochondrial fission and fusion in Alzheimer's disease
    • Wang X., Su B., Lee H. G., Li X., Perry G., Smith M. A., Zhu X., Impaired balance of mitochondrial fission and fusion in Alzheimer's disease Journal of Neuroscience 2009 29 28 9090 9103
    • (2009) Journal of Neuroscience , vol.29 , Issue.28 , pp. 9090-9103
    • Wang, X.1    Su, B.2    Lee, H.G.3    Li, X.4    Perry, G.5    Smith, M.A.6    Zhu, X.7
  • 68
    • 24644456470 scopus 로고    scopus 로고
    • Calcium dysregulation in Alzheimer's disease: Recent advances gained from genetically modified animals
    • DOI 10.1016/j.ceca.2005.06.021, PII S0143416005001089
    • Smith I. F., Green K. N., LaFerla F. M., Calcium dysregulation in Alzheimer's disease: recent advances gained from genetically modified animals Cell Calcium 2005 38 3-4 427 437 (Pubitemid 41283281)
    • (2005) Cell Calcium , vol.38 , Issue.3-4 SPEC. ISS. , pp. 427-437
    • Smith, I.F.1    Green, K.N.2    LaFerla, F.M.3
  • 70
    • 72149118206 scopus 로고    scopus 로고
    • Mitochondrial permeability transition pore in Alzheimer's disease: Cyclophilin D and amyloid beta
    • Du H., Yan S. S., Mitochondrial permeability transition pore in Alzheimer's disease: cyclophilin D and amyloid beta Biochimica et Biophysica Acta 2010 1802 1 198 204
    • (2010) Biochimica et Biophysica Acta , vol.1802 , Issue.1 , pp. 198-204
    • Du, H.1    Yan, S.S.2
  • 71
    • 33745268224 scopus 로고    scopus 로고
    • Different conformations of amyloid da Cruz e Silva E.Finduce neurotoxicity by distinct mechanisms in human cortical neurons
    • DOI 10.1523/JNEUROSCI.1189-06.2006
    • Deshpande A., Mina E., Glabe C., Busciglio J., Different conformations of amyloid induce neurotoxicity by distinct mechanisms in human cortical neurons Journal of Neuroscience 2006 26 22 6011 6018 (Pubitemid 44318367)
    • (2006) Journal of Neuroscience , vol.26 , Issue.22 , pp. 6011-6018
    • Deshpande, A.1    Mina, E.2    Glabe, C.3    Busciglio, J.4
  • 72
    • 39149122810 scopus 로고    scopus 로고
    • Amyloid beta, mitochondrial dysfunction and synaptic damage: Implications for cognitive decline in aging and Alzheimer's disease
    • Reddy P. H., Beal M. F., Amyloid beta, mitochondrial dysfunction and synaptic damage: implications for cognitive decline in aging and Alzheimer's disease Trends in Molecular Medicine 2008 14 2 45 53
    • (2008) Trends in Molecular Medicine , vol.14 , Issue.2 , pp. 45-53
    • Reddy, P.H.1    Beal, M.F.2
  • 74
    • 36549064191 scopus 로고    scopus 로고
    • Bcl-2 overexpression protects against amyloid-beta and prion toxicity in GT1-7 neural cells
    • Ferreiro E., Eufrsio A., Pereira C., Oliveira C. R., Rego A. C., Bcl-2 overexpression protects against amyloid-beta and prion toxicity in GT1-7 neural cells Journal of Alzheimer's Disease 2007 12 3 223 228 (Pubitemid 350179253)
    • (2007) Journal of Alzheimer's Disease , vol.12 , Issue.3 , pp. 223-228
    • Ferreiro, E.1    Eufrasio, A.2    Pereira, C.3    Oliveira, C.R.4    Rego, A.C.5
  • 75
    • 41149176407 scopus 로고    scopus 로고
    • Lack of pathology in a triple transgenic mouse model of Alzheimer's disease after overexpression of the anti-apoptotic protein Bcl-2
    • DOI 10.1523/JNEUROSCI.5620-07.2008
    • Rohn T. T., Vyas V., Hernandez-Estrada T., Nichol K. E., Christie L. A., Head E., Lack of pathology in a triple transgenic mouse model of Alzheimer's disease after overexpression of the anti-apoptotic protein Bcl-2 Journal of Neuroscience 2008 28 12 3051 3059 (Pubitemid 351442294)
    • (2008) Journal of Neuroscience , vol.28 , Issue.12 , pp. 3051-3059
    • Rohn, T.T.1    Vyas, V.2    Hernandez-Estrada, T.3    Nichol, K.E.4    Christie, L.-A.5    Head, E.6
  • 76
    • 81555195711 scopus 로고    scopus 로고
    • Mitochondria are related to synaptic pathology in Alzheimer's disease
    • Baloyannis S. J., Mitochondria are related to synaptic pathology in Alzheimer's disease International Journal of Alzheimer's Disease 2011 2011 7
    • (2011) International Journal of Alzheimer's Disease , vol.2011 , pp. 7
    • Baloyannis, S.J.1
  • 77
    • 79751537405 scopus 로고    scopus 로고
    • Amyloid beta impairs mitochondrial anterograde transport and degenerates synapses in Alzheimer's disease neurons
    • Calkins M. J., Reddy P. H., Amyloid beta impairs mitochondrial anterograde transport and degenerates synapses in Alzheimer's disease neurons Biochimica et Biophysica Acta 2011 1812 4 507 513
    • (2011) Biochimica et Biophysica Acta , vol.1812 , Issue.4 , pp. 507-513
    • Calkins, M.J.1    Reddy, P.H.2
  • 78
    • 33744964144 scopus 로고    scopus 로고
    • 2+ overload than nonsynaptic mitochondria
    • DOI 10.1074/jbc.M510303200
    • Brown M. R., Sullivan P. G., Geddes J. W., Synaptic mitochondria are more susceptible to Ca 2+ overload than nonsynaptic mitochondria Journal of Biological Chemistry 2006 281 17 11658 11668 (Pubitemid 43855423)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.17 , pp. 11658-11668
    • Brown, M.R.1    Sullivan, P.G.2    Geddes, J.W.3
  • 79
    • 0032487648 scopus 로고    scopus 로고
    • Amyloid -peptide induces apoptosis-related events in synapses and dendrites
    • DOI 10.1016/S0006-8993(98)00763-X, PII S000689939800763X
    • Mattson M. P., Partin J., Begley J. G., Amyloid -peptide induces apoptosis-related events in synapses and dendrites Brain Research 1998 807 1-2 167 176 (Pubitemid 29005249)
    • (1998) Brain Research , vol.807 , Issue.1-2 , pp. 167-176
    • Mattson, M.P.1    Partin, J.2    Begley, J.G.3
  • 80
    • 84855945036 scopus 로고    scopus 로고
    • NMDA GluN2A and GluN2B receptors play separate roles in the induction of LTP and LTD in the amygdala and in the acquisition and extinction of conditioned fear
    • Dalton G. L., Wu D. C., Wang Y. T., Floresco S. B., Phillips A. G., NMDA GluN2A and GluN2B receptors play separate roles in the induction of LTP and LTD in the amygdala and in the acquisition and extinction of conditioned fear Neuropharmacology 2012 62 2 797 806
    • (2012) Neuropharmacology , vol.62 , Issue.2 , pp. 797-806
    • Dalton, G.L.1    Wu, D.C.2    Wang, Y.T.3    Floresco, S.B.4    Phillips, A.G.5
  • 83
    • 16544376850 scopus 로고    scopus 로고
    • Role of distinct NMDA receptor subtypes at central synapses
    • ARTICLE RE16
    • Cull-Candy S. G., Leszkiewicz D. N., Role of distinct NMDA receptor subtypes at central synapses Science's STKE 2004 2004 255, article re16
    • (2004) Science's STKE , vol.2004 , Issue.255
    • Cull-Candy, S.G.1    Leszkiewicz, D.N.2
  • 84
    • 34248172476 scopus 로고    scopus 로고
    • Toxicity of -amyloid in HEK293 cells expressing NR1/NR2A or NR1/NR2B N-methyl-d-aspartate receptor subunits
    • DOI 10.1016/j.neuint.2007.03.001, PII S0197018607000605
    • Domingues A., Almeida S., da Cruz e Silva E. F., Oliveira C. R., Rego A. C., Toxicity of -amyloid in HEK293 cells expressing NR1/NR2A or NR1/NR2B N-methyl-d-aspartate receptor subunits Neurochemistry International 2007 50 6 872 880 (Pubitemid 46710199)
    • (2007) Neurochemistry International , vol.50 , Issue.6 , pp. 872-880
    • Domingues, A.1    Almeida, S.2    Da Cruz E Silva, E.F.3    Oliveira, C.R.4    Rego, A.C.5
  • 85
    • 80054890113 scopus 로고    scopus 로고
    • Activation of NOX2 by the stimulation of ionotropic and metabotropic glutamate receptors contributes to glutamate neurotoxicity in vivo through the production of reactive oxygen species and calpain activation
    • Guemez-Gamboa A., Estrada-Sanchez A. M., Montiel T., Paramo B., Massieu L., Moran J., Activation of NOX2 by the stimulation of ionotropic and metabotropic glutamate receptors contributes to glutamate neurotoxicity in vivo through the production of reactive oxygen species and calpain activation Journal of Neuropathology Experimental Neurology 2011 70 11 1020 1035
    • (2011) Journal of Neuropathology Experimental Neurology , vol.70 , Issue.11 , pp. 1020-1035
    • Guemez-Gamboa, A.1    Estrada-Sanchez, A.M.2    Montiel, T.3    Paramo, B.4    Massieu, L.5    Moran, J.6
  • 88
    • 34249672242 scopus 로고    scopus 로고
    • A oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine
    • DOI 10.1074/jbc.M607483200
    • De Felice F. G., Velasco P. T., Lambert M. P., Viola K., Fernandez S. J., Ferreira S. T., Klein W. L., A oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine Journal of Biological Chemistry 2007 282 15 11590 11601 (Pubitemid 47100810)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.15 , pp. 11590-11601
    • De Felice, F.G.1    Velasco, P.T.2    Lambert, M.P.3    Viola, K.4    Fernandez, S.J.5    Ferreira, S.T.6    Klein, W.L.7
  • 89
    • 84856958510 scopus 로고    scopus 로고
    • Amyloid beta peptide 142 disturbs intracellular calcium homeostasis through activation of GluN2B-containing N-methyl-d-aspartate receptors in cortical cultures
    • Ferreira I. L., Bajouco L. M., Mota S. I., Auberson Y. P., Oliveira C. R., Rego A. C., Amyloid beta peptide 142 disturbs intracellular calcium homeostasis through activation of GluN2B-containing N-methyl-d-aspartate receptors in cortical cultures Cell Calcium 2012 51 2 95 106
    • (2012) Cell Calcium , vol.51 , Issue.2 , 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
  • 90
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid- protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • DOI 10.1523/JNEUROSCI.4970-06.2007
    • Shankar G. M., Bloodgood B. L., Townsend M., Walsh D. M., Selkoe D. J., Sabatini B. L., Natural oligomers of the Alzheimer amyloid- protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway Journal of Neuroscience 2007 27 11 2866 2875 (Pubitemid 46438992)
    • (2007) Journal of Neuroscience , vol.27 , Issue.11 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 92
    • 33750379305 scopus 로고    scopus 로고
    • Amyloid -peptide preconditioning reduces glutamate-induced neurotoxicity by promoting endocytosis of NMDA receptor
    • DOI 10.1016/j.bbrc.2006.10.030, PII S0006291X06022686
    • Goto Y., Niidome T., Akaike A., Kihara T., Sugimoto H., Amyloid -peptide preconditioning reduces glutamate-induced neurotoxicity by promoting endocytosis of NMDA receptor Biochemical and Biophysical Research Communications 2006 351 1 259 265 (Pubitemid 44635435)
    • (2006) Biochemical and Biophysical Research Communications , vol.351 , Issue.1 , pp. 259-265
    • Goto, Y.1    Niidome, T.2    Akaike, A.3    Kihara, T.4    Sugimoto, H.5
  • 93
    • 65249093004 scopus 로고    scopus 로고
    • A role for synaptic zinc in activity-dependent a oligomer formation and accumulation at excitatory synapses
    • Deshpande A., Kawai H., Metherate R., Glabe C. G., Busciglio J., A role for synaptic zinc in activity-dependent a oligomer formation and accumulation at excitatory synapses Journal of Neuroscience 2009 29 13 4004 4015
    • (2009) Journal of Neuroscience , vol.29 , Issue.13 , pp. 4004-4015
    • Deshpande, A.1    Kawai, H.2    Metherate, R.3    Glabe, C.G.4    Busciglio, J.5
  • 94
    • 35948937549 scopus 로고    scopus 로고
    • The dichotomy of NMDA receptor signaling
    • DOI 10.1177/10738584070130060401
    • Papadia S., Hardingham G. E., The dichotomy of NMDA receptor signaling Neuroscientist 2007 13 6 572 579 (Pubitemid 350077306)
    • (2007) Neuroscientist , vol.13 , Issue.6 , pp. 572-579
    • Papadia, S.1    Hardingham, G.E.2
  • 95
    • 78649417803 scopus 로고    scopus 로고
    • Activation of extrasynaptic, but not synaptic, NMDA receptors modifies amyloid precursor protein expression pattern and increases amyloid- production
    • Bordji K., Becerril-Ortega J., Nicole O., Buisson A., Activation of extrasynaptic, but not synaptic, NMDA receptors modifies amyloid precursor protein expression pattern and increases amyloid- production Journal of Neuroscience 2010 30 47 15927 15942
    • (2010) Journal of Neuroscience , vol.30 , Issue.47 , pp. 15927-15942
    • Bordji, K.1    Becerril-Ortega, J.2    Nicole, O.3    Buisson, A.4
  • 96
    • 33646839766 scopus 로고    scopus 로고
    • Preconditioning doses of NMDA promote neuroprotection by enhancing neuronal excitability
    • DOI 10.1523/JNEUROSCI.0455-06.2006
    • Soriano F. X., Papadia S., Hofmann F., Hardingham N. R., Bading H., Hardingham G. E., Preconditioning doses of NMDA promote neuroprotection by enhancing neuronal excitability Journal of Neuroscience 2006 26 17 4509 4518 (Pubitemid 44315350)
    • (2006) Journal of Neuroscience , vol.26 , Issue.17 , pp. 4509-4518
    • Soriano, F.X.1    Papadia, S.2    Hofmann, F.3    Hardingham, N.R.4    Bading, H.5    Hardingham, G.E.6
  • 97
    • 70450182118 scopus 로고    scopus 로고
    • Coupling of the NMDA receptor to neuroprotective and neurodestructive events
    • Hardingham G. E., Coupling of the NMDA receptor to neuroprotective and neurodestructive events Biochemical Society Transactions 2009 37 6 1147 1160
    • (2009) Biochemical Society Transactions , vol.37 , Issue.6 , pp. 1147-1160
    • Hardingham, G.E.1
  • 98
    • 0037301661 scopus 로고    scopus 로고
    • The Yin and Yang of NMDA receptor signalling
    • DOI 10.1016/S0166-2236(02)00040-1, PII S0166223602000401
    • Hardingham G. E., Bading H., The Yin and Yang of NMDA receptor signalling Trends in Neurosciences 2003 26 2 81 89 (Pubitemid 36110542)
    • (2003) Trends in Neurosciences , vol.26 , Issue.2 , pp. 81-89
    • Hardingham, G.E.1    Bading, H.2
  • 99
    • 57349135887 scopus 로고    scopus 로고
    • Neuronal viability is controlled by a functional relation between synaptic and extrasynaptic NMDA receptors
    • Léveillé F., El Gaamouch F., Gouix E., Lecocq M., Lobner D., Nicole O., Buisson A., Neuronal viability is controlled by a functional relation between synaptic and extrasynaptic NMDA receptors The FASEB Journal 2008 22 12 4258 4271
    • (2008) The FASEB Journal , vol.22 , Issue.12 , pp. 4258-4271
    • Léveillé, F.1    El Gaamouch, F.2    Gouix, E.3    Lecocq, M.4    Lobner, D.5    Nicole, O.6    Buisson, A.7
  • 100
    • 0036241207 scopus 로고    scopus 로고
    • Extrasynaptic NMDARs oppose synaptic NMDARs by triggering CREB shut-off and cell death pathways
    • DOI 10.1038/nn835
    • Hardingham G. E., Fukunaga Y., Bading H., Extrasynaptic NMDARs oppose synaptic NMDARs by triggering CREB shut-off and cell death pathways Nature Neuroscience 2002 5 5 405 414 (Pubitemid 34454245)
    • (2002) Nature Neuroscience , vol.5 , Issue.5 , pp. 405-414
    • Hardingham, G.E.1    Fukunaga, Y.2    Bading, H.3
  • 101
    • 33645837486 scopus 로고    scopus 로고
    • Opposing role of synaptic and extrasynaptic NMDA receptors in regulation of the extracellular signal-regulated kinases (ERK) activity in cultured rat hippocampal neurons
    • Ivanov A., Pellegrino C., Rama S., Dumalska I., Salyha Y., Ben-Ari Y., Medina I., Opposing role of synaptic and extrasynaptic NMDA receptors in regulation of the extracellular signal-regulated kinases (ERK) activity in cultured rat hippocampal neurons Journal of Physiology 2006 572 3 789 798
    • (2006) Journal of Physiology , vol.572 , Issue.3 , pp. 789-798
    • Ivanov, A.1    Pellegrino, C.2    Rama, S.3    Dumalska, I.4    Salyha, Y.5    Ben-Ari, Y.6    Medina, I.7
  • 103
    • 33645010267 scopus 로고    scopus 로고
    • Developmental changes in NMDA neurotoxicity reflect developmental changes in subunit composition of NMDA receptors
    • Zhou M., Baudry M., Developmental changes in NMDA neurotoxicity reflect developmental changes in subunit composition of NMDA receptors Journal of Neuroscience 2006 26 11 2956 2963
    • (2006) Journal of Neuroscience , vol.26 , Issue.11 , pp. 2956-2963
    • Zhou, M.1    Baudry, M.2
  • 104
    • 33947331063 scopus 로고    scopus 로고
    • NMDA receptor subunits have differential roles in mediating excitotoxic neuronal death both in vitro and in vivo
    • DOI 10.1523/JNEUROSCI.0116-07.2007
    • Liu Y., Tak P. W., Aarts M., Rooyakkers A., Liu L., Ted W. L., Dong C. W., Lu J., Tymianski M., Craig A. M., Yu T. W., NMDA receptor subunits have differential roles in mediating excitotoxic neuronal death both in vitro and in vivo Journal of Neuroscience 2007 27 11 2846 2857 (Pubitemid 46438991)
    • (2007) Journal of Neuroscience , vol.27 , Issue.11 , pp. 2846-2857
    • Liu, Y.1    Tak, P.W.2    Aarts, M.3    Rooyakkers, A.4    Liu, L.5    Ted, W.L.6    Dong, C.W.7    Lu, J.8    Tymianski, M.9    Craig, A.M.10    Yu, T.W.11
  • 106
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter P., Ron D., The unfolded protein response: from stress pathway to homeostatic regulation Science 2011 334 6059 1081 1086
    • (2011) Science , vol.334 , Issue.6059 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 107
    • 57049117856 scopus 로고    scopus 로고
    • Cell death and endoplasmic reticulum stress: Disease relevance and therapeutic opportunities
    • Kim I., Xu W., Reed J. C., Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities Nature Reviews Drug Discovery 2008 7 12 1013 1030
    • (2008) Nature Reviews Drug Discovery , vol.7 , Issue.12 , pp. 1013-1030
    • Kim, I.1    Xu, W.2    Reed, J.C.3
  • 108
    • 0036314984 scopus 로고    scopus 로고
    • Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response
    • DOI 10.1016/S0022-2836(02)00234-6
    • Ma Y., Brewer J. W., Alan Diehl J., Hendershot L. M., Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response Journal of Molecular Biology 2002 318 5 1351 1365 (Pubitemid 34754003)
    • (2002) Journal of Molecular Biology , vol.318 , Issue.5 , pp. 1351-1365
    • Ma, Y.1    Brewer, J.W.2    Alan Diehl, J.3    Hendershot, L.M.4
  • 109
    • 0037317592 scopus 로고    scopus 로고
    • Growth arrest and DNA damage-inducible protein GADD34 targets protein phosphatase 1 to the endoplasmic reticulum and promotes dephosphorylation of the subunit of eukaryotic translation initiation factor 2
    • DOI 10.1128/MCB.23.4.1292-1303.2003
    • Brush M. H., Weiser D. C., Shenolikar S., Growth arrest and DNA damage-inducible protein GADD34 targets protein phosphatase 1 to the endoplasmic reticulum and promotes dephosphorylation of the subunit of eukaryotic translation initiation factor 2 Molecular and Cellular Biology 2003 23 4 1292 1303 (Pubitemid 36177038)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.4 , pp. 1292-1303
    • Brush, M.H.1    Weiser, D.C.2    Shenolikar, S.3
  • 110
    • 0035947778 scopus 로고    scopus 로고
    • Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2
    • Novoa I., Zeng H., Harding H. P., Ron D., Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2 Journal of Cell Biology 2001 153 5 1011 1022
    • (2001) Journal of Cell Biology , vol.153 , Issue.5 , pp. 1011-1022
    • Novoa, I.1    Zeng, H.2    Harding, H.P.3    Ron, D.4
  • 112
    • 0035144493 scopus 로고    scopus 로고
    • Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bc12 and perturbing the cellular redox state
    • DOI 10.1128/MCB.21.4.1249-1259.2001
    • McCullough K. D., Martindale J. L., Klotz L. O., Aw T. Y., Holbrook N. J., Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bc12 and perturbing the cellular redox state Molecular and Cellular Biology 2001 21 4 1249 1259 (Pubitemid 32114973)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.4 , pp. 1249-1259
    • McCullough, K.D.1    Martindale, J.L.2    Klotz, L.-O.3    Aw, T.-Y.4    Holbrook, N.J.5
  • 114
    • 26444442450 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress: Cell life and death decisions
    • DOI 10.1172/JCI26373
    • Xu C., Bailly-Maitre B., Reed J. C., Endoplasmic reticulum stress: cell life and death decisions Journal of Clinical Investigation 2005 115 10 2656 2664 (Pubitemid 41434389)
    • (2005) Journal of Clinical Investigation , vol.115 , Issue.10 , pp. 2656-2664
    • Xu, C.1    Bailly-Maitre, B.2    Reed, J.C.3
  • 115
    • 33745844503 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in health and disease
    • DOI 10.1016/j.ceb.2006.06.005, PII S0955067406000810
    • Zhao L., Ackerman S. L., Endoplasmic reticulum stress in health and disease Current Opinion in Cell Biology 2006 18 4 444 452 (Pubitemid 44026518)
    • (2006) Current Opinion in Cell Biology , vol.18 , Issue.4 , pp. 444-452
    • Zhao, L.1    Ackerman, S.L.2
  • 116
    • 0035232146 scopus 로고    scopus 로고
    • Perturbed endoplasmic reticulum function, synaptic apoptosis and the pathogenesis of Alzheimer's disease
    • Mattson M. P., Gary D. S., Chan S. L., Duan W., Perturbed endoplasmic reticulum function, synaptic apoptosis and the pathogenesis of Alzheimer's disease Biochemical Society Symposium 2001 67 151 162 (Pubitemid 33602683)
    • (2001) Biochemical Society Symposium , vol.67 , pp. 151-162
    • Mattson, M.P.1    Gary, D.S.2    Chan, S.L.3    Duan, W.4
  • 117
    • 0036830947 scopus 로고    scopus 로고
    • Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease
    • LaFerla F. M., Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease Nature Reviews Neuroscience 2002 3 11 862 872
    • (2002) Nature Reviews Neuroscience , vol.3 , Issue.11 , pp. 862-872
    • Laferla, F.M.1
  • 118
    • 4444298732 scopus 로고    scopus 로고
    • Induction of neuronal death by ER stress in Alzheimer's disease
    • DOI 10.1016/j.jchemneu.2003.12.004, PII S0891061804000225
    • Katayama T., Imaizumi K., Manabe T., Hitomi J., Kudo T., Tohyama M., Induction of neuronal death by ER stress in Alzheimer's disease Journal of Chemical Neuroanatomy 2004 28 1-2 67 78 (Pubitemid 39198955)
    • (2004) Journal of Chemical Neuroanatomy , vol.28 , Issue.1-2 , pp. 67-78
    • Katayama, T.1    Imaizumi, K.2    Manabe, T.3    Hitomi, J.4    Kudo, T.5    Tohyama, M.6
  • 119
    • 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 J. H., Won S. M., Suh J., Son S. J., Moon G. J., Park U. J., Gwag B. J., Induction of the unfolded protein response and cell death pathway in alzheimer's disease, but not in aged Tg2576 mice Experimental and Molecular Medicine 2010 42 5 386 394
    • (2010) Experimental and Molecular Medicine , vol.42 , Issue.5 , 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
  • 122
    • 33744985455 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress features are prominent in Alzheimer disease but not in prion diseases in vivo
    • DOI 10.1097/01.jnen.0000218445.30535.6f, PII 0000507220060400000005
    • Unterberger U., Hftberger R., Gelpi E., Flicker H., Budka H., Voigtlnder T., Endoplasmic reticulum stress features are prominent in Alzheimer disease but not in prion diseases in vivo Journal of Neuropathology and Experimental Neurology 2006 65 4 348 357 (Pubitemid 44264832)
    • (2006) Journal of Neuropathology and Experimental Neurology , vol.65 , Issue.4 , pp. 348-357
    • Unterberger, U.1    Hoftberger, R.2    Gelpi, E.3    Flicker, H.4    Budka, H.5    Voigtlander, T.6
  • 129
    • 84860215166 scopus 로고    scopus 로고
    • A persistent stress response to impeded axonal transport leads to accumulation of amyloid-beta in the endoplasmic reticulum, and is a probable cause of sporadic Alzheimer's disease
    • Muresan V., Muresan Z., A persistent stress response to impeded axonal transport leads to accumulation of amyloid-beta in the endoplasmic reticulum, and is a probable cause of sporadic Alzheimer's disease Neurodegenerative Diseases 2012 10 14 60 63
    • (2012) Neurodegenerative Diseases , vol.10 , Issue.14 , pp. 60-63
    • Muresan, V.1    Muresan, Z.2
  • 130
    • 79955601720 scopus 로고    scopus 로고
    • Intraneuronal amyloid 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 M. P., Klein W. L., Mori H., Intraneuronal amyloid oligomers cause cell death via endoplasmic reticulum stress, endosomal/lysosomal leakage, and mitochondrial dysfunction in vivo Journal of Neuroscience Research 2011 89 7 1031 1042
    • (2011) Journal of Neuroscience Research , vol.89 , Issue.7 , 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
  • 133
    • 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., Sugimoto H., Amyloid precursor protein promotes endoplasmic reticulum stress-induced cell death via C/EBP homologous protein-mediated pathway Journal of Neurochemistry 2009 109 5 1324 1337
    • (2009) Journal of Neurochemistry , vol.109 , Issue.5 , pp. 1324-1337
    • Takahashi, K.1    Niidome, T.2    Akaike, A.3    Kihara, T.4    Sugimoto, H.5
  • 134
    • 62549147038 scopus 로고    scopus 로고
    • The E693 mutation in amyloid precursor protein increases intracellular accumulation of amyloid oligomers and causes endoplasmic reticulum stress-induced apoptosis in cultured cells
    • Nishitsuji K., Tomiyama T., Ishibashi K., Ito K., Teraoka R., Lambert M. P., Klein W. L., Mori H., The E693 mutation in amyloid precursor protein increases intracellular accumulation of amyloid oligomers and causes endoplasmic reticulum stress-induced apoptosis in cultured cells American Journal of Pathology 2009 174 3 957 969
    • (2009) American Journal of Pathology , vol.174 , Issue.3 , pp. 957-969
    • Nishitsuji, K.1    Tomiyama, T.2    Ishibashi, K.3    Ito, K.4    Teraoka, R.5    Lambert, M.P.6    Klein, W.L.7    Mori, H.8
  • 136
    • 49249118742 scopus 로고    scopus 로고
    • Neurotoxic effect of oligomeric and fibrillar species of amyloid-beta peptide 142: Involvement of endoplasmic reticulum calcium release in oligomer-induced cell death
    • Resende R., Ferreiro E., Pereira C., Resende de Oliveira C., Neurotoxic effect of oligomeric and fibrillar species of amyloid-beta peptide 142: involvement of endoplasmic reticulum calcium release in oligomer-induced cell death Neuroscience 2008 155 3 725 737
    • (2008) Neuroscience , vol.155 , Issue.3 , pp. 725-737
    • Resende, R.1    Ferreiro, E.2    Pereira, C.3    Resende De Oliveira, C.4
  • 138
    • 0041623716 scopus 로고    scopus 로고
    • Different expression of calreticulin and immunoglobulin binding protein in Alzheimer's disease brain
    • Taguchi J., Fujii A., Fujino Y., Tsujioka Y., Takahashi M., Tsuboi Y., Wada I., Yamada T., Different expression of calreticulin and immunoglobulin binding protein in Alzheimer's disease brain Acta Neuropathologica 2000 100 2 153 160 (Pubitemid 30456137)
    • (2000) Acta Neuropathologica , vol.100 , Issue.2 , pp. 153-160
    • Taguchi, J.1    Fujii, A.2    Fujino, Y.3    Tsujioka, Y.4    Takahashi, M.5    Tsuboi, Y.6    Wada, I.7    Yamada, T.8
  • 139
    • 24644460177 scopus 로고    scopus 로고
    • 2+ release in the 3xTg-AD mouse model of Alzheimer's disease
    • DOI 10.1111/j.1471-4159.2005.03332.x
    • Smith I. F., Hitt B., Green K. N., Oddo S., LaFerla F. M., Enhanced caffeine-induced Ca 2+ release in the 3xTg-AD mouse model of Alzheimer's disease Journal of Neurochemistry 2005 94 6 1711 1718 (Pubitemid 41324651)
    • (2005) Journal of Neurochemistry , vol.94 , Issue.6 , pp. 1711-1718
    • Smith, I.F.1    Hitt, B.2    Green, K.N.3    Oddo, S.4    LaFerla, F.M.5
  • 140
    • 68049134265 scopus 로고    scopus 로고
    • Deviant ryanodine receptor-mediated calcium release resets synaptic homeostasis in presymptomatic 3xTg-AD mice
    • Chakroborty S., Goussakov I., Miller M. B., Stutzmann G. E., Deviant ryanodine receptor-mediated calcium release resets synaptic homeostasis in presymptomatic 3xTg-AD mice Journal of Neuroscience 2009 29 30 9458 9470
    • (2009) Journal of Neuroscience , vol.29 , Issue.30 , pp. 9458-9470
    • Chakroborty, S.1    Goussakov, I.2    Miller, M.B.3    Stutzmann, G.E.4
  • 141
    • 0037289779 scopus 로고    scopus 로고
    • 2+ signaling in mouse cortical neurons studied by two-photon imaging and photoreleased inositol triphosphate
    • Stutzmann G. E., LaFerla F. M., Parker I., Ca 2+ signaling in mouse cortical neurons studied by two-photon imaging and photoreleased inositol triphosphate Journal of Neuroscience 2003 23 3 758 765 (Pubitemid 36206166)
    • (2003) Journal of Neuroscience , vol.23 , Issue.3 , pp. 758-765
    • Stutzmann, G.E.1    LaFerla, F.M.2    Parker, I.3
  • 142
    • 1342288871 scopus 로고    scopus 로고
    • 2+ Signals and Altered Membrane Excitability
    • DOI 10.1523/JNEUROSCI.4386-03.2004
    • Stutzmann G. E., Caccamo A., LaFerla F. M., Parker I., Dysregulated IP 3 signaling in cortical neurons of knock-in mice expressing an Alzheimer's-linked mutation in presenilin1 results in exaggerated Ca 2+ signals and altered membrane excitability Journal of Neuroscience 2004 24 2 508 513 (Pubitemid 38112383)
    • (2004) Journal of Neuroscience , vol.24 , Issue.2 , pp. 508-513
    • Stutzmann, G.E.1    Caccamo, A.2    LaFerla, F.M.3    Parker, I.4
  • 144
    • 33748140720 scopus 로고    scopus 로고
    • 2+ Leak Channels, a Function Disrupted by Familial Alzheimer's Disease-Linked Mutations
    • DOI 10.1016/j.cell.2006.06.059, PII S0092867406010257
    • Tu H., Nelson O., Bezprozvanny A., Wang Z., Lee S. F., Hao Y. H., Serneels L., De Strooper B., Yu G., Bezprozvanny I., Presenilins form ER Ca 2+ leak channels, a function disrupted by familial Alzheimer's disease-linked mutations Cell 2006 126 5 981 993 (Pubitemid 44310781)
    • (2006) Cell , vol.126 , Issue.5 , pp. 981-993
    • Tu, H.1    Nelson, O.2    Bezprozvanny, A.3    Wang, Z.4    Lee, S.-F.5    Hao, Y.-H.6    Serneels, L.7    De Strooper, B.8    Yu, G.9    Bezprozvanny, I.10
  • 146
    • 2642541799 scopus 로고    scopus 로고
    • 2+ release through ryanodine and inositol 1,4,5-triphosphate receptors in the neurotoxic effects induced by the amyloid- peptide
    • DOI 10.1002/jnr.20135
    • Ferreiro E., Oliveira C. R., Pereira C. M. F., Involvement of endoplasmic reticulum Ca 2+ release through ryanodine and inositol 1,4,5-triphosphate receptors in the neurotoxic effects induced by the amyloid- peptide Journal of Neuroscience Research 2004 76 6 872 880 (Pubitemid 38720693)
    • (2004) Journal of Neuroscience Research , vol.76 , Issue.6 , pp. 872-880
    • Ferreiro, E.1    Oliveira, C.R.2    Pereira, C.M.F.3
  • 147
    • 33846018429 scopus 로고    scopus 로고
    • Amyloid-(1- 42) increases ryanodine receptor-3 expression and function in neurons of TgCRND8 mice
    • DOI 10.1074/jbc.M606736200
    • Supnet C., Grant J., Kong H., Westaway D., Mayne M., Amyloid- -(142) increases ryanodine receptor-3 expression and function in neurons of TgCRND8 mice Journal of Biological Chemistry 2006 281 50 38440 38447 (Pubitemid 46041967)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.50 , pp. 38440-38447
    • Supnet, C.1    Grant, J.2    Kong, H.3    Westaway, D.4    Mayne, M.5
  • 148
    • 80053586271 scopus 로고    scopus 로고
    • Long-term phenylbutyrate administration prevents memory deficits in Tg2576 mice by decreasing Abeta
    • Ricobaraza A., Cuadrado-Tejedor M., Garcia Osta A., Long-term phenylbutyrate administration prevents memory deficits in Tg2576 mice by decreasing Abeta Frontiers in Bioscience 2011 3 1375 1384
    • (2011) Frontiers in Bioscience , vol.3 , pp. 1375-1384
    • Ricobaraza, A.1    Cuadrado-Tejedor, M.2    Garcia Osta, A.3
  • 149
    • 79955979595 scopus 로고    scopus 로고
    • Phenylbutyric acid reduces amyloid plaques and rescues cognitive behavior in AD transgenic mice
    • Wiley J. C., Pettan-Brewer C., Ladiges W. C., Phenylbutyric acid reduces amyloid plaques and rescues cognitive behavior in AD transgenic mice Aging Cell 2011 10 3 418 428
    • (2011) Aging Cell , vol.10 , Issue.3 , pp. 418-428
    • Wiley, J.C.1    Pettan-Brewer, C.2    Ladiges, W.C.3
  • 150
    • 77949351808 scopus 로고    scopus 로고
    • Phenylbutyric acid rescues endoplasmic reticulum stress-induced suppression of APP proteolysis and prevents apoptosis in neuronal cells
    • Wiley J. C., Meabon J. S., Frankowski H., Smith E. A., Schecterson L. C., Bothwell M., Ladiges W. C., Phenylbutyric acid rescues endoplasmic reticulum stress-induced suppression of APP proteolysis and prevents apoptosis in neuronal cells PLoS ONE 2010 5 2
    • (2010) PLoS ONE , vol.5 , Issue.2
    • Wiley, J.C.1    Meabon, J.S.2    Frankowski, H.3    Smith, E.A.4    Schecterson, L.C.5    Bothwell, M.6    Ladiges, W.C.7
  • 151
    • 80054680024 scopus 로고    scopus 로고
    • Silencing GADD153/CHOP gene expression protects against Alzheimer's disease-like pathology induced by 27-hydroxycholesterol in rabbit hippocampus
    • Prasanthi J. R., Larson T., Schommer J., Ghribi O., Silencing GADD153/CHOP gene expression protects against Alzheimer's disease-like pathology induced by 27-hydroxycholesterol in rabbit hippocampus PLoS ONE 2011 6 10
    • (2011) PLoS ONE , vol.6 , Issue.10
    • Prasanthi, J.R.1    Larson, T.2    Schommer, J.3    Ghribi, O.4
  • 154
  • 155
    • 0035253099 scopus 로고    scopus 로고
    • A mitochondrial perspective on cell death
    • DOI 10.1016/S0968-0004(00)01745-X, PII S096800040001745X
    • Bernardi P., Petronilli V., Di Lisa F., Forte M., A mitochondrial perspective on cell death Trends in Biochemical Sciences 2001 26 2 112 117 (Pubitemid 32144746)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.2 , pp. 112-117
    • Bernardi, P.1    Petronilli, V.2    Di Lisa, F.3    Forte, M.4
  • 156
    • 35248824214 scopus 로고    scopus 로고
    • Mitochondria-endoplasmic reticulum choreography: Structure and signaling dynamics
    • DOI 10.1016/j.tcb.2007.07.011, PII S0962892407001705
    • Pizzo P., Pozzan T., Mitochondria-endoplasmic reticulum choreography: structure and signaling dynamics Trends in Cell Biology 2007 17 10 511 517 (Pubitemid 47562768)
    • (2007) Trends in Cell Biology , vol.17 , Issue.10 , pp. 511-517
    • Pizzo, P.1    Pozzan, T.2
  • 157
    • 77955824765 scopus 로고    scopus 로고
    • An intimate liaison: Spatial organization of the endoplasmic reticulum-mitochondria relationship
    • De Brito O. M., Scorrano L., An intimate liaison: spatial organization of the endoplasmic reticulum-mitochondria relationship EMBO Journal 2010 29 16 2715 2723
    • (2010) EMBO Journal , vol.29 , Issue.16 , pp. 2715-2723
    • De Brito, O.M.1    Scorrano, L.2
  • 163
    • 35549006797 scopus 로고    scopus 로고
    • 2+ signaling and cell survival
    • DOI 10.1016/j.cell.2007.08.036, PII S0092867407010999
    • Hayashi T., Su T. P., Sigma-1 receptor chaperones at the ER- mitochondrion interface regulate Ca 2+ signaling and cell survival Cell 2007 131 3 596 610 (Pubitemid 350017760)
    • (2007) Cell , vol.131 , Issue.3 , pp. 596-610
    • Hayashi, T.1    Su, T.-P.2
  • 165
    • 68649116755 scopus 로고    scopus 로고
    • SR/ER-mitochondrial local communication: Calcium and ROS
    • Csords G., Hajnczky G., SR/ER-mitochondrial local communication: calcium and ROS Biochimica et Biophysica Acta 2009 1787 11 1352 1362
    • (2009) Biochimica et Biophysica Acta , vol.1787 , Issue.11 , pp. 1352-1362
    • Csords, G.1    Hajnczky, G.2
  • 168
    • 43649083316 scopus 로고    scopus 로고
    • The release of calcium from the endoplasmic reticulum induced by amyloid-beta and prion peptides activates the mitochondrial apoptotic pathway
    • Ferreiro E., Oliveira C. R., Pereira C. M. F., The release of calcium from the endoplasmic reticulum induced by amyloid-beta and prion peptides activates the mitochondrial apoptotic pathway Neurobiology of Disease 2008 30 3 331 342
    • (2008) Neurobiology of Disease , vol.30 , Issue.3 , pp. 331-342
    • Ferreiro, E.1    Oliveira, C.R.2    Pereira, C.M.F.3
  • 169
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri K. F., Kroemer G., Organelle-specific initiation of cell death pathways Nature Cell Biology 2001 3 11 E255 E263
    • (2001) Nature Cell Biology , vol.3 , Issue.11
    • Ferri, K.F.1    Kroemer, G.2
  • 170
    • 38049155818 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis
    • Deniaud A., Sharaf El Dein O., Maillier E., Poncet D., Kroemer G., Lemaire C., Brenner C., Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis Oncogene 2008 27 3 285 299
    • (2008) Oncogene , vol.27 , Issue.3 , pp. 285-299
    • Deniaud, A.1    Sharaf El Dein, O.2    Maillier, E.3    Poncet, D.4    Kroemer, G.5    Lemaire, C.6    Brenner, C.7
  • 171
    • 0035355341 scopus 로고    scopus 로고
    • 2+ concentration of the endoplasmic reticulum is a key determinant of ceramide-induced apoptosis: Significance for the molecular mechanism of Bcl-2 action
    • DOI 10.1093/emboj/20.11.2690
    • Pinton P., Ferrari D., Rapizzi E., Di Virgilio F., Pozzan T., Rizzuto R., The Ca 2+ concentration of the endoplasmic reticulum is a key determinant of ceramide-induced apoptosis: significance for the molecular mechanism of Bcl-2 action EMBO Journal 2001 20 11 2690 2701 (Pubitemid 32938554)
    • (2001) EMBO Journal , vol.20 , Issue.11 , pp. 2690-2701
    • Pinton, P.1    Ferrari, D.2    Rapizzi, E.3    Di Virgilio, F.4    Pozzan, T.5    Rizzuto, R.6
  • 176
    • 67649547153 scopus 로고    scopus 로고
    • Mitochondrial apoptosis induced by BH3-only molecules in the exclusive presence of endoplasmic reticular Bak
    • Klee M., Pallauf K., Alcal S., Fleischer A., Pimentel-Muos F. X., Mitochondrial apoptosis induced by BH3-only molecules in the exclusive presence of endoplasmic reticular Bak EMBO Journal 2009 28 12 1757 1768
    • (2009) EMBO Journal , vol.28 , Issue.12 , pp. 1757-1768
    • Klee, M.1    Pallauf, K.2    Alcal, S.3    Fleischer, A.4    Pimentel-Muos, F.X.5
  • 177
    • 0033570890 scopus 로고    scopus 로고
    • 3-linked mitochondrial calcium signals
    • DOI 10.1093/emboj/18.22.6349
    • Szalai G., Krishnamurthy R., Hajnczky G., Apoptosis driven by IP 3 -linked mitochondrial calcium signals EMBO Journal 1999 18 22 6349 6361 (Pubitemid 29533239)
    • (1999) EMBO Journal , vol.18 , Issue.22 , pp. 6349-6361
    • Szalai, G.1    Krishnamurthy, R.2    Hajnoczky, G.3
  • 179
    • 0344825875 scopus 로고    scopus 로고
    • Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis
    • DOI 10.1038/ncb1063
    • Boehning D., Patterson R. L., Sedaghat L., Glebova N. O., Kurosaki T., Snyder S. H., Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis Nature Cell Biology 2003 5 12 1051 1061 (Pubitemid 37509111)
    • (2003) Nature Cell Biology , vol.5 , Issue.12 , pp. 1051-1061
    • Boehning, D.1    Patterson, R.L.2    Sedaghat, L.3    Glebova, N.O.4    Kurosaki, T.5    Snyder, S.H.6
  • 180
    • 4544252174 scopus 로고    scopus 로고
    • Apoptosis and calcium: New roles for cytochrome c and inositol 1,4,5-trisphosphate
    • Boehning D., Patterson R. L., Snyder S. H., Apoptosis and calcium: new roles for cytochrome c and inositol 1,4,5-trisphosphate Cell Cycle 2004 3 3 252 254 (Pubitemid 41359065)
    • (2004) Cell Cycle , vol.3 , Issue.3 , pp. 252-254
    • Boehning, D.1    Patterson, R.L.2    Snyder, S.H.3
  • 181
    • 3142623156 scopus 로고    scopus 로고
    • Cytochrome c: A crosslink between the mitochondria and the endoplasmic reticulum in calcium-dependent apoptosis
    • Wang S., El-Deiry W. S., Cytochrome c: a crosslink between the mitochondria and the endoplasmic reticulum in calcium-dependent apoptosis Cancer Biology and Therapy 2004 3 1 44 46 (Pubitemid 41342416)
    • (2004) Cancer Biology and Therapy , vol.3 , Issue.1 , pp. 44-46
    • Wang, S.1    El-Deiry, W.S.2
  • 182
    • 0037417334 scopus 로고    scopus 로고
    • Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol
    • DOI 10.1083/jcb.200212059
    • Breckenridge D. G., Stojanovic M., Marcellus R. C., Shore G. C., Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol Journal of Cell Biology 2003 160 7 1115 1127 (Pubitemid 36443879)
    • (2003) Journal of Cell Biology , vol.160 , Issue.7 , pp. 1115-1127
    • Breckenridge, D.G.1    Stojanovic, M.2    Marcellus, R.C.3    Shore, G.C.4
  • 183
    • 18444400187 scopus 로고    scopus 로고
    • Endoplasmic reticulum BIK initiates DRP1-regulated remodelling of mitochondrial cristae during apoptosis
    • DOI 10.1038/sj.emboj.7600592
    • Germain M., Mathai J. P., McBride H. M., Shore G. C., Endoplasmic reticulum BIK initiates DRP1-regulated remodelling of mitochondrial cristae during apoptosis EMBO Journal 2005 24 8 1546 1556 (Pubitemid 40646445)
    • (2005) EMBO Journal , vol.24 , Issue.8 , pp. 1546-1556
    • Germain, M.1    Mathai, J.P.2    McBride, H.M.3    Shore, G.C.4
  • 184
    • 4944222095 scopus 로고    scopus 로고
    • 2+-mediated apoptosis
    • DOI 10.1016/j.molcel.2004.09.026, PII S1097276504005428
    • Szabadkai G., Simoni A. M., Chami M., Wieckowski M. R., Youle R. J., Rizzuto R., Drp-1-dependent division of the mitochondrial network blocks intraorganellar Ca 2+ waves and protects against Ca 2+ -mediated apoptosis Molecular Cell 2004 16 1 59 68 (Pubitemid 39330152)
    • (2004) Molecular Cell , vol.16 , Issue.1 , pp. 59-68
    • Szabadkai, G.1    Simoni, A.M.2    Chami, M.3    Wieckowski, M.R.4    Youle, R.J.5    Rizzuto, R.6
  • 187
    • 70149098692 scopus 로고    scopus 로고
    • Increased association between rough endoplasmic reticulum membranes and mitochondria in transgenic mice that express P301L tau
    • Perreault S., Bousquet O., Lauzon M., Paiement J., Leclerc N., Increased association between rough endoplasmic reticulum membranes and mitochondria in transgenic mice that express P301L tau Journal of Neuropathology and Experimental Neurology 2009 68 5 503 514
    • (2009) Journal of Neuropathology and Experimental Neurology , vol.68 , Issue.5 , pp. 503-514
    • Perreault, S.1    Bousquet, O.2    Lauzon, M.3    Paiement, J.4    Leclerc, N.5
  • 188
    • 77954516455 scopus 로고    scopus 로고
    • ER stress-mediated apoptotic pathway induced by a peptide requires the presence of functional mitochondria
    • Costa R. O., Ferreiro E., Cardoso S. M., Oliveira C. R., Pereira C. M. F., ER stress-mediated apoptotic pathway induced by a peptide requires the presence of functional mitochondria Journal of Alzheimer's Disease 2010 20 2 625 636
    • (2010) Journal of Alzheimer's Disease , vol.20 , Issue.2 , pp. 625-636
    • Costa, R.O.1    Ferreiro, E.2    Cardoso, S.M.3    Oliveira, C.R.4    Pereira, C.M.F.5
  • 189
    • 70449433157 scopus 로고    scopus 로고
    • The role of cytochrome c oxidase deficiency in ROS and amyloid plaque formation
    • Pickrell A. M., Fukui H., Moraes C. T., The role of cytochrome c oxidase deficiency in ROS and amyloid plaque formation Journal of Bioenergetics and Biomembranes 2009 41 5 453 456
    • (2009) Journal of Bioenergetics and Biomembranes , vol.41 , Issue.5 , pp. 453-456
    • Pickrell, A.M.1    Fukui, H.2    Moraes, C.T.3
  • 192
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: Mechanisms and consequences
    • DOI 10.1083/jcb.200311055
    • Tu B. P., Weissman J. S., Oxidative protein folding in eukaryotes: mechanisms and consequences Journal of Cell Biology 2004 164 3 341 346 (Pubitemid 38174761)
    • (2004) Journal of Cell Biology , vol.164 , Issue.3 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 193
    • 0034711439 scopus 로고    scopus 로고
    • Biochemical basis of oxidative protein folding in the endoplasmic reticulum
    • Tu B. P., Ho-Schleyer S. C., Travers K. J., Weissman J. S., Biochemical basis of oxidative protein folding in the endoplasmic reticulum Science 2000 290 5496 1571 1574
    • (2000) Science , vol.290 , Issue.5496 , pp. 1571-1574
    • Tu, B.P.1    Ho-Schleyer, S.C.2    Travers, K.J.3    Weissman, J.S.4
  • 194
    • 1042266634 scopus 로고    scopus 로고
    • Different contributions of the three cxxc motifs of human protein-disulfide isomerase-related protein to isomerase activity and oxidative refolding
    • DOI 10.1074/jbc.M310922200
    • Horibe T., Gomi M., Iguchi D., Ito H., Kitamura Y., Masuoka T., Tsujimoto I., Kimura T., Kikuchi M., Different contributions of the three CXXC motifs of human protein-disulfide isomerase-related protein to isomerase activity and oxidative refolding Journal of Biological Chemistry 2004 279 6 4604 4611 (Pubitemid 38199052)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.6 , pp. 4604-4611
    • Horibe, T.1    Gomi, M.2    Iguchi, D.3    Ito, H.4    Kitamura, Y.5    Masuoka, T.6    Tsujimoto, I.7    Kimura, T.8    Kikuchi, M.9
  • 195
    • 0028785706 scopus 로고
    • Oxidation of kinetically trapped thiols by protein disulfide isomerase
    • Walker K. W., Gilbert H. F., Oxidation of kinetically trapped thiols by protein disulfide isomerase Biochemistry 1995 34 41 13642 13650
    • (1995) Biochemistry , vol.34 , Issue.41 , pp. 13642-13650
    • Walker, K.W.1    Gilbert, H.F.2
  • 196
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell J. C. A., McGovern K., Beckwith J., Identification of a protein required for disulfide bond formation in vivo Cell 1991 67 3 581 589 (Pubitemid 121001472)
    • (1991) Cell , vol.67 , Issue.3 , pp. 581-589
    • Bardwell, J.C.A.1    McGovern, K.2    Beckwith, J.3
  • 198
    • 33745315287 scopus 로고    scopus 로고
    • S-Nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration
    • DOI 10.1038/nature04782, PII NATURE04782
    • Uehara T., Nakamura T., Yao D., Shi Z. Q., Gu Z., Ma Y., Masliah E., Nomura Y., Lipton S. A., S-Nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration Nature 2006 441 7092 513 517 (Pubitemid 44050153)
    • (2006) Nature , vol.441 , Issue.7092 , pp. 513-517
    • Uehara, T.1    Nakamura, T.2    Yao, D.3    Shi, Z.-Q.4    Gu, Z.5    Ma, Y.6    Masliah, E.7    Nomura, Y.8    Lipton, S.A.9
  • 199
    • 0037083869 scopus 로고    scopus 로고
    • ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family
    • DOI 10.1093/emboj/21.4.835
    • Anelli T., Alessio M., Mezghrani A., Simmen T., Talamo F., Bachi A., Sitia R., ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family EMBO Journal 2002 21 4 835 844 (Pubitemid 34174063)
    • (2002) EMBO Journal , vol.21 , Issue.4 , pp. 835-844
    • Anelli, T.1    Alessio, M.2    Mezghrani, A.3    Simmen, T.4    Talamo, F.5    Bachi, A.6    Sitia, R.7
  • 201
    • 11844269232 scopus 로고    scopus 로고
    • Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44
    • DOI 10.1016/j.cell.2004.11.048, PII S0092867404011535
    • Higo T., Hattori M., Nakamura T., Natsume T., Michikawa T., Mikoshiba K., Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44 Cell 2005 120 1 85 98 (Pubitemid 40094605)
    • (2005) Cell , vol.120 , Issue.1 , pp. 85-98
    • Higo, T.1    Hattori, M.2    Nakamura, T.3    Natsume, T.4    Michikawa, T.5    Mikoshiba, K.6
  • 203
    • 54449100767 scopus 로고    scopus 로고
    • Effects of redox potential and Ca 2+ on the inositol 1,4,5-trisphosphate receptor L3-1 loop region: Implications for receptor regulation
    • Kang S., Kang J., Kwon H., Frueh D., Seung H. Y., Wagner G., Park S., Effects of redox potential and Ca 2+ on the inositol 1,4,5-trisphosphate receptor L3-1 loop region: implications for receptor regulation Journal of Biological Chemistry 2008 283 37 25567 25575
    • (2008) Journal of Biological Chemistry , vol.283 , Issue.37 , pp. 25567-25575
    • Kang, S.1    Kang, J.2    Kwon, H.3    Frueh, D.4    Seung, H.Y.5    Wagner, G.6    Park, S.7
  • 204
    • 77955708533 scopus 로고    scopus 로고
    • Ero1 requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM)
    • Gilady S. Y., Bui M., Lynes E. M., Benson M. D., Watts R., Vance J. E., Simmen T., Ero1 requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM) Cell Stress and Chaperones 2010 15 5 619 629
    • (2010) Cell Stress and Chaperones , vol.15 , Issue.5 , pp. 619-629
    • Gilady, S.Y.1    Bui, M.2    Lynes, E.M.3    Benson, M.D.4    Watts, R.5    Vance, J.E.6    Simmen, T.7
  • 205
    • 0034668931 scopus 로고    scopus 로고
    • The machinery of local Ca 2+ signalling between sarco-endoplasmic reticulum and mitochondria
    • Hajnczky G., Csords G., Madesh M., Pacher P., The machinery of local Ca 2+ signalling between sarco-endoplasmic reticulum and mitochondria Journal of Physiology 2000 529 1 69 81
    • (2000) Journal of Physiology , vol.529 , Issue.1 , pp. 69-81
    • Hajnczky, G.1    Csords, G.2    Madesh, M.3    Pacher, P.4
  • 206
    • 42049090126 scopus 로고    scopus 로고
    • Mitochondria: The hub of cellular Ca 2+ signaling
    • Szabadkai G., Duchen M. R., Mitochondria: the hub of cellular Ca 2+ signaling Physiology 2008 23 2 84 94
    • (2008) Physiology , vol.23 , Issue.2 , pp. 84-94
    • Szabadkai, G.1    Duchen, M.R.2
  • 207
    • 0037087782 scopus 로고    scopus 로고
    • 2+ and sustained opening of the permeability transition pore
    • Jacobson J., Duchen M. R., Mitochondrial oxidative stress and cell death in astrocytesrequirement for stored Ca 2+ and sustained opening of the permeability transition pore Journal of Cell Science 2002 115 6 1175 1188 (Pubitemid 34272482)
    • (2002) Journal of Cell Science , vol.115 , Issue.6 , pp. 1175-1188
    • Jacobson, J.1    Duchen, M.R.2
  • 208
    • 16244405250 scopus 로고    scopus 로고
    • Hepatitis C virus, ER stress, and oxidative stress
    • DOI 10.1016/j.tim.2005.02.004
    • Tardif K. D., Waris G., Siddiqui A., Hepatitis C virus, ER stress, and oxidative stress Trends in Microbiology 2005 13 4 159 163 (Pubitemid 40463317)
    • (2005) Trends in Microbiology , vol.13 , Issue.4 , pp. 159-163
    • Tardif, K.D.1    Waris, G.2    Siddiqui, A.3
  • 209
    • 35848957485 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and oxidative stress: A vicious cycle or a double-edged sword?
    • DOI 10.1089/ars.2007.1782
    • Malhotra J. D., Kaufman R. J., Endoplasmic reticulum stress and oxidative stress: a vicious cycle or a double-edged sword? Antioxidants and Redox Signaling 2007 9 12 2277 2293 (Pubitemid 350059010)
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.12 , pp. 2277-2293
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 210
    • 0033163758 scopus 로고    scopus 로고
    • Competition between glutathione and protein thiols for disulphide-bond formation
    • Cuozzo J. W., Kaiser C. A., Competition between glutathione and protein thiols for disulphide-bond formation Nature Cell Biology 1999 1 3 130 135 (Pubitemid 129656016)
    • (1999) Nature Cell Biology , vol.1 , Issue.3 , pp. 130-135
    • Cuozzo, J.W.1    Kaiser, C.A.2
  • 211
    • 33645784167 scopus 로고    scopus 로고
    • The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress
    • Chakravarthi S., Jessop C. E., Bulleid N. J., The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress EMBO Reports 2006 7 3 271 275
    • (2006) EMBO Reports , vol.7 , Issue.3 , pp. 271-275
    • Chakravarthi, S.1    Jessop, C.E.2    Bulleid, N.J.3
  • 212
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang C., Sinskey A. J., Lodish H. F., Oxidized redox state of glutathione in the endoplasmic reticulum Science 1992 257 5076 1496 1502
    • (1992) Science , vol.257 , Issue.5076 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 213
    • 0026343873 scopus 로고
    • Alzheimer's and Parkinson's disease: Brain levels of glutathione, glutathione disulfide, and vitamin e
    • Adams J. D., Klaidman L. K., Odunze I. N., Shen H. C., Miller C. A., Alzheimer's and Parkinson's disease: brain levels of glutathione, glutathione disulfide, and vitamin E Molecular and Chemical Neuropathology 1991 14 3 213 226
    • (1991) Molecular and Chemical Neuropathology , vol.14 , Issue.3 , pp. 213-226
    • Adams, J.D.1    Klaidman, L.K.2    Odunze, I.N.3    Shen, H.C.4    Miller, C.A.5
  • 214
    • 0035917819 scopus 로고    scopus 로고
    • Changes in thiol content and expression of glutathione redox system genes in the hippocampus and cerebellum in Alzheimer's disease
    • DOI 10.1016/S0304-3940(01)01636-6, PII S0304394001016366
    • Aksenov M. Y., Markesbery W. R., Changes in thiol content and expression of glutathione redox system genes in the hippocampus and cerebellum in Alzheimer's disease Neuroscience Letters 2001 302 2-3 141 145 (Pubitemid 32274229)
    • (2001) Neuroscience Letters , vol.302 , Issue.2-3 , pp. 141-145
    • Aksenov, M.Y.1    Markesbery, W.R.2
  • 216
    • 4744369310 scopus 로고    scopus 로고
    • Aging-related increase in oxidative stress correlates with developmental pattern of beta-secretase activity and beta-amyloid plaque formation in transgenic Tg2576 mice with Alzheimer-like pathology
    • DOI 10.1016/j.ijdevneu.2004.07.006, PII S0736574804000929, Molecular Mechanisms of Neurodegeneration and Neuroprotection
    • Apelt J., Bigl M., Wunderlich P., Schliebs R., Aging-related increase in oxidative stress correlates with developmental pattern of beta-secretase activity and beta-amyloid plaque formation in transgenic Tg2576 mice with Alzheimer-like pathology International Journal of Developmental Neuroscience 2004 22 7 475 484 (Pubitemid 39311436)
    • (2004) International Journal of Developmental Neuroscience , vol.22 , Issue.7 , pp. 475-484
    • Apelt, J.1    Bigl, M.2    Wunderlich, P.3    Schliebs, R.4
  • 217
    • 0033010755 scopus 로고    scopus 로고
    • Exacerbation of copper toxicity in primary neuronal cultures depleted of cellular glutathione
    • DOI 10.1046/j.1471-4159.1999.0722092.x
    • White A. R., Bush A. I., Beyreuther K., Masters C. L., Cappai R., Exacerbation of copper toxicity in primary neuronal cultures depleted of cellular glutathione Journal of Neurochemistry 1999 72 5 2092 2098 (Pubitemid 29186015)
    • (1999) Journal of Neurochemistry , vol.72 , Issue.5 , pp. 2092-2098
    • White, A.R.1    Bush, A.I.2    Beyreuther, K.3    Masters, C.L.4    Cappai, R.5
  • 218
    • 0141752795 scopus 로고    scopus 로고
    • Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival
    • DOI 10.1128/MCB.23.20.7198-7209.2003
    • Cullinan S. B., Zhang D., Hannink M., Arvisais E., Kaufman R. J., Diehl J. A., Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival Molecular and Cellular Biology 2003 23 20 7198 7209 (Pubitemid 37211002)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.20 , pp. 7198-7209
    • Cullinan, S.B.1    Zhang, D.2    Hannink, M.3    Arvisais, E.4    Kaufman, R.J.5    Diehl, J.A.6
  • 219
    • 67649402187 scopus 로고    scopus 로고
    • The Nrf2-antioxidant response element signaling pathway and its activation by oxidative stress
    • Nguyen T., Nioi P., Pickett C. B., The Nrf2-antioxidant response element signaling pathway and its activation by oxidative stress Journal of Biological Chemistry 2009 284 20 13291 13295
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.20 , pp. 13291-13295
    • Nguyen, T.1    Nioi, P.2    Pickett, C.B.3
  • 220
    • 2442542312 scopus 로고    scopus 로고
    • PERK-dependent Activation of Nrf2 Contributes to Redox Homeostasis and Cell Survival following Endoplasmic Reticulum Stress
    • DOI 10.1074/jbc.M314219200
    • Cullinan S. B., Diehl J. A., PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress Journal of Biological Chemistry 2004 279 19 20108 20117 (Pubitemid 38623455)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.19 , pp. 20108-20117
    • Cullinan, S.B.1    Diehl, J.A.2
  • 223
    • 70349905357 scopus 로고    scopus 로고
    • Role of ERO1- -mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis
    • Li G., Mongillo M., Chin K. T., Harding H., Ron D., Marks A. R., Tabas I., Role of ERO1- -mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis Journal of Cell Biology 2009 186 6 783 792
    • (2009) Journal of Cell Biology , vol.186 , Issue.6 , pp. 783-792
    • Li, G.1    Mongillo, M.2    Chin, K.T.3    Harding, H.4    Ron, D.5    Marks, A.R.6    Tabas, I.7
  • 225
    • 78650105442 scopus 로고    scopus 로고
    • NADPH oxidase links endoplasmic reticulum stress, oxidative stress, and PKR activation to induce apoptosis
    • Li G., Scull C., Ozcan L., Tabas I., NADPH oxidase links endoplasmic reticulum stress, oxidative stress, and PKR activation to induce apoptosis Journal of Cell Biology 2010 191 6 1113 1125
    • (2010) Journal of Cell Biology , vol.191 , Issue.6 , pp. 1113-1125
    • Li, G.1    Scull, C.2    Ozcan, L.3    Tabas, I.4
  • 226
    • 33746238205 scopus 로고    scopus 로고
    • Molecular indices of oxidative stress and mitochondrial dysfunction occur early and often progress with severity of Alzheimer's disease
    • De La Monte S. M., Wands J. R., Molecular indices of oxidative stress and mitochondrial dysfunction occur early and often progress with severity of Alzheimer's disease Journal of Alzheimer's Disease 2006 9 2 167 181 (Pubitemid 44088244)
    • (2006) Journal of Alzheimer's Disease , vol.9 , Issue.2 , pp. 167-181
    • De La Monte, S.M.1    Wands, J.R.2
  • 227
    • 0033923221 scopus 로고    scopus 로고
    • High-capacity redox control at the plasma membrane of mammalian cells: Trans-membrane, cell surface, and serum NADH-oxidases
    • Berridge M. V., Tan A. S., High-capacity redox control at the plasma membrane of mammalian cells: trans-membrane, cell surface, and serum NADH-oxidases Antioxidants and Redox Signaling 2000 2 2 231 242 (Pubitemid 30445935)
    • (2000) Antioxidants and Redox Signaling , vol.2 , Issue.2 , pp. 231-242
    • Berridge, M.V.1    Tan, A.S.2
  • 228
    • 0036182380 scopus 로고    scopus 로고
    • Calcium and oxidative stress: From cell signaling to cell death
    • DOI 10.1016/S0161-5890(01)00108-0, PII S0161589001001080
    • Ermak G., Davies K. J. A., Calcium and oxidative stress: from cell signaling to cell death Molecular Immunology 2002 38 10 713 721 (Pubitemid 34158874)
    • (2002) Molecular Immunology , vol.38 , Issue.10 , pp. 713-721
    • Ermak, G.1    Davies, K.J.A.2
  • 229
    • 0034185616 scopus 로고    scopus 로고
    • Protein oxidation and age-dependent alterations in calcium homeostasis
    • Squier T. C., Bigelow D. J., Protein oxidation and age-dependent alterations in calcium homeostasis Frontiers in Bioscience 2000 5 D504 D526
    • (2000) Frontiers in Bioscience , vol.5
    • Squier, T.C.1    Bigelow, D.J.2
  • 230
    • 0034665152 scopus 로고    scopus 로고
    • Nitric oxide-dependent modification of the sarcoplasmic reticulum Ca- ATPase: Localization of cysteine target sites
    • Viner R. I., Williams T. D., Schneich C., Nitric oxide-dependent modification of the sarcoplasmic reticulum Ca- ATPase: localization of cysteine target sites Free Radical Biology and Medicine 2000 29 6 489 496
    • (2000) Free Radical Biology and Medicine , vol.29 , Issue.6 , pp. 489-496
    • Viner, R.I.1    Williams, T.D.2    Schneich, C.3
  • 235
    • 0036970014 scopus 로고    scopus 로고
    • Plasma susceptibility to free radical-induced antioxidant consumption and lipid peroxidation is increased in very old subjects with Alzheimer disease
    • Polidori M. C., Mecocci P., Plasma susceptibility to free radical-induced antioxidant consumption and lipid peroxidation is increased in very old subjects with Alzheimer disease Journal of Alzheimer's Disease 2002 4 6 517 522 (Pubitemid 36142841)
    • (2002) Journal of Alzheimer's Disease , vol.4 , Issue.6 , pp. 517-522
    • Polidori, M.C.1    Mecocci, P.2
  • 236
    • 33846226106 scopus 로고    scopus 로고
    • Determination of malondialdehyde, reduced glutathione levels and APOE4 allele frequency in late-onset Alzheimer's disease in Denizli, Turkey
    • DOI 10.1016/j.clinbiochem.2006.09.005, PII S0009912006003031
    • Aybek H., Ercan F., Aslan D., ahiner T., Determination of malondialdehyde, reduced glutathione levels and APOE4 allele frequency in late-onset Alzheimer's disease in Denizli, Turkey Clinical Biochemistry 2007 40 3-4 172 176 (Pubitemid 46108698)
    • (2007) Clinical Biochemistry , vol.40 , Issue.3-4 , pp. 172-176
    • Aybek, H.1    Ercan, F.2    Aslan, D.3    Sahiner, T.4
  • 237
    • 38949123654 scopus 로고    scopus 로고
    • Lipid peroxidation and antioxidant enzyme activities in vascular and alzheimer dementias
    • DOI 10.1007/s11064-007-9453-3
    • Casado A., Encarnacion Lopez-Fernandez M., Concepcin Casado M., De La Torre R., Lipid peroxidation and antioxidant enzyme activities in vascular and alzheimer dementias Neurochemical Research 2008 33 3 450 458 (Pubitemid 351230446)
    • (2008) Neurochemical Research , vol.33 , Issue.3 , pp. 450-458
    • Casado, A.1    Encarnacion Lopez-Fernandez, M.2    Concepcion Casado, Ma.3    De La Torre, R.4
  • 238
    • 72649096229 scopus 로고    scopus 로고
    • Changes of some oxidative stress markers in the serum of patients with mild cognitive impairment and Alzheimer's disease
    • Padurariu M., Ciobica A., Hritcu L., Stoica B., Bild W., Stefanescu C., Changes of some oxidative stress markers in the serum of patients with mild cognitive impairment and Alzheimer's disease Neuroscience Letters 2010 469 1 6 10
    • (2010) Neuroscience Letters , vol.469 , Issue.1 , pp. 6-10
    • Padurariu, M.1    Ciobica, A.2    Hritcu, L.3    Stoica, B.4    Bild, W.5    Stefanescu, C.6
  • 242
    • 0029871412 scopus 로고    scopus 로고
    • Peripheral antioxidant enzyme activities and selenium in elderly subjects and in dementia of Alzheimer's type - Place of the extracellular glutathione peroxidase
    • DOI 10.1016/0891-5849(95)02058-6
    • Ceballos-Picot I., Merad-Boudia M., Nicole A., Thevenin M., Hellier G., Legrain S., Berr C., Peripheral antioxidant enzyme activities and selenium in elderly subjects and in dementia of Alzheimer's typeplace of the extracellular glutathione peroxidase Free Radical Biology and Medicine 1996 20 4 579 587 (Pubitemid 26097275)
    • (1996) Free Radical Biology and Medicine , vol.20 , Issue.4 , pp. 579-587
    • Ceballos-Picot, I.1    Merad-Boudia, M.2    Nicole, A.3    Thevenin, M.4    Hellier, G.5    Legrain, S.6    Berr, C.7
  • 245
    • 0030714092 scopus 로고    scopus 로고
    • Elevated 4-hydroxynonenal in ventricular fluid in Alzheimer's disease
    • DOI 10.1016/S0197-4580(97)00108-5, PII S0197458097001085
    • Lovell M. A., Ehmann W. D., Mattson M. P., Markesbery W. R., Elevated 4-hydroxynonenal in ventricular fluid in Alzheimer's disease Neurobiology of Aging 1997 18 5 457 461 (Pubitemid 27497140)
    • (1997) Neurobiology of Aging , vol.18 , Issue.5 , pp. 457-461
    • Lovell, M.A.1    Ehmann, W.D.2    Mattson, M.P.3    Markesbery, W.R.4
  • 247
    • 0031676742 scopus 로고    scopus 로고
    • Altered plasma antioxidant status in subjects with Alzheimer's disease and vascular dementia
    • DOI 10.1002/(SICI)1099-1166(1998120) 13:12<840::AID-GPS877>3.0. CO;2-R
    • Sinclair A. J., Bayer A. J., Johnston J., Warner C., Maxwell S. R., Altered plasma antioxidant status in subjects with Alzheimer's disease and vascular dementia International Journal of Geriatric Psychiatry 1998 13 12 840 845 (Pubitemid 28564482)
    • (1998) International Journal of Geriatric Psychiatry , vol.13 , Issue.12 , pp. 840-845
    • Sinclair, A.J.1    Bayer, A.J.2    Johnston, J.O.3    Warner, C.4    Maxwell, S.R.J.5
  • 248
    • 0037111170 scopus 로고    scopus 로고
    • Oxidative stress and reduced antioxidant defenses in peripheral cells from familial Alzheimer's patients
    • DOI 10.1016/S0891-5849(02)01049-3, PII S0891584902010493
    • Cecchi C., Fiorillo C., Sorbi S., Latorraca S., Nacmias B., Bagnoli S., Nassi P., Liguri G., Oxidative stress and reduced antioxidant defenses in peripheral cells from familial Alzheimer's patients Free Radical Biology and Medicine 2002 33 10 1372 1379 (Pubitemid 35284921)
    • (2002) Free Radical Biology and Medicine , vol.33 , Issue.10 , pp. 1372-1379
    • Cecchi, C.1    Fiorillo, C.2    Sorbi, S.3    Latorraca, S.4    Nacmias, B.5    Bagnoli, S.6    Nassi, P.7    Liguri, G.8
  • 249
    • 0031594916 scopus 로고    scopus 로고
    • 2-isoprostane levels are increased in Alzheimer's disease
    • DOI 10.1002/ana.410440322
    • Montine T. J., Markesbery W. R., Morrow J. D., Roberts L. J., Cerebrospinal fluid F2-isoprostane levels are increased in Alzheimer's disease Annals of Neurology 1998 44 3 410 413 (Pubitemid 28421451)
    • (1998) Annals of Neurology , vol.44 , Issue.3 , pp. 410-413
    • Montine, T.J.1    Markesbery, W.R.2    Morrow, J.D.3    Roberts II, L.J.4
  • 251
    • 0036284936 scopus 로고    scopus 로고
    • Increase of brain oxidative stress in mild cognitive impairment: A possible predictor of Alzheimer disease
    • Pratic D., Clark C. M., Liun F., Lee V. Y. M., Trojanowski J. Q., Increase of brain oxidative stress in mild cognitive impairment: a possible predictor of Alzheimer disease Archives of Neurology 2002 59 6 972 976 (Pubitemid 34640757)
    • (2002) Archives of Neurology , vol.59 , Issue.6 , pp. 972-976
    • Pratico, D.1    Clark, C.M.2    Liun, F.3    Lee, V.Y.-M.4    Trojanowski, J.Q.5
  • 252
    • 0033762711 scopus 로고    scopus 로고
    • Increased 8,12-iso-iPF2alpha-VI in Alzheimer's disease: Correlation of a noninvasive index of lipid peroxidation with disease severity
    • Pratico D., Clark C. M., Lee V. M., Trojanowski J. Q., Rokach J., FitzGerald G. A., Increased 8,12-iso-iPF2alpha-VI in Alzheimer's disease: correlation of a noninvasive index of lipid peroxidation with disease severity Annals of Neurology 2000 48 5 809 812
    • (2000) Annals of Neurology , vol.48 , Issue.5 , pp. 809-812
    • Pratico, D.1    Clark, C.M.2    Lee, V.M.3    Trojanowski, J.Q.4    Rokach, J.5    Fitzgerald, G.A.6
  • 253
    • 0034745018 scopus 로고    scopus 로고
    • 2-isoprostane concentrations in patients with Alzheimer disease, other dementias, and in age-matched controls
    • Montine T. J., Kaye J. A., Montine K. S., McFarland L., Morrow J. D., Quinn J. F., Cerebrospinal fluid A 42, tau, and F2-isoprostane concentrations in patients with Alzheimer disease, other dementias, and in age-matched controls Archives of Pathology and Laboratory Medicine 2001 125 4 510 512 (Pubitemid 32291556)
    • (2001) Archives of Pathology and Laboratory Medicine , vol.125 , Issue.4 , pp. 510-512
    • Montine, T.J.1    Kaye, J.A.2    Montine, K.S.3    McFarland, L.4    Morrow, J.D.5    Quinn, J.F.6
  • 259
    • 3242690571 scopus 로고    scopus 로고
    • 2-isoprostanes levels in the patients with Alzheimer's disease
    • DOI 10.1016/j.brainresbull.2004.04.016, PII S0361923004001236
    • Kim K. M., Jung B. H., Paeng K. J., Kim I., Chung B. C., Increased urinary F2-isoprostanes levels in the patients with Alzheimer's disease Brain Research Bulletin 2004 64 1 47 51 (Pubitemid 38953468)
    • (2004) Brain Research Bulletin , vol.64 , Issue.1 , pp. 47-51
    • Kim, K.M.1    Jung, B.H.2    Paeng, K.-J.3    Kim, I.4    Chung, B.C.5
  • 261
    • 35048845219 scopus 로고    scopus 로고
    • Plasma F2A isoprostane levels in Alzheimer's and Parkinson's disease
    • DOI 10.1159/000107699
    • Irizarry M. C., Yao Y., Hyman B. T., Growdon J. H., Pratic D., Plasma F2A isoprostane levels in Alzheimer's and Parkinson's disease Neurodegenerative Diseases 2007 4 6 403 405 (Pubitemid 47557280)
    • (2007) Neurodegenerative Diseases , vol.4 , Issue.6 , pp. 403-405
    • Irizarry, M.C.1    Yao, Y.2    Hyman, B.T.3    Growdon, J.H.4    Pratico, D.5
  • 263
    • 39749157595 scopus 로고    scopus 로고
    • Peripheral levels of glutathione and protein oxidation as markers in the development of Alzheimer's disease from Mild Cognitive Impairment
    • DOI 10.1080/10715760701861373, PII 790807039
    • Bermejo P., Martn-Aragn S., Bened J., Susn C., Felici E., Gil P., Ribera J. M., Villar. M., Peripheral levels of glutathione and protein oxidation as markers in the development of Alzheimer's disease from Mild Cognitive Impairment Free Radical Research 2008 42 2 162 170 (Pubitemid 351298365)
    • (2008) Free Radical Research , vol.42 , Issue.2 , pp. 162-170
    • Bermejo, P.1    Martin-Aragon, S.2    Benedi, J.3    Susin, C.4    Felici, E.5    Gil, P.6    Ribera, J.M.7    Villar, A.Ma.8
  • 264
    • 0032531735 scopus 로고    scopus 로고
    • Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation
    • Hensley K., Maidt M. L., Yu Z., Sang H., Markesbery W. R., Floyd R. A., Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation Journal of Neuroscience 1998 18 20 8126 8132 (Pubitemid 28464991)
    • (1998) Journal of Neuroscience , vol.18 , Issue.20 , pp. 8126-8132
    • Hensley, K.1    Maidt, M.L.2    Yu, Z.3    Sang, H.4    Markesbery, W.R.5    Floyd, R.A.6
  • 265
    • 0033516677 scopus 로고    scopus 로고
    • Alterations of 3-nitrotyrosine concentration in the cerebrospinal fluid during aging and in patients with Alzheimer's disease
    • DOI 10.1016/S0304-3940(99)00406-1, PII S0304394099004061
    • Tohgi H., Abe T., Yamazaki K., Murata T., Ishizaki E., Isobe C., Alterations of 3-nitrotyrosine concentration in the cerebrospinal fluid during aging and in patients with Alzheimer's disease Neuroscience Letters 1999 269 1 52 54 (Pubitemid 29305700)
    • (1999) Neuroscience Letters , vol.269 , Issue.1 , pp. 52-54
    • Tohgi, H.1    Abe, T.2    Yamazaki, K.3    Murata, T.4    Ishizaki, E.5    Isobe, C.6
  • 266
    • 1842788079 scopus 로고    scopus 로고
    • Cerebrospinal fluid levels of free 3-nitrotyrosine are not elevated in the majority of patients with amyotrophic lateral sclerosis or Alzheimer's disease
    • DOI 10.1016/j.neuint.2003.12.012, PII S0197018604000154
    • Ryberg H., Sderling A. S., Davidsson P., Blennow K., Caidahl K., Persson L. I., Cerebrospinal fluid levels of free 3-nitrotyrosine are not elevated in the majority of patients with amyotrophic lateral sclerosis or Alzheimer's disease Neurochemistry International 2004 45 1 57 62 (Pubitemid 38479564)
    • (2004) Neurochemistry International , vol.45 , Issue.1 , pp. 57-62
    • Ryberg, H.1    Soderling, A.-S.2    Davidsson, P.3    Blennow, K.4    Caidahl, K.5    Persson, L.I.6
  • 267
    • 0032933750 scopus 로고    scopus 로고
    • Increased DNA oxidation and decreased levels of repair products in Alzheimer's disease ventricular CSF
    • DOI 10.1046/j.1471-4159.1999.0720771.x
    • Lovell M. A., Gabbita S. P., Markesbery W. R., Increased DNA oxidation and decreased levels of repair products in Alzheimer's disease ventricular CSF Journal of Neurochemistry 1999 72 2 771 776 (Pubitemid 29055242)
    • (1999) Journal of Neurochemistry , vol.72 , Issue.2 , pp. 771-776
    • Lovell, M.A.1    Gabbita, S.P.2    Markesbery, W.R.3
  • 268
    • 0035105715 scopus 로고    scopus 로고
    • Ratio of 8-hydroxyguanine in intact DNA to free 8-hydroxyguanine is increased in Alzheimer disease ventricular cerebrospinal fluid
    • Lovell M. A., Markesbery W. R., Ratio of 8-hydroxyguanine in intact DNA to free 8-hydroxyguanine is increased in Alzheimer disease ventricular cerebrospinal fluid Archives of Neurology 2001 58 3 392 396 (Pubitemid 32217455)
    • (2001) Archives of Neurology , vol.58 , Issue.3 , pp. 392-396
    • Lovell, M.A.1    Markesbery, W.R.2
  • 269
    • 77951204459 scopus 로고    scopus 로고
    • Levels of reduced and oxidized coenzyme Q-10 and 8-hydroxy-2′- deoxyguanosine in the CSF of patients with Alzheimer's disease demonstrate that mitochondrial oxidative damage and/or oxidative DNA damage contributes to the neurodegenerative process
    • Isobe C., Abe T., Terayama Y., Levels of reduced and oxidized coenzyme Q-10 and 8-hydroxy-2′- deoxyguanosine in the CSF of patients with Alzheimer's disease demonstrate that mitochondrial oxidative damage and/or oxidative DNA damage contributes to the neurodegenerative process Journal of Neurology 2010 257 3 399 404
    • (2010) Journal of Neurology , vol.257 , Issue.3 , pp. 399-404
    • Isobe, C.1    Abe, T.2    Terayama, Y.3
  • 272
    • 34548162663 scopus 로고    scopus 로고
    • Increased urinary level of oxidized nucleosides in patients with mild-to-moderate Alzheimer's disease
    • DOI 10.1016/j.clinbiochem.2006.11.021, PII S0009912007000161
    • Hee Lee S., Kim I., Chul Chung B., Increased urinary level of oxidized nucleosides in patients with mild-to-moderate Alzheimer's disease Clinical Biochemistry 2007 40 13-14 936 938 (Pubitemid 47307331)
    • (2007) Clinical Biochemistry , vol.40 , Issue.13-14 , pp. 936-938
    • Hee Lee, S.1    Kim, I.2    Chul Chung, B.3
  • 273
    • 0037010314 scopus 로고    scopus 로고
    • Remarkable increase in the concentration of 8-hydroxyguanosine in cerebrospinal fluid from patients with Alzheimer's disease
    • DOI 10.1002/jnr.10349
    • Abe T., Tohgi H., Isobe C., Murata T., Sato C., Remarkable increase in the concentration of 8-hydroxyguanosine in cerebrospinal fluid from patients with Alzheimer's disease Journal of Neuroscience Research 2002 70 3 447 450 (Pubitemid 35222381)
    • (2002) Journal of Neuroscience Research , vol.70 , Issue.3 , pp. 447-450
    • Abe, T.1    Tohgi, H.2    Isobe, C.3    Murata, T.4    Sato, C.5
  • 274
    • 0027366364 scopus 로고
    • Decreased superoxide dismutase activity in erythrocytes from patients with Alzheimer's disease
    • Fernandes M. A. S., Santana I., Januario C., Cunha L., Oliveira C. R., Decreased superoxide dismutase activity in erythrocytes from patients with Alzheimer's disease Medical Science Research 1993 21 18 679 682 (Pubitemid 23284397)
    • (1993) Medical Science Research , vol.21 , Issue.18 , pp. 679-682
    • Fernandes, M.A.S.1    Santana, I.2    Januario, C.3    Cunha, L.4    Oliveira, C.R.5
  • 278
    • 0034193155 scopus 로고    scopus 로고
    • Vitamin E: Non-antioxidant roles
    • DOI 10.1016/S0163-7827(00)00006-0, PII S0163782700000060
    • Azzi A., Stocker A., Vitamin E: non-antioxidant roles Progress in Lipid Research 2000 39 3 231 255 (Pubitemid 30224705)
    • (2000) Progress in Lipid Research , vol.39 , Issue.3 , pp. 231-255
    • Azzi, A.1    Stocker, A.2
  • 281
    • 0035503597 scopus 로고    scopus 로고
    • The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse
    • Lim G. P., Chu T., Yang F., Beech W., Frautschy S. A., Cole G. M., The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse Journal of Neuroscience 2001 21 21 8370 8377 (Pubitemid 33051435)
    • (2001) Journal of Neuroscience , vol.21 , Issue.21 , pp. 8370-8377
    • Lim, G.P.1    Chu, T.2    Yang, F.3    Beech, W.4    Frautschy, S.A.5    Cole, G.M.6
  • 284
    • 0036164525 scopus 로고    scopus 로고
    • Influence of the severity of cognitive impairment on the effect of the Ginkgo biloba extract EGb 761 in Alzheimer's disease
    • DOI 10.1159/000048668
    • Le Bars P. L., Velasco F. M., Ferguson J. M., Dessain E. C., Kieser M., Hoerr R., Influence of the severity of cognitive impairment on the effect of the Ginkgo biloba extract EGb 761 in Alzheimer's disease Neuropsychobiology 2002 45 1 19 26 (Pubitemid 34117724)
    • (2002) Neuropsychobiology , vol.45 , Issue.1 , pp. 19-26
    • Le Bars, P.L.1    Velasco, F.M.2    Ferguson, J.M.3    Dessain, E.C.4    Kieser, M.5    Hoerr, R.6
  • 287
    • 57649221161 scopus 로고    scopus 로고
    • Evidence of oxidative stress in Alzheimer's disease brain and antioxidant therapy: Lights and shadows
    • Pratic D., Evidence of oxidative stress in Alzheimer's disease brain and antioxidant therapy: lights and shadows Annals of the New York Academy of Sciences 2008 1147 70 78
    • (2008) Annals of the New York Academy of Sciences , vol.1147 , pp. 70-78
    • Pratic, D.1
  • 289
    • 75149148788 scopus 로고    scopus 로고
    • Why vitamin e therapy fails for treatment of Alzheimer's disease
    • Brewer G. J., Why vitamin e therapy fails for treatment of Alzheimer's disease Journal of Alzheimer's Disease 2010 19 1 27 30
    • (2010) Journal of Alzheimer's Disease , vol.19 , Issue.1 , pp. 27-30
    • Brewer, G.J.1
  • 291
    • 77956207871 scopus 로고    scopus 로고
    • Mitochondria and antioxidant targeted therapeutic strategies for Alzheimer's disease
    • Dumont M., Lin M. T., Beal M. F., Mitochondria and antioxidant targeted therapeutic strategies for Alzheimer's disease Journal of Alzheimer's Disease 2010 20 supplement 2 S633 S643
    • (2010) Journal of Alzheimer's Disease , vol.20 , Issue.SUPPL. 2
    • Dumont, M.1    Lin, M.T.2    Beal, M.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.