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Volumn 28, Issue 5, 2012, Pages 631-640

Mitochondrial dysfunction and cellular metabolic deficiency in Alzheimer's disease

Author keywords

Alzheimer's disease; Amyloid ; Metabolic deficiency; Mitochondrial dysfunction

Indexed keywords

ALCOHOL DEHYDROGENASE; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; CELL SURFACE PROTEIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; LACTIC ACID; NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE;

EID: 84871452231     PISSN: 16737067     EISSN: 19958218     Source Type: Journal    
DOI: 10.1007/s12264-012-1270-2     Document Type: Review
Times cited : (38)

References (83)
  • 1
    • 80055039585 scopus 로고    scopus 로고
    • Amyloid-beta protein precursor family members: A review from homology to biological function
    • Huang HC, Jiang ZF. Amyloid-beta protein precursor family members: a review from homology to biological function. J Alzheimers Dis 2011, 26: 607-626.
    • (2011) J Alzheimers Dis , vol.26 , pp. 607-626
    • Huang, H.C.1    Jiang, Z.F.2
  • 2
    • 58849143335 scopus 로고    scopus 로고
    • Accumulated amyloid-beta peptide and hyperphosphorylated tau protein: Relationship and links in Alzheimer's disease
    • Huang HC, Jiang ZF. Accumulated amyloid-beta peptide and hyperphosphorylated tau protein: relationship and links in Alzheimer's disease. J Alzheimers Dis 2009, 16: 15-27.
    • (2009) J Alzheimers Dis , vol.16 , pp. 15-27
    • Huang, H.C.1    Jiang, Z.F.2
  • 3
    • 78751566697 scopus 로고    scopus 로고
    • Disrupted energy metabolism and neuronal circuit dysfunction in cognitive impairment and Alzheimer's disease
    • Kapogiannis D, Mattson MP. Disrupted energy metabolism and neuronal circuit dysfunction in cognitive impairment and Alzheimer's disease. Lancet Neurol 2011, 10: 187-198.
    • (2011) Lancet Neurol , vol.10 , pp. 187-198
    • Kapogiannis, D.1    Mattson, M.P.2
  • 4
    • 79955658979 scopus 로고    scopus 로고
    • Increased protein and lipid oxidative damage in mitochondria isolated from lymphocytes from patients with Alzheimer's disease: Insights into the role of oxidative stress in Alzheimer's disease and initial investigations into a potential biomarker for this dementing disorder
    • Sultana R, Mecocci P, Mangialasche F, Cecchetti R, Baglioni M, Butterfield DA. Increased protein and lipid oxidative damage in mitochondria isolated from lymphocytes from patients with Alzheimer's disease: insights into the role of oxidative stress in Alzheimer's disease and initial investigations into a potential biomarker for this dementing disorder. J Alzheimers Dis 2011, 24: 77-84.
    • (2011) J Alzheimers Dis , vol.24 , pp. 77-84
    • Sultana, R.1    Mecocci, P.2    Mangialasche, F.3    Cecchetti, R.4    Baglioni, M.5    Butterfield, D.A.6
  • 6
    • 0028796841 scopus 로고
    • Deficits in cerebral glucose metabolism demonstrated by positron emission tomography in individuals at risk of familial Alzheimer's disease
    • Kennedy AM, Frackowiak RS, Newman SK, Bloomfield PM, Seaward J, Roques P, et al. Deficits in cerebral glucose metabolism demonstrated by positron emission tomography in individuals at risk of familial Alzheimer's disease. Neurosci Lett 1995, 186: 17-20.
    • (1995) Neurosci Lett , vol.186 , pp. 17-20
    • Kennedy, A.M.1    Frackowiak, R.S.2    Newman, S.K.3    Bloomfield, P.M.4    Seaward, J.5    Roques, P.6
  • 7
    • 80055028073 scopus 로고    scopus 로고
    • Amyloid-beta and glucose metabolism in Alzheimer's disease
    • Furst AJ, Lal RA. Amyloid-beta and glucose metabolism in Alzheimer's disease. J Alzheimers Dis 2011, 26 (Suppl 3): 105-116.
    • (2011) J Alzheimers Dis , vol.26 SUPPL. 3 , pp. 105-116
    • Furst, A.J.1    Lal, R.A.2
  • 8
    • 1842785179 scopus 로고    scopus 로고
    • Glucose metabolism and insulin receptor signal transduction in Alzheimer disease
    • DOI 10.1016/j.ejphar.2004.02.049, PII S0014299904002067
    • Hoyer S. Glucose metabolism and insulin receptor signal transduction in Alzheimer disease. Eur J Pharmacol 2004, 490: 115-125. (Pubitemid 38482165)
    • (2004) European Journal of Pharmacology , vol.490 , Issue.1-3 , pp. 115-125
    • Hoyer, S.1
  • 9
    • 84858018995 scopus 로고    scopus 로고
    • The dying of the light: Mitochondrial failure in Alzheimer's disease
    • Young-Collier KJ, McArdle M, Bennett JP. The dying of the light: mitochondrial failure in Alzheimer's disease. J Alzheimers Dis 2012, 28: 771-781.
    • (2012) J Alzheimers Dis , vol.28 , pp. 771-781
    • Young-Collier, K.J.1    McArdle, M.2    Bennett, J.P.3
  • 11
    • 84871417031 scopus 로고    scopus 로고
    • Role of mitochondrial homeostasis and dynamics in Alzheimer's disease
    • doi:10.1016/j.nbd.2011.12.057
    • Selfridge JE, Lu J, Swerdlow RH. Role of mitochondrial homeostasis and dynamics in Alzheimer's disease. Neurobiol Dis 2012, doi:10.1016/j.nbd.2011.12. 057.
    • (2012) Neurobiol Dis
    • Selfridge, J.E.1    Lu, J.2    Swerdlow, R.H.3
  • 12
    • 84855687153 scopus 로고    scopus 로고
    • Impaired mitochondrial biogenesis contributes to mitochondrial dysfunction in Alzheimer's disease
    • Sheng B, Wang X, Su B, Lee HG, Casadesus G, Perry G, et al. Impaired mitochondrial biogenesis contributes to mitochondrial dysfunction in Alzheimer's disease. J Neurochem 2012, 120: 419-429.
    • (2012) J Neurochem , vol.120 , pp. 419-429
    • Sheng, B.1    Wang, X.2    Su, B.3    Lee, H.G.4    Casadesus, G.5    Perry, G.6
  • 13
    • 34547136377 scopus 로고    scopus 로고
    • Inhibition of dynamin-dependent endocytosis increases shedding of the amyloid precursor protein ectodomain and reduces generation of amyloid beta protein
    • Carey RM, Balcz BA, Lopez-Coviella I, Slack BE. Inhibition of dynamin-dependent endocytosis increases shedding of the amyloid precursor protein ectodomain and reduces generation of amyloid beta protein. BMC Cell Biol 2005, 6: 30.
    • (2005) BMC Cell Biol , vol.6 , pp. 30
    • Carey, R.M.1    Balcz, B.A.2    Lopez-Coviella, I.3    Slack, B.E.4
  • 14
    • 0029950149 scopus 로고    scopus 로고
    • Trafficking of cellsurface amyloid beta-protein precursor I. Secretion endocytosis and recycling as detected by labeled monoclonal antibody
    • Koo EH, Squazzo SL, Selkoe DJ, Koo CH. Trafficking of cellsurface amyloid beta-protein precursor. I. Secretion, endocytosis and recycling as detected by labeled monoclonal antibody. J Cell Sci 1996, 109 (Pt 5): 991-998.
    • (1996) J Cell Sci , vol.109 PART 5 , pp. 991-998
    • Koo, E.H.1    Squazzo, S.L.2    Selkoe, D.J.3    Koo, C.H.4
  • 15
    • 0029934134 scopus 로고    scopus 로고
    • Trafficking of cell-surface amyloid β-protein precursor: II. Endocytosis, recycling, and lysosomal targeting detected by immunolocalization
    • Yamazaki T, Koo EH, Selkoe DJ. Trafficking of cell-surface amyloid beta-protein precursor. II. Endocytosis, recycling and lysosomal targeting detected by immunolocalization. J Cell Sci 1996, 109 (Pt 5): 999-1008. (Pubitemid 126477168)
    • (1996) Journal of Cell Science , vol.109 , Issue.5 , pp. 999-1008
    • Yamazaki, T.1    Koo, E.H.2    Selkoe, D.J.3
  • 20
    • 2342495787 scopus 로고    scopus 로고
    • Amyloid β-peptide interactions with neuronal and glial cell plasma membrane: Binding sites and implications for Alzheimer's disease
    • DOI 10.1002/psc.573
    • Verdier Y, Zarandi M, Penke B. Amyloid beta-peptide interactions with neuronal and glial cell plasma membrane: binding sites and implications for Alzheimer's disease. J Pept Sci 2004, 10: 229-248. (Pubitemid 38594184)
    • (2004) Journal of Peptide Science , vol.10 , Issue.5 , pp. 229-248
    • Verdier, Y.1    Zarandi, M.2    Penke, B.3
  • 21
  • 23
    • 80051760335 scopus 로고    scopus 로고
    • In situ measurements of the formation and morphology of intracellular beta-amyloid fibrils by super-resolution fluorescence imaging
    • Kaminski Schierle GS, van de Linde S, Erdelyi M, Esbjorner EK, Klein T, Rees E, et al. In situ measurements of the formation and morphology of intracellular beta-amyloid fibrils by super-resolution fluorescence imaging. J Am Chem Soc 2011, 133: 12902-12905.
    • (2011) J Am Chem Soc , vol.133 , pp. 12902-12905
    • Kaminski Schierle, G.S.1    Van De Linde, S.2    Erdelyi, M.3    Esbjorner, E.K.4    Klein, T.5    Rees, E.6
  • 25
    • 34447564164 scopus 로고    scopus 로고
    • Intracellular Aβ and cognitive deficits precede β-amyloid deposition in transgenic arcAβ mice
    • DOI 10.1016/j.neurobiolaging.2006.06.019, PII S0197458006002259
    • Knobloch M, Konietzko U, Krebs DC, Nitsch RM. Intracellular Abeta and cognitive deficits precede beta-amyloid deposition in transgenic arcAbeta mice. Neurobiol Aging 2007, 28: 1297-1306. (Pubitemid 47081235)
    • (2007) Neurobiology of Aging , vol.28 , Issue.9 , pp. 1297-1306
    • Knobloch, M.1    Konietzko, U.2    Krebs, D.C.3    Nitsch, R.M.4
  • 28
    • 68549127183 scopus 로고    scopus 로고
    • Synaptic activity reduces intraneuronal Abeta, promotes APP transport to synapses, and protects against Abeta-related synaptic alterations
    • Tampellini D, Rahman N, Gallo EF, Huang Z, Dumont M, Capetillo- Zarate E, et al. Synaptic activity reduces intraneuronal Abeta, promotes APP transport to synapses, and protects against Abeta-related synaptic alterations. J Neurosci 2009, 29: 9704-9713.
    • (2009) J Neurosci , vol.29 , pp. 9704-9713
    • Tampellini, D.1    Rahman, N.2    Gallo, E.F.3    Huang, Z.4    Dumont, M.5    Capetillo- Zarate, E.6
  • 30
    • 84899571989 scopus 로고    scopus 로고
    • Intracellular accumulation of amyloid-Betaa predictor for synaptic dysfunction and neuron loss in Alzheimer's disease
    • Bayer TA, Wirths O. Intracellular accumulation of amyloid-Betaa predictor for synaptic dysfunction and neuron loss in Alzheimer's disease. Front Aging Neurosci 2010, 2: 8.
    • (2010) Front Aging Neurosci , vol.2 , Issue.8
    • Bayer, T.A.1    Wirths, O.2
  • 33
    • 39149122810 scopus 로고    scopus 로고
    • Amyloid beta, mitochondrial dysfunction and synaptic damage: Implications for cognitive decline in aging and Alzheimer's disease
    • Reddy PH, Beal MF. Amyloid beta, mitochondrial dysfunction and synaptic damage: implications for cognitive decline in aging and Alzheimer's disease. Trends Mol Med 2008, 14: 45-53.
    • (2008) Trends Mol Med , vol.14 , pp. 45-53
    • Reddy, P.H.1    Beal, M.F.2
  • 35
    • 0033046060 scopus 로고    scopus 로고
    • Binding of amyloid β-peptide to mitochondrial hydroxyacyl-CoA dehydrogenase (ERAB): Regulation of an SDR enzyme activity with implications for apoptosis in Alzheimer's disease
    • DOI 10.1016/S0014-5793(99)00586-4, PII S0014579399005864
    • Oppermann UC, Salim S, Tjernberg LO, Terenius L, Jornvall H. Binding of amyloid beta-peptide to mitochondrial hydroxyacyl- CoA dehydrogenase (ERAB): regulation of an SDR enzyme activity with implications for apoptosis in Alzheimer's disease. FEBS Lett 1999, 451: 238-242. (Pubitemid 29243784)
    • (1999) FEBS Letters , vol.451 , Issue.3 , pp. 238-242
    • Oppermann, U.C.T.1    Salim, S.2    Tjernberg, L.O.3    Terenius, L.4    Jornvall, H.5
  • 36
    • 20444441575 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and Alzheimer's disease: Role of amyloid-β peptide alcohol dehydrogenase (ABAD)
    • DOI 10.1111/j.0959-9673.2005.00427.x
    • Yan SD, Stern DM. Mitochondrial dysfunction and Alzheimer's disease: role of amyloid-beta peptide alcohol dehydrogenase (ABAD). Int J Exp Pathol 2005, 86: 161-171. (Pubitemid 40813912)
    • (2005) International Journal of Experimental Pathology , vol.86 , Issue.3 , pp. 161-171
    • Yan, S.D.1    Stern, D.M.2
  • 38
    • 79951548587 scopus 로고    scopus 로고
    • Inhibition of amyloid-beta (Abeta) peptide-binding alcohol dehydrogenase- Abeta interaction reduces Abeta accumulation and improves mitochondrial function in a mouse model of Alzheimer's disease
    • Yao J, Du H, Yan S, Fang F, Wang C, Lue LF, et al. Inhibition of amyloid-beta (Abeta) peptide-binding alcohol dehydrogenase- Abeta interaction reduces Abeta accumulation and improves mitochondrial function in a mouse model of Alzheimer's disease. J Neurosci 2011, 31: 2313-2320.
    • (2011) J Neurosci , vol.31 , pp. 2313-2320
    • Yao, J.1    Du, H.2    Yan, S.3    Fang, F.4    Wang, C.5    Lue, L.F.6
  • 39
    • 84856002072 scopus 로고    scopus 로고
    • Early induction of oxidative stress in mouse model of Alzheimer disease with reduced mitochondrial superoxide dismutase activity
    • Lee HP, Pancholi N, Esposito L, Previll LA, Wang X, Zhu X, et al. Early induction of oxidative stress in mouse model of Alzheimer disease with reduced mitochondrial superoxide dismutase activity. PLoS One 2012, 7: e28033.
    • (2012) PLoS One , vol.7
    • Lee, H.P.1    Pancholi, N.2    Esposito, L.3    Previll, L.A.4    Wang, X.5    Zhu, X.6
  • 40
    • 80052538857 scopus 로고    scopus 로고
    • Aging and amyloid beta-induced oxidative DNA damage and mitochondrial dysfunction in Alzheimer's disease: Implications for early intervention and therapeutics
    • Mao P, Reddy PH. Aging and amyloid beta-induced oxidative DNA damage and mitochondrial dysfunction in Alzheimer's disease: implications for early intervention and therapeutics. Biochim Biophys Acta 2011, 1812: 1359-1370.
    • (2011) Biochim Biophys Acta , vol.1812 , pp. 1359-1370
    • Mao, P.1    Reddy, P.H.2
  • 41
    • 77953257870 scopus 로고    scopus 로고
    • Involvements of the lipid peroxidation product, HNE, in the pathogenesis and progression of Alzheimer's disease
    • Butterfield DA, Bader Lange ML, Sultana R. Involvements of the lipid peroxidation product, HNE, in the pathogenesis and progression of Alzheimer's disease. Biochim Biophys Acta 2010, 1801: 924-929.
    • (2010) Biochim Biophys Acta , vol.1801 , pp. 924-929
    • Butterfield, D.A.1    Bader Lange, M.L.2    Sultana, R.3
  • 42
    • 78650142376 scopus 로고    scopus 로고
    • Protein oxidative modifications in the ageing brain: Consequence for the onset of neurodegenerative disease
    • Grimm S, Hoehn A, Davies KJ, Grune T. Protein oxidative modifications in the ageing brain: consequence for the onset of neurodegenerative disease. Free Radic Res 2011, 45: 73-88.
    • (2011) Free Radic Res , vol.45 , pp. 73-88
    • Grimm, S.1    Hoehn, A.2    Davies, K.J.3    Grune, T.4
  • 44
    • 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 TI, Lynn BC, Markesbery WR, Lovell MA. Increased levels of 4-hydroxynonenal and acrolein, neurotoxic markers of lipid peroxidation, in the brain in Mild Cognitive Impairment and early Alzheimer's disease. Neurobiol Aging 2006, 27: 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
  • 45
    • 77952672909 scopus 로고    scopus 로고
    • Increased levels of 4-hydroxynonenal and acrolein in the brain in preclinical Alzheimer disease
    • Bradley MA, Markesbery WR, Lovell MA. Increased levels of 4-hydroxynonenal and acrolein in the brain in preclinical Alzheimer disease. Free Radic Biol Med 2010, 48: 1570-1576.
    • (2010) Free Radic Biol Med , vol.48 , pp. 1570-1576
    • Bradley, M.A.1    Markesbery, W.R.2    Lovell, M.A.3
  • 47
    • 77953659232 scopus 로고    scopus 로고
    • Potential role of acrolein in neurodegeneration and in Alzheimer's disease
    • Nam DT, Arseneault M, Murthy V, Ramassamy C. Potential role of acrolein in neurodegeneration and in Alzheimer's disease. Curr Mol Pharmacol 2010, 3: 66-78.
    • (2010) Curr Mol Pharmacol , vol.3 , pp. 66-78
    • Nam, D.T.1    Arseneault, M.2    Murthy, V.3    Ramassamy, C.4
  • 48
    • 70350089195 scopus 로고    scopus 로고
    • Redox proteomics identification of 4-hydroxynonenalmodified brain proteins in Alzheimer's disease: Role of lipid peroxidation in Alzheimer's disease pathogenesis
    • Perluigi M, Sultana R, Cenini G, Di Domenico F, Memo M, Pierce WM, et al. Redox proteomics identification of 4-hydroxynonenalmodified brain proteins in Alzheimer's disease: Role of lipid peroxidation in Alzheimer's disease pathogenesis. Proteomics Clin Appl 2009, 3: 682-693.
    • (2009) Proteomics Clin Appl , vol.3 , pp. 682-693
    • Perluigi, M.1    Sultana, R.2    Cenini, G.3    Di Domenico, F.4    Memo, M.5    Pierce, W.M.6
  • 49
    • 0031020993 scopus 로고    scopus 로고
    • Amyloid β-peptide impairs glucose transport in hippocampal and cortical neurons: Involvement of membrane lipid peroxidation
    • Mark RJ, Pang Z, Geddes JW, Uchida K, Mattson MP. Amyloid beta-peptide impairs glucose transport in hippocampal and cortical neurons: involvement of membrane lipid peroxidation. J Neurosci 1997, 17: 1046-1054. (Pubitemid 27043963)
    • (1997) Journal of Neuroscience , vol.17 , Issue.3 , pp. 1046-1054
    • Mark, R.J.1    Pang, Z.2    Geddes, J.W.3    Uchida, K.4    Mattson, M.P.5
  • 50
    • 84864012821 scopus 로고    scopus 로고
    • Oxidative lipid modification of nicastrin enhances amyloidogenic gamma-secretase activity in Alzheimer's disease
    • doi: 10.1111/j.1474-9726.2012.00817.x
    • Gwon AR, Park JS, Arumugam TV, Kwon YK, Chan SL, Kim SH, et al. Oxidative lipid modification of nicastrin enhances amyloidogenic gamma-secretase activity in Alzheimer's disease. Aging Cell 2012, doi: 10.1111/j.1474-9726.2012.00817.x.
    • (2012) Aging Cell
    • Gwon, A.R.1    Park, J.S.2    Arumugam, T.V.3    Kwon, Y.K.4    Chan, S.L.5    Kim, S.H.6
  • 51
    • 1342306400 scopus 로고    scopus 로고
    • Acrolein inhibits NADH-linked mitochondrial enzyme activity: Implications for Alzheimer's disease
    • Pocernich CB, Butterfield DA. Acrolein inhibits NADH-linked mitochondrial enzyme activity: implications for Alzheimer's disease. Neurotox Res 2003, 5: 515-520.
    • (2003) Neurotox Res , vol.5 , pp. 515-520
    • Pocernich, C.B.1    Butterfield, D.A.2
  • 52
    • 38049010515 scopus 로고    scopus 로고
    • Oxidative DNA damage in mild cognitive impairment and late-stage Alzheimer's disease
    • Lovell MA, Markesbery WR. Oxidative DNA damage in mild cognitive impairment and late-stage Alzheimer's disease. Nucleic Acids Res 2007, 35: 7497-7504.
    • (2007) Nucleic Acids Res , vol.35 , pp. 7497-7504
    • Lovell, M.A.1    Markesbery, W.R.2
  • 53
    • 4344622376 scopus 로고    scopus 로고
    • Deficiency of the Mre11 DNA repair complex in Alzheimer's disease brains
    • DOI 10.1016/j.molbrainres.2004.05.023, PII S0169328X04002554
    • Jacobsen E, Beach T, Shen Y, Li R, Chang Y. Deficiency of the Mre11 DNA repair complex in Alzheimer's disease brains. Brain Res Mol Brain Res 2004, 128: 1-7. (Pubitemid 39158875)
    • (2004) Molecular Brain Research , vol.128 , Issue.1 , pp. 1-7
    • Jacobsen, E.1    Beach, T.2    Shen, Y.3    Li, R.4    Chang, Y.5
  • 54
    • 18844462415 scopus 로고    scopus 로고
    • Increased oxidative damage in nuclear and mitochondrial DNA in Alzheimer's disease
    • DOI 10.1111/j.1471-4159.2005.03053.x
    • Wang J, Xiong S, Xie C, Markesbery WR, Lovell MA. Increased oxidative damage in nuclear and mitochondrial DNA in Alzheimer's disease. J Neurochem 2005, 93: 953-962. (Pubitemid 40695754)
    • (2005) Journal of Neurochemistry , vol.93 , Issue.4 , pp. 953-962
    • Wang, J.1    Xiong, S.2    Xie, C.3    Markesbery, W.R.4    Lovell, M.A.5
  • 55
    • 81555195711 scopus 로고    scopus 로고
    • Mitochondria are related to synaptic pathology in Alzheimer's disease
    • Baloyannis SJ. Mitochondria are related to synaptic pathology in Alzheimer's disease. Int J Alzheimers Dis 2011, 2011: 305395.
    • (2011) Int J Alzheimers Dis 2011 , pp. 305395
    • Baloyannis, S.J.1
  • 58
    • 77958140445 scopus 로고    scopus 로고
    • Mitochondria on guard: Role of mitochondrial fusion and fission in the regulation of apoptosis
    • Karbowski M. Mitochondria on guard: role of mitochondrial fusion and fission in the regulation of apoptosis. Adv Exp Med Biol 2010, 687: 131-142.
    • (2010) Adv Exp Med Biol , vol.687 , pp. 131-142
    • Karbowski, M.1
  • 59
    • 77958130220 scopus 로고    scopus 로고
    • The interplay between BCL-2 family proteins and mitochondrial morphology in the regulation of apoptosis
    • Soriano ME, Scorrano L. The interplay between BCL-2 family proteins and mitochondrial morphology in the regulation of apoptosis. Adv Exp Med Biol 2010, 687: 97-114.
    • (2010) Adv Exp Med Biol , vol.687 , pp. 97-114
    • Soriano, M.E.1    Scorrano, L.2
  • 61
    • 84857046742 scopus 로고    scopus 로고
    • Fluorodeoxyglucose in patients with dementia with Lewy bodies
    • fluorodeoxyglucose in patients with dementia with Lewy bodies. J Neurol Sci 2012, 314: 111-119.
    • (2012) J Neurol Sci , vol.314 , pp. 111-119
  • 62
    • 77953124257 scopus 로고    scopus 로고
    • A metabolomic study of the CRND8 transgenic mouse model of Alzheimer's disease
    • Salek RM, Xia J, Innes A, Sweatman BC, Adalbert R, Randle S, et al. A metabolomic study of the CRND8 transgenic mouse model of Alzheimer's disease. Neurochem Int 2010, 56: 937-947.
    • (2010) Neurochem Int , vol.56 , pp. 937-947
    • Salek, R.M.1    Xia, J.2    Innes, A.3    Sweatman, B.C.4    Adalbert, R.5    Randle, S.6
  • 63
    • 0025011401 scopus 로고
    • Enzyme activities in relation to pH and lactate in postmortem brain in Alzheimertype and other dementias
    • Yates CM, Butterworth J, Tennant MC, Gordon A. Enzyme activities in relation to pH and lactate in postmortem brain in Alzheimertype and other dementias. J Neurochem 1990, 55: 1624-1630.
    • (1990) J Neurochem , vol.55 , pp. 1624-1630
    • Yates, C.M.1    Butterworth, J.2    Tennant, M.C.3    Gordon, A.4
  • 64
    • 78149485884 scopus 로고    scopus 로고
    • Lactic acid induces aberrant amyloid precursor protein processing by promoting its interaction with endoplasmic reticulum chaperone proteins
    • Xiang Y, Xu G, Weigel-Van Aken KA. Lactic acid induces aberrant amyloid precursor protein processing by promoting its interaction with endoplasmic reticulum chaperone proteins. PLoS One 2010, 5: e13820.
    • (2010) PLoS One , vol.5
    • Xiang, Y.1    Xu, G.2    Weigel-Van Aken, K.A.3
  • 65
    • 0015278655 scopus 로고
    • Control of the redox state of the nicotinamide-adenine dinucleotide couple in rat liver cytoplasm
    • Stubbs M, Veech RL, Krebs HA. Control of the redox state of the nicotinamide-adenine dinucleotide couple in rat liver cytoplasm. Biochem J 1972, 126: 59-65.
    • (1972) Biochem J , vol.126 , pp. 59-65
    • Stubbs, M.1    Veech, R.L.2    Krebs, H.A.3
  • 66
    • 0037040581 scopus 로고    scopus 로고
    • Regulation of corepressor function by nuclear NADH
    • DOI 10.1126/science.1069300
    • Zhang Q, Piston DW, Goodman RH. Regulation of corepressor function by nuclear NADH. Science 2002, 295: 1895-1897. (Pubitemid 34214127)
    • (2002) Science , vol.295 , Issue.5561 , pp. 1895-1897
    • Zhang, Q.1    Piston, D.W.2    Goodman, R.H.3
  • 67
    • 30444437034 scopus 로고    scopus 로고
    • Neuronal and astrocytic shuttle mechanisms for cytosolic-mitochondrial transfer of reducing equivalents: Current evidence and pharmacological tools
    • DOI 10.1016/j.bcp.2005.10.011, PII S0006295205006623
    • McKenna MC, Waagepetersen HS, Schousboe A, Sonnewald U. Neuronal and astrocytic shuttle mechanisms for cytosolic-mitochondrial transfer of reducing equivalents: current evidence and pharmacological tools. Biochem Pharmacol 2006, 71: 399-407. (Pubitemid 43077074)
    • (2006) Biochemical Pharmacology , vol.71 , Issue.4 , pp. 399-407
    • McKenna, M.C.1    Waagepetersen, H.S.2    Schousboe, A.3    Sonnewald, U.4
  • 68
    • 84871451491 scopus 로고    scopus 로고
    • Curcumin-mediated neuroprotection against amyloid-beta-induced mitochondrial dysfunction involves the inhibition of GSK-3beta
    • doi: 10.3233/ JAD-2012-120688
    • Huang HC, Xu K, Jiang ZF. Curcumin-mediated neuroprotection against amyloid-beta-induced mitochondrial dysfunction involves the inhibition of GSK-3beta. J Alzheimers Dis 2012, doi: 10.3233/ JAD-2012-120688.
    • (2012) J Alzheimers Dis
    • Huang, H.C.1    Xu, K.2    Jiang, Z.F.3
  • 69
    • 0032475957 scopus 로고    scopus 로고
    • The chaperone BiP/GRP78 binds to amyloid precursor protein and decreases Aβ40 and Aβ42 secretion
    • DOI 10.1074/jbc.273.40.25552
    • Yang Y, Turner RS, Gaut Jr. The chaperone BiP/GRP78 binds to amyloid precursor protein and decreases Abeta40 and Abeta42 secretion. J Biol Chem 1998, 273: 25552-25555. (Pubitemid 28475772)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.40 , pp. 25552-25555
    • Yang, Y.1    Turner, R.S.2    Gaut, J.R.3
  • 71
    • 0032973950 scopus 로고    scopus 로고
    • New insights into an old protein: The functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
    • DOI 10.1016/S0167-4838(99)00119-3, PII S0167483899001193
    • Sirover MA. New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase. Biochim Biophys Acta 1999, 1432: 159-184. (Pubitemid 29304525)
    • (1999) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1432 , Issue.2 , pp. 159-184
    • Sirover, M.A.1
  • 72
    • 34547957476 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase enhances transcriptional activity of androgen receptor in prostate cancer cells
    • DOI 10.1074/jbc.M610724200
    • Harada N, Yasunaga R, Higashimura Y, Yamaji R, Fujimoto K, Moss J, et al. Glyceraldehyde-3-phosphate dehydrogenase enhances transcriptional activity of androgen receptor in prostate cancer cells. J Biol Chem 2007, 282: 22651-22661. (Pubitemid 47267369)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.31 , pp. 22651-22661
    • Harada, N.1    Yasunaga, R.2    Higashimura, Y.3    Yamaji, R.4    Fujimoto, K.5    Moss, J.6    Inui, H.7    Nakano, Y.8
  • 74
    • 0035951872 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is required for vesicular transport in the early secretory pathway
    • Tisdale EJ. Glyceraldehyde-3-phosphate dehydrogenase is required for vesicular transport in the early secretory pathway. J Biol Chem 2001, 276: 2480-2486.
    • (2001) J Biol Chem , vol.276 , pp. 2480-2486
    • Tisdale, E.J.1
  • 75
    • 77954497959 scopus 로고    scopus 로고
    • Oxidatively modified glyceraldehyde- 3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: Many pathways to neurodegeneration
    • Butterfield DA, Hardas SS, Lange ML. Oxidatively modified glyceraldehyde- 3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: many pathways to neurodegeneration. J Alzheimers Dis 2010, 20: 369-393.
    • (2010) J Alzheimers Dis , vol.20 , pp. 369-393
    • Butterfield, D.A.1    Hardas, S.S.2    Lange, M.L.3
  • 77
    • 28744448949 scopus 로고    scopus 로고
    • Amyloid-β induces disulfide bonding and aggregation of GAPDH in Alzheimer's disease
    • DOI 10.1096/fj.05-4195fje
    • Cumming RC, Schubert D. Amyloid-beta induces disulfide bonding and aggregation of GAPDH in Alzheimer's disease. FASEB J 2005, 19: 2060-2062. (Pubitemid 41759765)
    • (2005) FASEB Journal , vol.19 , Issue.14 , pp. 2060-2062
    • Cumming, R.C.1    Schubert, D.2
  • 78
    • 18144406844 scopus 로고    scopus 로고
    • Proteomic analysis of neurofibrillary tangles in Alzheimer disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein
    • DOI 10.1096/fj.04-3210fje
    • Wang Q, Woltjer RL, Cimino PJ, Pan C, Montine KS, Zhang J, et al. Proteomic analysis of neurofibrillary tangles in Alzheimer disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein. FASEB J 2005, 19: 869-871. (Pubitemid 40617412)
    • (2005) FASEB Journal , vol.19 , Issue.7 , pp. 869-871
    • Wang, Q.1    Woltjer, R.L.2    Cimino, P.J.3    Pan, C.4    Montine, K.S.5    Zhang, J.6    Montine, T.J.7
  • 79
    • 0027314334 scopus 로고
    • Rat brain glyceraldehyde-3-phosphate dehydrogenase interacts with the recombinant cytoplasmic domain of Alzheimer's β-amyloid precursor protein
    • Schulze H, Schuler A, Stuber D, Dobeli H, Langen H, Huber G. Rat brain glyceraldehyde-3-phosphate dehydrogenase interacts with the recombinant cytoplasmic domain of Alzheimer's beta-amyloid precursor protein. J Neurochem 1993, 60: 1915-1922. (Pubitemid 23127600)
    • (1993) Journal of Neurochemistry , vol.60 , Issue.5 , pp. 1915-1922
    • Schulze, H.1    Schuler, A.2    Stuber, D.3    Dobeli, H.4    Langen, H.5    Huber, G.6
  • 80
    • 54549093577 scopus 로고    scopus 로고
    • Non-native glyceraldehyde-3-phosphate dehydrogenase can be an intrinsic component of amyloid structures
    • Naletova I, Schmalhausen E, Kharitonov A, Katrukha A, Saso L, Caprioli A, et al. Non-native glyceraldehyde-3-phosphate dehydrogenase can be an intrinsic component of amyloid structures. Biochim Biophys Acta 2008, 1784: 2052-2058.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 2052-2058
    • Naletova, I.1    Schmalhausen, E.2    Kharitonov, A.3    Katrukha, A.4    Saso, L.5    Caprioli, A.6
  • 82
    • 0029939002 scopus 로고    scopus 로고
    • Gene expression of ND4, a subunit of complex I of oxidative phosphorylation in mitochondria, is decreased in temporal cortex of brains of Alzheimer's disease patients
    • DOI 10.1016/0006-8993(95)01517-5
    • Fukuyama R, Hatanpaa K, Rapoport SI, Chandrasekaran K. Gene expression of ND4, a subunit of complex I of oxidative phosphorylation in mitochondria, is decreased in temporal cortex of brains of Alzheimer's disease patients. Brain Res 1996, 713: 290-293. (Pubitemid 26114850)
    • (1996) Brain Research , vol.713 , Issue.1-2 , pp. 290-293
    • Fukuyama, R.1    Hatanpaa, K.2    Rapoport, S.I.3    Chandrasekaran, K.4
  • 83
    • 2342628596 scopus 로고    scopus 로고
    • Differential expression of oxidative phosphorylation genes in patients with Alzheimer's disease: Implications for early mitochondrial dysfunction and oxidative damage
    • DOI 10.1385/NMM:5:2:147
    • Manczak M, Park BS, Jung Y, Reddy PH. Differential expression of oxidative phosphorylation genes in patients with Alzheimer's disease: implications for early mitochondrial dysfunction and oxidative damage. Neuromolecular Med 2004, 5: 147-162. (Pubitemid 38596548)
    • (2004) NeuroMolecular Medicine , vol.5 , Issue.2 , pp. 147-162
    • Manczak, M.1    Park, B.S.2    Jung, Y.3    Reddy, P.H.4


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