메뉴 건너뛰기




Volumn 7, Issue 8, 2012, Pages

Amyloid-β peptide binds to cytochrome C oxidase subunit 1

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; CYTOCHROME C OXIDASE; CYTOCHROME C OXIDASE SUBUNIT 1; UNCLASSIFIED DRUG;

EID: 84865200019     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0042344     Document Type: Article
Times cited : (84)

References (60)
  • 2
    • 5344277556 scopus 로고    scopus 로고
    • Deciphering the molecular basis of memory failure in Alzheimer's disease
    • Walsh DM, Selkoe DJ, (2004) Deciphering the molecular basis of memory failure in Alzheimer's disease. Neuron 44: 181-193.
    • (2004) Neuron , vol.44 , pp. 181-193
    • Walsh, D.M.1    Selkoe, D.J.2
  • 3
    • 7244236841 scopus 로고    scopus 로고
    • A modified beta-amyloid hypothesis: intraneuronal accumulation of the beta-amyloid peptide - the first step of a fatal cascade
    • Wirths O, Multhaup G, Bayer TA, (2004) A modified beta-amyloid hypothesis: intraneuronal accumulation of the beta-amyloid peptide- the first step of a fatal cascade. J Neurochem 91: 513-520.
    • (2004) J Neurochem , vol.91 , pp. 513-520
    • Wirths, O.1    Multhaup, G.2    Bayer, T.A.3
  • 4
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide
    • Haass C, Selkoe DJ, (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 8: 101-112.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 5
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-β in Alzheimer's disease
    • LaFerla F, Green KN, Oddo S, (2007) Intracellular amyloid-β in Alzheimer's disease. Nat Rev Neurosci 8: 499-509.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 499-509
    • LaFerla, F.1    Green, K.N.2    Oddo, S.3
  • 6
    • 77953019895 scopus 로고    scopus 로고
    • Intraneuronal beta-amyloid accumulation and synapse pathology in Alzheimer's disease
    • Gouras GK, Tampellini D, Takahashi RH, Capetillo-Zarate E, (2010) Intraneuronal beta-amyloid accumulation and synapse pathology in Alzheimer's disease. Acta Neuropathol 119: 523-541.
    • (2010) Acta Neuropathol , vol.119 , pp. 523-541
    • Gouras, G.K.1    Tampellini, D.2    Takahashi, R.H.3    Capetillo-Zarate, E.4
  • 8
    • 82355192272 scopus 로고    scopus 로고
    • The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer's disease
    • Ferreira ST, Klein WL, (2011) The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer's disease. Neurobiol Learn Mem 96: 529-543.
    • (2011) Neurobiol Learn Mem , vol.96 , pp. 529-543
    • Ferreira, S.T.1    Klein, W.L.2
  • 9
    • 8744276616 scopus 로고    scopus 로고
    • Amyloid beta-peptide (1-42) contributes to the oxidative stress and neurodegeneration found in Alzheimer disease brain
    • Butterfield DA, Boyd-Kimball D, (2004) Amyloid beta-peptide (1-42) contributes to the oxidative stress and neurodegeneration found in Alzheimer disease brain. Brain Pathol 14: 426-432.
    • (2004) Brain Pathol , vol.14 , pp. 426-432
    • Butterfield, D.A.1    Boyd-Kimball, D.2
  • 10
    • 1842504323 scopus 로고    scopus 로고
    • Redox-active metals, oxidative stress, and Alzheimer's disease pathology
    • Huang X, Moir RD, Tanzi RE, Bush AI, Rogers JT, (2004) Redox-active metals, oxidative stress, and Alzheimer's disease pathology. Ann NY Acad Sci 1012: 153-163.
    • (2004) Ann NY Acad Sci , vol.1012 , pp. 153-163
    • Huang, X.1    Moir, R.D.2    Tanzi, R.E.3    Bush, A.I.4    Rogers, J.T.5
  • 11
    • 33846047004 scopus 로고    scopus 로고
    • Pathways by which Abeta facilitates tau pathology
    • Blurton-Jones M, LaFerla FM, (2006) Pathways by which Abeta facilitates tau pathology. Curr Alzheimer Res 3: 437-448.
    • (2006) Curr Alzheimer Res , vol.3 , pp. 437-448
    • Blurton-Jones, M.1    LaFerla, F.M.2
  • 12
    • 77951251848 scopus 로고    scopus 로고
    • Calcium signaling and amyloid toxicity in Alzheimer disease
    • Demuro A, Parker I, Stutzmann GE, (2010) Calcium signaling and amyloid toxicity in Alzheimer disease. J Biol Chem 285: 12463-12468.
    • (2010) J Biol Chem , vol.285 , pp. 12463-12468
    • Demuro, A.1    Parker, I.2    Stutzmann, G.E.3
  • 13
    • 77955084717 scopus 로고    scopus 로고
    • Why pleiotropic interventions are needed for Alzheimer's disease
    • Frautschy SA, Cole GM, (2010) Why pleiotropic interventions are needed for Alzheimer's disease. Mol Neurobiol 41: 392-409.
    • (2010) Mol Neurobiol , vol.41 , pp. 392-409
    • Frautschy, S.A.1    Cole, G.M.2
  • 15
    • 1542377619 scopus 로고    scopus 로고
    • Toxicity of amyloid β peptide: tales of calcium, mitochondria, and oxidative stress
    • Canevari L, Abramov AY, Duchen MR, (2004) Toxicity of amyloid β peptide: tales of calcium, mitochondria, and oxidative stress. Neurochem Res 29: 637-650.
    • (2004) Neurochem Res , vol.29 , pp. 637-650
    • Canevari, L.1    Abramov, A.Y.2    Duchen, M.R.3
  • 16
    • 78649983748 scopus 로고    scopus 로고
    • Alzheimer's disease: effects of β-amyloid on mitochondria
    • Tillement L, Lecanu L, Papadopoulos V, (2011) Alzheimer's disease: effects of β-amyloid on mitochondria. Mitochondrion 11: 13-21.
    • (2011) Mitochondrion , vol.11 , pp. 13-21
    • Tillement, L.1    Lecanu, L.2    Papadopoulos, V.3
  • 17
    • 81455157378 scopus 로고    scopus 로고
    • Mitochondria dysfunction - the beginning of the end in Alzheimer's disease? Separate and synergistic modes of tau and amyloid-b toxicity
    • Eckert A, Schmitt K, Gotz J, (2011) Mitochondria dysfunction - the beginning of the end in Alzheimer's disease? Separate and synergistic modes of tau and amyloid-b toxicity. Alzheimers Res Ther 3: 15.
    • (2011) Alzheimers Res Ther , vol.3 , pp. 15
    • Eckert, A.1    Schmitt, K.2    Gotz, J.3
  • 18
    • 0037100213 scopus 로고    scopus 로고
    • Effect of amyloid beta-peptide on permeability transition pore: a comparative study
    • Moreira PI, Santos MS, Moreno A, Rego AC, Oliveira C, (2002) Effect of amyloid beta-peptide on permeability transition pore: a comparative study. J Neurosci Res 69: 257-267.
    • (2002) J Neurosci Res , vol.69 , pp. 257-267
    • Moreira, P.I.1    Santos, M.S.2    Moreno, A.3    Rego, A.C.4    Oliveira, C.5
  • 19
    • 0036272650 scopus 로고    scopus 로고
    • β-Amyloid inhibits integrated mitochondrial respiration and key enzyme activities
    • Casley CS, Canevari L, Land JM, Clark JB, Sharpe MA, (2002) β-Amyloid inhibits integrated mitochondrial respiration and key enzyme activities. J Neurochem 80: 91-100.
    • (2002) J Neurochem , vol.80 , pp. 91-100
    • Casley, C.S.1    Canevari, L.2    Land, J.M.3    Clark, J.B.4    Sharpe, M.A.5
  • 20
    • 33745608709 scopus 로고    scopus 로고
    • The spirostenol (22R, 25R)-20α-spirost-5-en-3β-yl hexanoate blocks mitochondrial uptake of Aβ in neuronal cells and prevents Aβ-induced impairment of mitochondrial function
    • Tillement L, Lecanu L, Yao W, Greeson J, Papadopoulos V, (2006) The spirostenol (22R, 25R)-20α-spirost-5-en-3β-yl hexanoate blocks mitochondrial uptake of Aβ in neuronal cells and prevents Aβ-induced impairment of mitochondrial function. Steroids 71: 725-735.
    • (2006) Steroids , vol.71 , pp. 725-735
    • Tillement, L.1    Lecanu, L.2    Yao, W.3    Greeson, J.4    Papadopoulos, V.5
  • 21
    • 67650732998 scopus 로고    scopus 로고
    • Impaired balance of mitochondrial fission and fussion in Alzheimer's disease
    • Wang X, Su B, Lee H-g, Li X, Perry G, et al. (2009) Impaired balance of mitochondrial fission and fussion in Alzheimer's disease. J Neurosci 29: 9090-9103.
    • (2009) J Neurosci , vol.29 , pp. 9090-9103
    • Wang, X.1    Su, B.2    Lee, H.-g.3    Li, X.4    Perry, G.5
  • 22
    • 77956199031 scopus 로고    scopus 로고
    • A synergistic dysfunction of mitochondrial fission/fusion dynamics and miitophagy in Alzheimer's disease
    • Santos RX, Correia SC, Wang X, Perry G, Smith MA, et al. (2010) A synergistic dysfunction of mitochondrial fission/fusion dynamics and miitophagy in Alzheimer's disease. J Alzheimers Dis 20: S401-S412.
    • (2010) J Alzheimers Dis , vol.20
    • Santos, R.X.1    Correia, S.C.2    Wang, X.3    Perry, G.4    Smith, M.A.5
  • 23
    • 69249211284 scopus 로고    scopus 로고
    • Mitochondrial dysfunction: an early event in Alzheimer pathology accumulates with age in AD transgenic mice
    • Hauptmann S, Scherping I, Drose S, Brandt U, Schulz KL, et al. (2009) Mitochondrial dysfunction: an early event in Alzheimer pathology accumulates with age in AD transgenic mice. Neurobiol Aging 30: 1574-1586.
    • (2009) Neurobiol Aging , vol.30 , pp. 1574-1586
    • Hauptmann, S.1    Scherping, I.2    Drose, S.3    Brandt, U.4    Schulz, K.L.5
  • 24
    • 0032810909 scopus 로고    scopus 로고
    • Beta-amyloid fragment 25-35 selectively decreases complex IV activity in isolated mitochondria
    • Canevari L, Clark JB, Bates TE, (1999) Beta-amyloid fragment 25-35 selectively decreases complex IV activity in isolated mitochondria. FEBS Lett 457: 131-134.
    • (1999) FEBS Lett , vol.457 , pp. 131-134
    • Canevari, L.1    Clark, J.B.2    Bates, T.E.3
  • 25
    • 19944433571 scopus 로고    scopus 로고
    • Copper-dependent inhibition of human cytochrome c oxidase by a dimeric comformer of amyloid-β 1-42
    • Crouch PJ, Blake R, Duce JA, Ciccotosto GD, Li QX, et al. (2005) Copper-dependent inhibition of human cytochrome c oxidase by a dimeric comformer of amyloid-β 1-42. J Neurosci 25: 672-679.
    • (2005) J Neurosci , vol.25 , pp. 672-679
    • Crouch, P.J.1    Blake, R.2    Duce, J.A.3    Ciccotosto, G.D.4    Li, Q.X.5
  • 26
    • 84859496195 scopus 로고    scopus 로고
    • Glutamatergic alterations and mitochondrial impairment in a murine model of Alzheimer disease
    • Cassano T, Serviddio G, Gaetani S, Romano A, Dipasquale P, et al. (2011) Glutamatergic alterations and mitochondrial impairment in a murine model of Alzheimer disease. Neurobiol Aging doi:10.1016/j.neurobiolaging.2011.09.021.
    • (2011) Neurobiol Aging
    • Cassano, T.1    Serviddio, G.2    Gaetani, S.3    Romano, A.4    Dipasquale, P.5
  • 27
    • 11144353586 scopus 로고    scopus 로고
    • ABAD directly links Aβ to mitochondrial toxicity in Alzheimer's disease
    • Lustbader JW, Cirilli M, Lin C, Xu HW, Takuma K, et al. (2004) ABAD directly links Aβ to mitochondrial toxicity in Alzheimer's disease. Science 304: 448-452.
    • (2004) Science , vol.304 , pp. 448-452
    • Lustbader, J.W.1    Cirilli, M.2    Lin, C.3    Xu, H.W.4    Takuma, K.5
  • 28
    • 0013079948 scopus 로고    scopus 로고
    • An intracellular protein that binds amyloid-β peptide and mediates neurotoxicity in Alzheimer's disease
    • Yan SD, Fu J, Soto C, Chen X, Zhu H, et al. (1997) An intracellular protein that binds amyloid-β peptide and mediates neurotoxicity in Alzheimer's disease. Nature 389: 689-695.
    • (1997) Nature , vol.389 , pp. 689-695
    • Yan, S.D.1    Fu, J.2    Soto, C.3    Chen, X.4    Zhu, H.5
  • 29
    • 20144388830 scopus 로고    scopus 로고
    • ABAD enhances A beta-induced cell stress via mitochondrial dysfunction
    • Takuma K, Yao J, Huang J, Xu H, Chen X, et al. (2005) ABAD enhances A beta-induced cell stress via mitochondrial dysfunction. FASEB J 19: 597-598.
    • (2005) FASEB J , vol.19 , pp. 597-598
    • Takuma, K.1    Yao, J.2    Huang, J.3    Xu, H.4    Chen, X.5
  • 30
    • 20444441575 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and Alzheimer's disease: role of amyloid-beta peptide alcohol dehydrogenase (ABAD)
    • Yan SD, Stern DM, (2005) Mitochondrial dysfunction and Alzheimer's disease: role of amyloid-beta peptide alcohol dehydrogenase (ABAD). Int J Exp Pathol 86: 161-171.
    • (2005) Int J Exp Pathol , vol.86 , pp. 161-171
    • Yan, S.D.1    Stern, D.M.2
  • 31
    • 79951548587 scopus 로고    scopus 로고
    • Inhibition of amyloid-beta (Aβ) peptide-binding alcohol dehydrogenase-Aβ interaction reduces Aβ accumulation and improves mitochondrial function in a mouse model of Alzheimer's disease
    • Yao J, Du H, Yan S, Fang F, Wang C, et al. (2011) Inhibition of amyloid-beta (Aβ) peptide-binding alcohol dehydrogenase-Aβ interaction reduces Aβ accumulation and improves mitochondrial function in a mouse model of Alzheimer's disease. J Neurosci 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
  • 32
    • 33644755673 scopus 로고    scopus 로고
    • Identification of amyloid-beta 1-42 binding protein fragments by screening of a human brain cDNA library
    • Munguia ME, Govezensky T, Martinez R, Manoutcharian K, Gevorkian G, (2006) Identification of amyloid-beta 1-42 binding protein fragments by screening of a human brain cDNA library. Neurosci Lett 397: 79-82.
    • (2006) Neurosci Lett , vol.397 , pp. 79-82
    • Munguia, M.E.1    Govezensky, T.2    Martinez, R.3    Manoutcharian, K.4    Gevorkian, G.5
  • 34
    • 77953540108 scopus 로고    scopus 로고
    • Novel amyloid-beta specific scFv and VH antibody fragments from human and mouse phage display antibody libraries
    • Medecigo M, Manoutcharian K, Vasilevko V, Govezensky T, Munguia ME, et al. (2010) Novel amyloid-beta specific scFv and VH antibody fragments from human and mouse phage display antibody libraries. J Neuroimmunol 223: 104-114.
    • (2010) J Neuroimmunol , vol.223 , pp. 104-114
    • Medecigo, M.1    Manoutcharian, K.2    Vasilevko, V.3    Govezensky, T.4    Munguia, M.E.5
  • 35
    • 0021271971 scopus 로고
    • Clinical diagnosis of Alzheimer's disease: report of the NINCDS-ADRDA Work Group under the auspices of Department of Health and Human services Task Force on Alzheimer's Disease
    • McKhann G, Drachman D, Folstein M, Katzman R, Price D, et al. (1984) Clinical diagnosis of Alzheimer's disease: report of the NINCDS-ADRDA Work Group under the auspices of Department of Health and Human services Task Force on Alzheimer's Disease. Neurology 34: 939-944.
    • (1984) Neurology , vol.34 , pp. 939-944
    • McKhann, G.1    Drachman, D.2    Folstein, M.3    Katzman, R.4    Price, D.5
  • 36
  • 37
    • 78649443534 scopus 로고    scopus 로고
    • Anti-11 [E]-pyroglutamate-modified amyloid β antibodies cross-react with other pathological Aβ species: relevante for immunotherapy
    • Perez-Garmendia R, Ibarra-Bracamontes V, Vasilevko V, Luna-Munoz J, Mena R, et al. (2010) Anti-11 [E]-pyroglutamate-modified amyloid β antibodies cross-react with other pathological Aβ species: relevante for immunotherapy. J Neuroimmunol 229: 248-255.
    • (2010) J Neuroimmunol , vol.229 , pp. 248-255
    • Perez-Garmendia, R.1    Ibarra-Bracamontes, V.2    Vasilevko, V.3    Luna-Munoz, J.4    Mena, R.5
  • 38
    • 0032483035 scopus 로고    scopus 로고
    • Solution Structure of Amyloid-β Peptide (1-40) in Water-Micelle Environment. Is the Membrane-Spanning Domain Where We Think It Is?
    • Coles M, Bicknell W, Watson AA, Fairlie DP, Craik DJ, (1998) Solution Structure of Amyloid-β Peptide (1-40) in Water-Micelle Environment. Is the Membrane-Spanning Domain Where We Think It Is? Biochemistry 37: 11064-11077.
    • (1998) Biochemistry , vol.37 , pp. 11064-11077
    • Coles, M.1    Bicknell, W.2    Watson, A.A.3    Fairlie, D.P.4    Craik, D.J.5
  • 39
    • 0006683046 scopus 로고    scopus 로고
    • HyperChem Professional release 8.0., Hypercube Inc
    • HyperChem Professional release 8.0., 2007. Molecular Modeling System. Hypercube Inc.
    • (2007) Molecular Modeling System
  • 40
    • 77952331283 scopus 로고    scopus 로고
    • Bovine Cytochrome C Oxidase Structures Enable O2 Reduction with Minimization of Reactive Oxygen and Provide a Proton-Pumping Gate
    • Muramoto K, Ohtab K, Shinzawa-Itoh K, Kandaa K, Taniguchi M, (2010) Bovine Cytochrome C Oxidase Structures Enable O2 Reduction with Minimization of Reactive Oxygen and Provide a Proton-Pumping Gate. Proc Natl Acad Sci U.S.A 107: 7740-7745.
    • (2010) Proc Natl Acad Sci U.S.A , vol.107 , pp. 7740-7745
    • Muramoto, K.1    Ohtab, K.2    Shinzawa-Itoh, K.3    Kandaa, K.4    Taniguchi, M.5
  • 46
    • 0028984919 scopus 로고
    • Long amyloid b-protein secreted from wild-type human neuroblastoma IMR-32 cells
    • Asami-Odaka A, Ishibashi Y, Kikuchi T, Kitada C, Suzuki N, (1995) Long amyloid b-protein secreted from wild-type human neuroblastoma IMR-32 cells. Biochemistry 34: 10272-10278.
    • (1995) Biochemistry , vol.34 , pp. 10272-10278
    • Asami-Odaka, A.1    Ishibashi, Y.2    Kikuchi, T.3    Kitada, C.4    Suzuki, N.5
  • 47
    • 26444588771 scopus 로고    scopus 로고
    • Gradual alteration of mitochondrial structure and function by β-amyloids: importance of membrane viscosity changes, energy deprivation, reactive oxygen species production, and cytochrome c release
    • Aleardi AM, Benard G, Augereau O, Malgat M, Talbot JC, et al. (2005) Gradual alteration of mitochondrial structure and function by β-amyloids: importance of membrane viscosity changes, energy deprivation, reactive oxygen species production, and cytochrome c release. J Bioenerg Biomembr 37: 207-225.
    • (2005) J Bioenerg Biomembr , vol.37 , pp. 207-225
    • Aleardi, A.M.1    Benard, G.2    Augereau, O.3    Malgat, M.4    Talbot, J.C.5
  • 48
    • 28744449206 scopus 로고    scopus 로고
    • Mitochondrial Abeta: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease
    • Caspersen C, Wang N, Yao J, Sosunov A, Chen X, et al. (2005) Mitochondrial Abeta: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease. FASEB J 19: 2040-2041.
    • (2005) FASEB J , vol.19 , pp. 2040-2041
    • Caspersen, C.1    Wang, N.2    Yao, J.3    Sosunov, A.4    Chen, X.5
  • 49
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of Ab accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression
    • Manczak M, Anekonda TS, Henson E, Park BS, Quinn J, et al. (2006) Mitochondria are a direct site of Ab accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression. Hum Mol Genet 15: 1437-1449.
    • (2006) Hum Mol Genet , vol.15 , pp. 1437-1449
    • Manczak, M.1    Anekonda, T.S.2    Henson, E.3    Park, B.S.4    Quinn, J.5
  • 50
    • 51349110166 scopus 로고    scopus 로고
    • The amyloid beta-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae
    • Hansson Petersen CA, Alikhani N, Behbahani H, Wiehager B, Pavlov PF, et al. (2008) The amyloid beta-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae. Proc Natl Acad Sci U S A 105: 13145-13150.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 13145-13150
    • Hansson Petersen, C.A.1    Alikhani, N.2    Behbahani, H.3    Wiehager, B.4    Pavlov, P.F.5
  • 51
    • 77953562457 scopus 로고    scopus 로고
    • Possible role of amyloid-beta, adenine nucleotide translocase and cyclophilin-D interaction in mitochondrial dysfunction of Alzheimer's disease
    • Singh P, Suman S, Chandna S, Das TK, (2009) Possible role of amyloid-beta, adenine nucleotide translocase and cyclophilin-D interaction in mitochondrial dysfunction of Alzheimer's disease. Bioinformation 3: 440-445.
    • (2009) Bioinformation , vol.3 , pp. 440-445
    • Singh, P.1    Suman, S.2    Chandna, S.3    Das, T.K.4
  • 52
    • 79952901937 scopus 로고    scopus 로고
    • Cyclophilin D deficiency improves mitochondrial function and learning and memory in aging Alzheimer disease mouse model
    • Du H, Guo L, Zhang W, Rydzewska M, Yan S, (2011) Cyclophilin D deficiency improves mitochondrial function and learning and memory in aging Alzheimer disease mouse model. Neurobiol Aging 32: 398-406.
    • (2011) Neurobiol Aging , vol.32 , pp. 398-406
    • Du, H.1    Guo, L.2    Zhang, W.3    Rydzewska, M.4    Yan, S.5
  • 53
    • 79251584617 scopus 로고    scopus 로고
    • Mitochondrial g-secretase participates in the metabolism of mitochondria-associated amyloid precursor protein
    • Pavlov PF, Wiehager B, Sakai J, Frykman S, Behbahani H, et al. (2011) Mitochondrial g-secretase participates in the metabolism of mitochondria-associated amyloid precursor protein. FASEB J 25: 78-88.
    • (2011) FASEB J , vol.25 , pp. 78-88
    • Pavlov, P.F.1    Wiehager, B.2    Sakai, J.3    Frykman, S.4    Behbahani, H.5
  • 54
    • 0034103586 scopus 로고    scopus 로고
    • Inherent abnormalities in energy metabolism in Alzheimer disease. Interaction with cerebrovascular compromise
    • Blass JP, Sheu RK, Gibson GE, (2000) Inherent abnormalities in energy metabolism in Alzheimer disease. Interaction with cerebrovascular compromise. Ann N Y Acad Sci 903: 204-221.
    • (2000) Ann N Y Acad Sci , vol.903 , pp. 204-221
    • Blass, J.P.1    Sheu, R.K.2    Gibson, G.E.3
  • 55
    • 70149093436 scopus 로고    scopus 로고
    • Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease
    • Yao J, Irwin R, Zhao L, Nilsen J, Hamilton RT, et al. (2009) Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease. Proc Natl Acad Sci U S A 106: 14670-14675.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 14670-14675
    • Yao, J.1    Irwin, R.2    Zhao, L.3    Nilsen, J.4    Hamilton, R.T.5
  • 56
    • 78649815388 scopus 로고    scopus 로고
    • Early deficits in synaptic mitochondria in an Alzheimer's disease mouse model
    • Du H, Guo L, Yan S, Sosunov AA, McKhann GM, et al. (2010) Early deficits in synaptic mitochondria in an Alzheimer's disease mouse model. Proc Natl Acad Sci U S A 107: 18670-18675.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 18670-18675
    • Du, H.1    Guo, L.2    Yan, S.3    Sosunov, A.A.4    McKhann, G.M.5
  • 57
    • 77956197971 scopus 로고    scopus 로고
    • Mitochondrial amyloid-beta levels are associated Ruth the extent of mitochondrial dysfunction in different brain regions and the degree of cognitive impairment in Alzheimer's transgenic mice
    • Dragicevic N, Mamcarz M, Zhu Y, Buzzeo R, Tan J, et al. (2010) Mitochondrial amyloid-beta levels are associated Ruth the extent of mitochondrial dysfunction in different brain regions and the degree of cognitive impairment in Alzheimer's transgenic mice. J Alzheimers Dis 20: S535-S550.
    • (2010) J Alzheimers Dis , vol.20
    • Dragicevic, N.1    Mamcarz, M.2    Zhu, Y.3    Buzzeo, R.4    Tan, J.5
  • 58
    • 0035378322 scopus 로고    scopus 로고
    • Functional mitochondia are required for amyloid b-mediated neurotoxicity
    • Cardoso SM, Santos S, Swerdlow RH, Oliveira CR, (2001) Functional mitochondia are required for amyloid b-mediated neurotoxicity. FASEB J 15: 1439-1441.
    • (2001) FASEB J , vol.15 , pp. 1439-1441
    • Cardoso, S.M.1    Santos, S.2    Swerdlow, R.H.3    Oliveira, C.R.4
  • 59
    • 35348923542 scopus 로고    scopus 로고
    • Cytochrome c oxidase deficiency in neurons decreases both oxidative stress and amyloid formation in a Mouse model of Alzheimer's disease
    • Fukui H, Diaz F, Garcia S, Moraes CT, (2007) Cytochrome c oxidase deficiency in neurons decreases both oxidative stress and amyloid formation in a Mouse model of Alzheimer's disease. Proc Natl Acad Sci U S A 104: 14163-14168.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 14163-14168
    • Fukui, H.1    Diaz, F.2    Garcia, S.3    Moraes, C.T.4
  • 60
    • 18144447465 scopus 로고    scopus 로고
    • Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase
    • Yoshikawa S, Shinzawa-Itoh K, Nakashima R, Yaono R, Yamashita E, et al. (1998) Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase. Science 280: 1723-1729.
    • (1998) Science , vol.280 , pp. 1723-1729
    • Yoshikawa, S.1    Shinzawa-Itoh, K.2    Nakashima, R.3    Yaono, R.4    Yamashita, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.