메뉴 건너뛰기




Volumn 14, Issue 10, 2008, Pages 1097-1105

Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; CALCIUM; CYCLOPHILIN D; OXYGEN;

EID: 53549129483     PISSN: 10788956     EISSN: 1546170X     Source Type: Journal    
DOI: 10.1038/nm.1868     Document Type: Article
Times cited : (810)

References (56)
  • 1
    • 0034612075 scopus 로고    scopus 로고
    • A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients
    • Mauren, I., Zierz, S. & Moller, H.J. A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients. Neurobiol. Aging 21, 455-462 (2000).
    • (2000) Neurobiol. Aging , vol.21 , pp. 455-462
    • Mauren, I.1    Zierz, S.2    Moller, H.J.3
  • 2
    • 0034512488 scopus 로고    scopus 로고
    • The mitochondrial spiral. An adequate cause of dementia in the Alzheimer's syndrome
    • Blass, J.P. The mitochondrial spiral. An adequate cause of dementia in the Alzheimer's syndrome. Ann. NY Acad. Sci. 924, 170-183 (2000).
    • (2000) Ann. NY Acad. Sci , vol.924 , pp. 170-183
    • Blass, J.P.1
  • 3
    • 0030923869 scopus 로고    scopus 로고
    • Calcium homeostasis and reactive oxygen species production in cells transformed by mitochondria from individuals with sporadic Alzheimer's disease
    • Sheehan, J.P. et al. Calcium homeostasis and reactive oxygen species production in cells transformed by mitochondria from individuals with sporadic Alzheimer's disease. J. Neurosci. 17, 4612-4622 (1997).
    • (1997) J. Neurosci , vol.17 , pp. 4612-4622
    • Sheehan, J.P.1
  • 4
    • 3042513691 scopus 로고    scopus 로고
    • Mitochondria dysfunction of Alzheimer's disease cybrids enhances Aβ toxicity
    • Cardoso, S.M., Santana, I., Swerdlow, R.H. & Oliveira, C.R. Mitochondria dysfunction of Alzheimer's disease cybrids enhances Aβ toxicity. J. Neurochem. 89, 1417-1426 (2004).
    • (2004) J. Neurochem , vol.89 , pp. 1417-1426
    • Cardoso, S.M.1    Santana, I.2    Swerdlow, R.H.3    Oliveira, C.R.4
  • 5
    • 33750683018 scopus 로고    scopus 로고
    • Alzheimer's APP mangles mitochondria
    • Lin, M.T. & Beal, M.F. Alzheimer's APP mangles mitochondria. Nat. Med. 12, 1241-1243 (2006).
    • (2006) Nat. Med , vol.12 , pp. 1241-1243
    • Lin, M.T.1    Beal, M.F.2
  • 6
    • 28744449206 scopus 로고    scopus 로고
    • Mitochondrial Aβ: A potential focal point for neuronal metabolic dysfunction in Alzheimer's disease
    • Caspersen, C. et al. Mitochondrial Aβ: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease. FASEB J. 19, 2040-2041 (2005).
    • (2005) FASEB J , vol.19 , pp. 2040-2041
    • Caspersen, C.1
  • 7
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: Implications for free radical generation and oxidative damage in disease progression
    • Manczak, M. et al. Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression. Hum. Mol. Genet. 15, 1437-1449 (2006).
    • (2006) Hum. Mol. Genet , vol.15 , pp. 1437-1449
    • Manczak, M.1
  • 8
    • 20144388830 scopus 로고    scopus 로고
    • ABAD enhances Aβ-induced cell stress via mitochondrial dysfunction
    • Takuma, K. et al. ABAD enhances Aβ-induced cell stress via mitochondrial dysfunction. FASEB J. 19, 597-598 (2005).
    • (2005) FASEB J , vol.19 , pp. 597-598
    • Takuma, K.1
  • 9
    • 11144353586 scopus 로고    scopus 로고
    • ABAD directly links Aβ to mitochondrial toxicity in Alzheimer's disease
    • Lustbader, J.W. et al. ABAD directly links Aβ to mitochondrial toxicity in Alzheimer's disease. Science 304, 448-452 (2004).
    • (2004) Science , vol.304 , pp. 448-452
    • Lustbader, J.W.1
  • 10
    • 33644845279 scopus 로고    scopus 로고
    • Amyloid precursor protein-mediated free radicals and oxidative damage: Implications for the development and progression of Alzheimer's disease
    • Reddy, P.H. Amyloid precursor protein-mediated free radicals and oxidative damage: implications for the development and progression of Alzheimer's disease. J. Neurochem. 96, 1-13 (2006).
    • (2006) J. Neurochem , vol.96 , pp. 1-13
    • Reddy, P.H.1
  • 11
    • 33746367134 scopus 로고    scopus 로고
    • Hepatitis C virus non-structural protein NS5A interacts with FKBP38 and inhibits apoptosis in Huh7 hepatoma cells
    • Wang, J. et al. Hepatitis C virus non-structural protein NS5A interacts with FKBP38 and inhibits apoptosis in Huh7 hepatoma cells. FEBS Lett. 580, 4392-4400 (2006).
    • (2006) FEBS Lett , vol.580 , pp. 4392-4400
    • Wang, J.1
  • 12
    • 33748744258 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and tau hyperphosphorylation in Ts1Cje, a mouse model for Down syndrome
    • Shukkur, E.A. et al. Mitochondrial dysfunction and tau hyperphosphorylation in Ts1Cje, a mouse model for Down syndrome. Hum. Mol. Genet. 15, 2752-2762 (2006).
    • (2006) Hum. Mol. Genet , vol.15 , pp. 2752-2762
    • Shukkur, E.A.1
  • 13
    • 0035341254 scopus 로고    scopus 로고
    • Mitochondrial abnormalities in Alzheimer's disease
    • Hirai, K. et al. Mitochondrial abnormalities in Alzheimer's disease. J. Neurosci. 21, 3017-3023 (2001).
    • (2001) J. Neurosci , vol.21 , pp. 3017-3023
    • Hirai, K.1
  • 14
    • 19944433571 scopus 로고    scopus 로고
    • Copper-dependent inhibition of human cytochrome c oxidase by a dimeric conformer of amyloid-β1-42
    • Crouch, P.J. et al. Copper-dependent inhibition of human cytochrome c oxidase by a dimeric conformer of amyloid-β1-42. J. Neurosci. 25, 672-679 (2005).
    • (2005) J. Neurosci , vol.25 , pp. 672-679
    • Crouch, P.J.1
  • 15
    • 33748283747 scopus 로고    scopus 로고
    • Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction
    • Devi, L., Prabhu, B.M., Galati, D.F., Avadhani, N.G. & Anandatheerthavarada, H.K. Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction. J. Neurosci. 26, 9057-9068 (2006).
    • (2006) J. Neurosci , vol.26 , pp. 9057-9068
    • Devi, L.1    Prabhu, B.M.2    Galati, D.F.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5
  • 16
    • 1542284022 scopus 로고    scopus 로고
    • Intra- and extracellular Aβ and PHF in clinically evaluated cases of Alzheimer's disease
    • Fernandez-Vizarra, P. et al. Intra- and extracellular Aβ and PHF in clinically evaluated cases of Alzheimer's disease. Histol. Histopathol. 19, 823-844 (2004).
    • (2004) Histol. Histopathol , vol.19 , pp. 823-844
    • Fernandez-Vizarra, P.1
  • 17
    • 41949098239 scopus 로고    scopus 로고
    • eds. Dawbarn, D. & Allen, S.J, Oxford University Press, Oxford
    • Chen, X., Stern, D. & Yan, S.D. in Neurobiology of Alzheimer's Disease (eds. Dawbarn, D. & Allen, S.J.) 227-244 (Oxford University Press, Oxford, 2007).
    • (2007) Neurobiology of Alzheimer's Disease , pp. 227-244
    • Chen, X.1    Stern, D.2    Yan, S.D.3
  • 18
    • 0035378322 scopus 로고    scopus 로고
    • Functional mitochondria are required for amyloid β-mediated neurotoxicity
    • Cardoso, S.M., Santos, S., Swerdlow, R.H. & Oliveira, C.R. Functional mitochondria are required for amyloid β-mediated neurotoxicity. FASEB J. 15, 1439-1441 (2001).
    • (2001) FASEB J , vol.15 , pp. 1439-1441
    • Cardoso, S.M.1    Santos, S.2    Swerdlow, R.H.3    Oliveira, C.R.4
  • 19
    • 4544280654 scopus 로고    scopus 로고
    • Mitochondria and aging: A role for the permeability transition?
    • Crompton, M. Mitochondria and aging: a role for the permeability transition? Aging Cell 3, 3-6 (2004).
    • (2004) Aging Cell , vol.3 , pp. 3-6
    • Crompton, M.1
  • 20
    • 0036478989 scopus 로고    scopus 로고
    • The permeability transition pore complex: Another view
    • Halestrap, A.P., McStay, G.P. & Clarke, S.J. The permeability transition pore complex: another view. Biochimie 84, 153-166 (2002).
    • (2002) Biochimie , vol.84 , pp. 153-166
    • Halestrap, A.P.1    McStay, G.P.2    Clarke, S.J.3
  • 21
    • 15844404722 scopus 로고    scopus 로고
    • Halestrap, A. Biochemistry: a pore way to die. Nature 434, 578-579 (2005).
    • Halestrap, A. Biochemistry: a pore way to die. Nature 434, 578-579 (2005).
  • 22
    • 27644597606 scopus 로고    scopus 로고
    • Mitochondrial permeability transition in apoptosis and necrosis
    • Zamzami, N., Larochette, N. & Kroemer, G. Mitochondrial permeability transition in apoptosis and necrosis. Cell Death Differ. 12 Suppl 2, 1478-1480 (2005).
    • (2005) Cell Death Differ , vol.12 , Issue.SUPPL. 2 , pp. 1478-1480
    • Zamzami, N.1    Larochette, N.2    Kroemer, G.3
  • 23
    • 0036479049 scopus 로고    scopus 로고
    • Mitochondrial intermembrane junctional complexes and their involvement in cell death
    • Crompton, M., Barksby, E., Johnson, N. & Capano, M. Mitochondrial intermembrane junctional complexes and their involvement in cell death. Biochimie 84, 143-152 (2002).
    • (2002) Biochimie , vol.84 , pp. 143-152
    • Crompton, M.1    Barksby, E.2    Johnson, N.3    Capano, M.4
  • 24
    • 33645994183 scopus 로고    scopus 로고
    • Calcium, mitochondria and reperfusion injury: A pore way to die
    • Halestrap, A.P. Calcium, mitochondria and reperfusion injury: a pore way to die. Biochem. Soc. Trans. 34, 232-237 (2006).
    • (2006) Biochem. Soc. Trans , vol.34 , pp. 232-237
    • Halestrap, A.P.1
  • 25
    • 33646255246 scopus 로고    scopus 로고
    • The mitochondrial permeability transition from in vitro artifact to disease target
    • Bernardi, P. et al. The mitochondrial permeability transition from in vitro artifact to disease target. FEBS J. 273, 2077-2099 (2006).
    • (2006) FEBS J , vol.273 , pp. 2077-2099
    • Bernardi, P.1
  • 26
    • 0032401567 scopus 로고    scopus 로고
    • Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore
    • Crompton, M., Virji, S. & Ward, J.M. Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore. Eur. J. Biochem. 258, 729-735 (1998).
    • (1998) Eur. J. Biochem , vol.258 , pp. 729-735
    • Crompton, M.1    Virji, S.2    Ward, J.M.3
  • 27
    • 0031013623 scopus 로고    scopus 로고
    • Oxidative stress, thiol reagents, and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase
    • Halestrap, A.P., Woodfield, K.Y. & Connern, C.P. Oxidative stress, thiol reagents, and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase. J. Biol. Chem. 272, 3346-3354 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 3346-3354
    • Halestrap, A.P.1    Woodfield, K.Y.2    Connern, C.P.3
  • 28
    • 0028075423 scopus 로고
    • Recruitment of mitochondrial cyclophilin to the mitochondrial inner membrane under conditions of oxidative stress that enhance the opening of a calcium-sensitive non-specific channel
    • Connern, C.P. & Halestrap, A.P. Recruitment of mitochondrial cyclophilin to the mitochondrial inner membrane under conditions of oxidative stress that enhance the opening of a calcium-sensitive non-specific channel. Biochem. J. 302, 321-324 (1994).
    • (1994) Biochem. J , vol.302 , pp. 321-324
    • Connern, C.P.1    Halestrap, A.P.2
  • 29
    • 0033393804 scopus 로고    scopus 로고
    • Cyclophilins and their possible role in the stress response
    • Andreeva, L., Heads, R. & Green, C.J. Cyclophilins and their possible role in the stress response. Int. J. Exp. Pathol. 80, 305-315 (1999).
    • (1999) Int. J. Exp. Pathol , vol.80 , pp. 305-315
    • Andreeva, L.1    Heads, R.2    Green, C.J.3
  • 30
    • 15844375853 scopus 로고    scopus 로고
    • Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death
    • Baines, C.P. et al. Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature 434, 658-662 (2005).
    • (2005) Nature , vol.434 , pp. 658-662
    • Baines, C.P.1
  • 31
    • 0032571294 scopus 로고    scopus 로고
    • The overexpression of Bax produces cell death upon induction of the mitochondrial permeability transition
    • Pastorino, J.G., Chen, S.T., Tafani, M., Snyder, J.W. & Farber, J.L. The overexpression of Bax produces cell death upon induction of the mitochondrial permeability transition. J. Biol. Chem. 273, 7770-7775 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 7770-7775
    • Pastorino, J.G.1    Chen, S.T.2    Tafani, M.3    Snyder, J.W.4    Farber, J.L.5
  • 32
    • 15844407874 scopus 로고    scopus 로고
    • Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death
    • Nakagawa, T. et al. Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature 434, 652-658 (2005).
    • (2005) Nature , vol.434 , pp. 652-658
    • Nakagawa, T.1
  • 33
    • 21244446551 scopus 로고    scopus 로고
    • Properties of the permeability transition pore in mitochondria devoid of cyclophilin D
    • Basso, E. et al. Properties of the permeability transition pore in mitochondria devoid of cyclophilin D. J. Biol. Chem. 280, 18558-18561 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 18558-18561
    • Basso, E.1
  • 34
    • 24744460273 scopus 로고    scopus 로고
    • Cyclophilin D is a component of mitochondrial permeability transition and mediates neuronal cell death after focal cerebral ischemia
    • Schinzel, A.C. et al. Cyclophilin D is a component of mitochondrial permeability transition and mediates neuronal cell death after focal cerebral ischemia. Proc. Natl. Acad. Sci. USA 102, 12005-12010 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 12005-12010
    • Schinzel, A.C.1
  • 35
    • 33847051684 scopus 로고    scopus 로고
    • Surface plasmon resonance and nuclear magnetic resonance studies of ABAD-Ab interaction
    • Yan, Y. et al. Surface plasmon resonance and nuclear magnetic resonance studies of ABAD-Ab interaction. Biochemistry 46, 1724-1731 (2007).
    • (2007) Biochemistry , vol.46 , pp. 1724-1731
    • Yan, Y.1
  • 36
    • 15844369794 scopus 로고    scopus 로고
    • Surface plasmon resonance for the analysis of β-amyloid interactions and fibril formation in Alzheimer's disease research
    • Aguilar, M.I. & Small, D.H. Surface plasmon resonance for the analysis of β-amyloid interactions and fibril formation in Alzheimer's disease research. Neurotox. Res. 7, 17-27 (2005).
    • (2005) Neurotox. Res , vol.7 , pp. 17-27
    • Aguilar, M.I.1    Small, D.H.2
  • 37
    • 38149041804 scopus 로고    scopus 로고
    • Immunogold quantification of amino acids and proteins in complex subcellular compartments
    • Bergersen, L.H., Storm-Mathisen, J. & Gundersen, V. Immunogold quantification of amino acids and proteins in complex subcellular compartments. Nat. Protoc. 3, 144-152 (2008).
    • (2008) Nat. Protoc , vol.3 , pp. 144-152
    • Bergersen, L.H.1    Storm-Mathisen, J.2    Gundersen, V.3
  • 38
    • 0036792096 scopus 로고    scopus 로고
    • Amyloid β-peptide inhibition of the PKA/CREB pathway and long-term potentiation: Reversibility by drugs that enhance cAMP signaling
    • Vitolo, O.V. et al. Amyloid β-peptide inhibition of the PKA/CREB pathway and long-term potentiation: reversibility by drugs that enhance cAMP signaling. Proc. Natl. Acad. Sci. USA 99, 13217-13221 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13217-13221
    • Vitolo, O.V.1
  • 39
    • 0032548843 scopus 로고    scopus 로고
    • A role for superoxide in protein kinase C activation and induction of long-term potentiation
    • Klann, E., Roberson, E.D., Knapp, L.T. & Sweatt, J.D. A role for superoxide in protein kinase C activation and induction of long-term potentiation. J. Biol. Chem. 273, 4516-4522 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 4516-4522
    • Klann, E.1    Roberson, E.D.2    Knapp, L.T.3    Sweatt, J.D.4
  • 40
    • 0344393017 scopus 로고    scopus 로고
    • Paradoxical actions of hydrogen peroxide on longterm potentiation in transgenic superoxide dismutase-1 mice
    • Kamsler, A. & Segal, M. Paradoxical actions of hydrogen peroxide on longterm potentiation in transgenic superoxide dismutase-1 mice. J. Neurosci. 23, 10359-10367 (2003).
    • (2003) J. Neurosci , vol.23 , pp. 10359-10367
    • Kamsler, A.1    Segal, M.2
  • 41
    • 34447498864 scopus 로고    scopus 로고
    • High cyclophilin D content of synaptic mitochondria results in increased vulnerability to permeability transition
    • Naga, K.K., Sullivan, P.G. & Geddes, J.W. High cyclophilin D content of synaptic mitochondria results in increased vulnerability to permeability transition. J. Neurosci. 27, 7469-7475 (2007).
    • (2007) J. Neurosci , vol.27 , pp. 7469-7475
    • Naga, K.K.1    Sullivan, P.G.2    Geddes, J.W.3
  • 42
    • 34547726790 scopus 로고    scopus 로고
    • Role of cyclophilin D in the resistance of brain mitochondria to the permeability transition
    • Eliseev, R.A. et al. Role of cyclophilin D in the resistance of brain mitochondria to the permeability transition. Neurobiol. Aging 28, 1532-1542 (2007).
    • (2007) Neurobiol. Aging , vol.28 , pp. 1532-1542
    • Eliseev, R.A.1
  • 43
    • 0037192392 scopus 로고    scopus 로고
    • Induction of cytochrome c-mediated apoptosis by amyloid b 25-35 requires functional mitochondria
    • Morais Cardoso, S., Swerdlow, R.H. & Oliveira, C.R. Induction of cytochrome c-mediated apoptosis by amyloid b 25-35 requires functional mitochondria. Brain Res. 931, 117-125 (2002).
    • (2002) Brain Res , vol.931 , pp. 117-125
    • Morais Cardoso, S.1    Swerdlow, R.H.2    Oliveira, C.R.3
  • 44
    • 0037100213 scopus 로고    scopus 로고
    • Effect of amyloid b-peptide on permeability transition pore: A comparative study
    • Moreira, P.I., Santos, M.S., Moreno, A., Rego, A.C. & Oliveira, C. Effect of amyloid b-peptide on permeability transition pore: a comparative study. J. Neurosci. Res. 69, 257-267 (2002).
    • (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
  • 45
    • 0034730446 scopus 로고    scopus 로고
    • Methamphetamine toxicity is attenuated in mice that overexpress human manganese superoxide dismutase
    • Maragos, W.F. et al. Methamphetamine toxicity is attenuated in mice that overexpress human manganese superoxide dismutase. Brain Res. 878, 218-222 (2000).
    • (2000) Brain Res , vol.878 , pp. 218-222
    • Maragos, W.F.1
  • 46
    • 0028180518 scopus 로고
    • A model for b-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: Relevance to Alzheimer disease
    • Hensley, K. et al. A model for b-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease. Proc. Natl. Acad. Sci. USA 91, 3270-3274 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3270-3274
    • Hensley, K.1
  • 47
    • 8444227821 scopus 로고    scopus 로고
    • Reactive oxygen species and synaptic plasticity in the aging hippocampus
    • Serrano, F. & Klann, E. Reactive oxygen species and synaptic plasticity in the aging hippocampus. Ageing Res. Rev. 3, 431-443 (2004).
    • (2004) Ageing Res. Rev , vol.3 , pp. 431-443
    • Serrano, F.1    Klann, E.2
  • 48
    • 0038491473 scopus 로고    scopus 로고
    • Reversal of age-related learning deficits and brain oxidative stress in mice with superoxide dismutase/catalase mimetics
    • Liu, R. et al. Reversal of age-related learning deficits and brain oxidative stress in mice with superoxide dismutase/catalase mimetics. Proc. Natl. Acad. Sci. USA 100, 8526-8531 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8526-8531
    • Liu, R.1
  • 49
    • 33646922865 scopus 로고    scopus 로고
    • Reduction in mitochondrial superoxide dismutase modulates Alzheimer's disease-like pathology and accelerates the onset of behavioral changes in human amyloid precursor protein transgenic mice
    • Esposito, L. et al. Reduction in mitochondrial superoxide dismutase modulates Alzheimer's disease-like pathology and accelerates the onset of behavioral changes in human amyloid precursor protein transgenic mice. J. Neurosci. 26, 5167-5179 (2006).
    • (2006) J. Neurosci , vol.26 , pp. 5167-5179
    • Esposito, L.1
  • 50
    • 8144223671 scopus 로고    scopus 로고
    • RAGE potentiates Aβ-induced perturbation of neuronal function in transgenic mice
    • Arancio, O. et al. RAGE potentiates Aβ-induced perturbation of neuronal function in transgenic mice. EMBO J. 23, 4096-4105 (2004).
    • (2004) EMBO J , vol.23 , pp. 4096-4105
    • Arancio, O.1
  • 51
    • 0013615899 scopus 로고    scopus 로고
    • RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
    • Yan, S.D. et al. RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease. Nature 382, 685-691 (1996).
    • (1996) Nature , vol.382 , pp. 685-691
    • Yan, S.D.1
  • 52
    • 25444457995 scopus 로고    scopus 로고
    • Calcium-regulated signaling pathways: Role in amyloid β-induced synaptic dysfunction
    • Xie, C.W. Calcium-regulated signaling pathways: role in amyloid β-induced synaptic dysfunction. Neuromolecular Med. 6, 53-64 (2004).
    • (2004) Neuromolecular Med , vol.6 , pp. 53-64
    • Xie, C.W.1
  • 53
    • 41549089757 scopus 로고    scopus 로고
    • Receptor for advanced glycation end product-dependent activation of p38 mitogen-activated protein kinase contributes to amyloid-β-mediated cortical synaptic dysfunction
    • Origlia, N. et al. Receptor for advanced glycation end product-dependent activation of p38 mitogen-activated protein kinase contributes to amyloid-β-mediated cortical synaptic dysfunction. J. Neurosci. 28, 3521-3530 (2008).
    • (2008) J. Neurosci , vol.28 , pp. 3521-3530
    • Origlia, N.1
  • 54
    • 0036232299 scopus 로고    scopus 로고
    • Receptor for advanced glycation end products on human synovial fibroblasts: Role in the pathogenesis of dialysis-related amyloidosis
    • Hou, F.F. et al. Receptor for advanced glycation end products on human synovial fibroblasts: role in the pathogenesis of dialysis-related amyloidosis. J. Am. Soc. Nephrol. 13, 1296-1306 (2002).
    • (2002) J. Am. Soc. Nephrol , vol.13 , pp. 1296-1306
    • Hou, F.F.1
  • 55
    • 0031974368 scopus 로고    scopus 로고
    • Mitocondrial susceptibility to oxidative stress exacerbates cerebral infarction that follows permanent focal cerebral ischemia in mutant mice with manganese superoxide dismutase deficiency
    • Murakami, K. et al. Mitocondrial susceptibility to oxidative stress exacerbates cerebral infarction that follows permanent focal cerebral ischemia in mutant mice with manganese superoxide dismutase deficiency. J. Neurosci. 18, 205-213 (1998).
    • (1998) J. Neurosci , vol.18 , pp. 205-213
    • Murakami, K.1
  • 56
    • 0033007651 scopus 로고    scopus 로고
    • Differences in the activation of the mitochondrial permeability transition among brain regions in the rat correlate with selective vulnerability
    • Friberg, H., Connern, C., Halestrap, A.P. & Wieloch, T. Differences in the activation of the mitochondrial permeability transition among brain regions in the rat correlate with selective vulnerability. J. Neurochem. 72, 2488-2497 (1999).
    • (1999) J. Neurochem , vol.72 , pp. 2488-2497
    • Friberg, H.1    Connern, C.2    Halestrap, A.P.3    Wieloch, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.