메뉴 건너뛰기




Volumn 9, Issue 2, 2006, Pages 127-137

Mitochondrial amyloid-beta peptide: Pathogenesis or late-phase development?

Author keywords

Alzheimer's disease; Apoptosis; Neurodegeneration; Reactive oxygen species; Respiratory chain complex

Indexed keywords

AMYLOID BETA PROTEIN; GAMMA SECRETASE; REACTIVE OXYGEN METABOLITE; SERINE PROTEINASE OMI;

EID: 33746080833     PISSN: 13872877     EISSN: None     Source Type: Journal    
DOI: 10.3233/jad-2006-9205     Document Type: Review
Times cited : (16)

References (96)
  • 1
    • 0035378322 scopus 로고    scopus 로고
    • Functional mitochondria are required for Aβ-mediated neurotoxicity
    • S. Cardoso, S. Santo, R. Swerdlow and C. Oliveira, Functional mitochondria are required for Aβ-mediated neurotoxicity, FASEB J 15 (2001), 1439-1441.
    • (2001) FASEB J , vol.15 , pp. 1439-1441
    • Cardoso, S.1    Santo, S.2    Swerdlow, R.3    Oliveira, C.4
  • 2
    • 0028236018 scopus 로고
    • Electron transport chain defects in Alzheimer's disease brain
    • W. Parker, J. Parks, C. Filley and B. Kleinschmidt-DeMasters, Electron transport chain defects in Alzheimer's disease brain, Neurology 44 (1994), 1090-1096.
    • (1994) Neurology , vol.44 , pp. 1090-1096
    • Parker, W.1    Parks, J.2    Filley, C.3    Kleinschmidt-DeMasters, B.4
  • 4
    • 0028110234 scopus 로고
    • Cortical cytochrome oxidase activity is reduced in Alzheimer's disease
    • E. Mutisya, A. Bowling and M. Beal, Cortical cytochrome oxidase activity is reduced in Alzheimer's disease, J. Neurochem. 63 (1994), 21769-22784.
    • (1994) J. Neurochem. , vol.63 , pp. 21769-22784
    • Mutisya, E.1    Bowling, A.2    Beal, M.3
  • 5
    • 0034612075 scopus 로고    scopus 로고
    • A selective defect of cytochrome c oxidase is present in brains of Alzheimer disease patients
    • I. Maurer, X. Zierz and H-J. Moller, A selective defect of cytochrome c oxidase is present in brains of Alzheimer disease patients, Neurobiol. Aging 21 (2000), 455-462.
    • (2000) Neurobiol. Aging , vol.21 , pp. 455-462
    • Maurer, I.1    Zierz, X.2    Moller, H.-J.3
  • 6
    • 0036231792 scopus 로고    scopus 로고
    • Cytochrome c oxidase and mitochondrial ATP synthase activities in platelets and brain from patients with Alzheimer's disease
    • F. Bosetti, F. Brizzi, S. Barogi, M. Mancuso, G. Sicialiano, E. Tendi, L. Muni, S. Rapoport and G. Solaini, Cytochrome c oxidase and mitochondrial ATP synthase activities in platelets and brain from patients with Alzheimer's disease, Neurobiol. Aging 23 (2002), 371-376.
    • (2002) Neurobiol. Aging , vol.23 , pp. 371-376
    • Bosetti, F.1    Brizzi, F.2    Barogi, S.3    Mancuso, M.4    Sicialiano, G.5    Tendi, E.6    Muni, L.7    Rapoport, S.8    Solaini, G.9
  • 7
    • 3042736860 scopus 로고    scopus 로고
    • Gene expression profiles of transcripts in amyloid precursor protein transgenic mice: Up-regulation of mitochondrial metabolism and apoptotic genes is an early cellular change in Alzheimer's disease
    • P. Reddy, S. McWeeney, B. Park, M. Manczak, R. Gutala, D. Partovi, Y. Jung, V. Yau, R. Searles, M. Mori and J. Quinn, Gene expression profiles of transcripts in amyloid precursor protein transgenic mice: up-regulation of mitochondrial metabolism and apoptotic genes is an early cellular change in Alzheimer's disease, Human Mol Genetics 13 (2004), 1225-1240.
    • (2004) Human Mol Genetics , vol.13 , pp. 1225-1240
    • Reddy, P.1    McWeeney, S.2    Park, B.3    Manczak, M.4    Gutala, R.5    Partovi, D.6    Jung, Y.7    Yau, V.8    Searles, R.9    Mori, M.10    Quinn, J.11
  • 8
    • 3242668604 scopus 로고    scopus 로고
    • Alzheimer's brains harbor somatic mtDNA control-region mutations that suppress mitochondrial transcription and replication
    • P. Coskun, M. Beal and D. Wallace, Alzheimer's brains harbor somatic mtDNA control-region mutations that suppress mitochondrial transcription and replication, PNAS 101 (2004), 10726-10731.
    • (2004) PNAS , vol.101 , pp. 10726-10731
    • Coskun, P.1    Beal, M.2    Wallace, D.3
  • 11
    • 0442323503 scopus 로고    scopus 로고
    • Alzheimer's disease-associated Aβ interacts with the human serine protease HtrA2/Omi
    • H-J. Park, Y-M. Seong, J-Y. Choi, S. Kang and H. Rhim, Alzheimer's disease-associated Aβ interacts with the human serine protease HtrA2/Omi, Neurosci. Lett. 357 (2004), 63-67.
    • (2004) Neurosci. Lett. , vol.357 , pp. 63-67
    • Park, H.-J.1    Seong, Y.-M.2    Choi, J.-Y.3    Kang, S.4    Rhim, H.5
  • 12
    • 0035957969 scopus 로고    scopus 로고
    • The mitochondrion: Is it central to apoptosis?
    • E. Finkel, The mitochondrion: is it central to apoptosis? Science 292 (2001), 624-626.
    • (2001) Science , vol.292 , pp. 624-626
    • Finkel, E.1
  • 13
    • 0035805523 scopus 로고    scopus 로고
    • APOPTOSIS: Death of a monopoly?
    • S. Hunot and R. Flavell, APOPTOSIS: death of a monopoly? Science 292 (2001), 865-866.
    • (2001) Science , vol.292 , pp. 865-866
    • Hunot, S.1    Flavell, R.2
  • 16
    • 0025734299 scopus 로고
    • The role of oxidative abnormalities in the pathophysiology of Alzheimer's disease
    • J. Blass and G. Gibson, The role of oxidative abnormalities in the pathophysiology of Alzheimer's disease, Rev. Neurol. (Paris) 147 (1991), 513-525.
    • (1991) Rev. Neurol. (Paris) , vol.147 , pp. 513-525
    • Blass, J.1    Gibson, G.2
  • 17
    • 0030874251 scopus 로고    scopus 로고
    • Metabolic reduction in the posterior cingulate cortex in very early Alzheimer's disease
    • S. Minoshima, B. Giordani, S. Berent, K. Frey, N. Foster and D. Kuhl, Metabolic reduction in the posterior cingulate cortex in very early Alzheimer's disease, Ann. Neurol. 42 (1997), 85-94.
    • (1997) Ann. Neurol. , vol.42 , pp. 85-94
    • Minoshima, S.1    Giordani, B.2    Berent, S.3    Frey, K.4    Foster, N.5    Kuhl, D.6
  • 19
    • 0000087029 scopus 로고    scopus 로고
    • Clinical value of neuroimaging in the dianosis of dementia
    • D. Silverman, G. Small and M. Phelps, Clinical value of neuroimaging in the dianosis of dementia, Clin. Positron Imaging 2 (1999), 119-130.
    • (1999) Clin. Positron Imaging , vol.2 , pp. 119-130
    • Silverman, D.1    Small, G.2    Phelps, M.3
  • 21
    • 0036660882 scopus 로고    scopus 로고
    • Added clinical benefit of incorporating 2-deoxy-2-[18]Fluoro-D-glucose with PET in the clinical evaluation of patients with cognitive impairment
    • D. Silverman, J. Cummings, G. Small, S. Gambhir, W. Chen, J. Dzernin and M. Phelps, Added clinical benefit of incorporating 2-deoxy-2-[18]Fluoro-D- glucose with PET in the clinical evaluation of patients with cognitive impairment, Mol. Imaging Biol. 4 (2002), 283-293.
    • (2002) Mol. Imaging Biol. , vol.4 , pp. 283-293
    • Silverman, D.1    Cummings, J.2    Small, G.3    Gambhir, S.4    Chen, W.5    Dzernin, J.6    Phelps, M.7
  • 22
    • 0024448458 scopus 로고
    • Human cells lacking mtDNA: Repopulation with exogenous mitochondria by complementation
    • M. King and G. Attardi, Human cells lacking mtDNA: repopulation with exogenous mitochondria by complementation, Science 246 (1989), 500-503.
    • (1989) Science , vol.246 , pp. 500-503
    • King, M.1    Attardi, G.2
  • 24
    • 3042513691 scopus 로고    scopus 로고
    • Mitochondrial dysfunction of Alzheimer's disease cybrids enhances Aβ toxicity
    • S. Cardoso, I. Santana, R. Swerdlow and C. Oliveira, Mitochondrial dysfunction of Alzheimer's disease cybrids enhances Aβ toxicity, J. Neurochem. 89 (2004), 1417-1426.
    • (2004) J. Neurochem. , vol.89 , pp. 1417-1426
    • Cardoso, S.1    Santana, I.2    Swerdlow, R.3    Oliveira, C.4
  • 27
    • 0018826694 scopus 로고
    • Coenzyme A-acetylating enzymes in Alzheimer's disease: Possible cholinergic 'compartment' of pyruvate deydrogenase
    • E. Perry, R. Perry, B. Tomlinson, G. Blessed and P. Gibson, Coenzyme A-acetylating enzymes in Alzheimer's disease: possible cholinergic 'compartment' of pyruvate deydrogenase, Neurosci. Lett. 18 (1980), 105-110.
    • (1980) Neurosci. Lett. , vol.18 , pp. 105-110
    • Perry, E.1    Perry, R.2    Tomlinson, B.3    Blessed, G.4    Gibson, P.5
  • 28
    • 0031737226 scopus 로고    scopus 로고
    • Abnormalities of mitochondrial enzymes in Alzheimer disease
    • G. Gibson, K. Sheu and J. Blass, Abnormalities of mitochondrial enzymes in Alzheimer disease, J. Neural Transm. 105 (1998), 855-870.
    • (1998) J. Neural Transm. , vol.105 , pp. 855-870
    • Gibson, G.1    Sheu, K.2    Blass, J.3
  • 29
    • 0034512488 scopus 로고    scopus 로고
    • The mitochondrial spiral. An adequate cause of dementia in the Alzheimer's syndrome
    • J. Blass, The mitochondrial spiral. An adequate cause of dementia in the Alzheimer's syndrome, Ann. New York Acad. Sci. 924 (2000), 170-183.
    • (2000) Ann. New York Acad. Sci. , vol.924 , pp. 170-183
    • Blass, J.1
  • 31
    • 0034795140 scopus 로고    scopus 로고
    • RAGE: A multi-ligand receptor serving as a progression factor amplifying the immune/inflammatory response
    • A. Schmidt, S-D. Yan, S-F. Yan and D. Stern, RAGE: a multi-ligand receptor serving as a progression factor amplifying the immune/inflammatory response, J. Clin. Invest. 108 (2001), 949-955.
    • (2001) J. Clin. Invest. , vol.108 , pp. 949-955
    • Schmidt, A.1    Yan, S.-D.2    Yan, S.-F.3    Stern, D.4
  • 32
    • 1642499152 scopus 로고    scopus 로고
    • Aβ induces mitochondrial dysfunction and oxidative stress in astrocytes and death of neurons through activation of NADPH oxidase
    • A. Abramov, L. Canevari and M. Duchen, Aβ induces mitochondrial dysfunction and oxidative stress in astrocytes and death of neurons through activation of NADPH oxidase, J. Neurosci. 24 (2004), 565-575.
    • (2004) J. Neurosci. , vol.24 , pp. 565-575
    • Abramov, A.1    Canevari, L.2    Duchen, M.3
  • 33
    • 10944272619 scopus 로고    scopus 로고
    • Fibrillar Aβ kills human primary neurons via NADPH oxidase-mediated activation of neutral sphingomyelinase. Implications for Alzheimer's disease
    • A. Jana and K. Pahan, Fibrillar Aβ kills human primary neurons via NADPH oxidase-mediated activation of neutral sphingomyelinase. Implications for Alzheimer's disease, J. Biol. Chem. 279 (2004), 51451-51459.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51451-51459
    • Jana, A.1    Pahan, K.2
  • 34
    • 14044258771 scopus 로고    scopus 로고
    • NADPH-oxidase-derived reactive oxygen species mediate the cerebrovascular dysfunction induced by Aβ
    • L. Park, J. Anreather, P. Zhou, K. Frys, R. Pitstick, S. Younkin, G. Carlson and C. Iadecola, NADPH-oxidase-derived reactive oxygen species mediate the cerebrovascular dysfunction induced by Aβ, J. Neurosci. 25 (2005), 1769-1777.
    • (2005) J. Neurosci. , vol.25 , pp. 1769-1777
    • Park, L.1    Anreather, J.2    Zhou, P.3    Frys, K.4    Pitstick, R.5    Younkin, S.6    Carlson, G.7    Iadecola, C.8
  • 35
    • 0026587335 scopus 로고
    • Mitochondrial genetics: A paradigm for aging and degenerative diseases?
    • D. Wallace, Mitochondrial genetics: a paradigm for aging and degenerative diseases? Science 256 (1992), 628-632.
    • (1992) Science , vol.256 , pp. 628-632
    • Wallace, D.1
  • 36
    • 0027171266 scopus 로고
    • Oxidants, antioxidants and the degenerative diseases of aging
    • B. Ames, M. Shigenaga and T. Hagen, Oxidants, antioxidants and the degenerative diseases of aging, PNAS 90 (1993), 7915-7922.
    • (1993) PNAS , vol.90 , pp. 7915-7922
    • Ames, B.1    Shigenaga, M.2    Hagen, T.3
  • 37
    • 0032933750 scopus 로고    scopus 로고
    • Increased DNA oxidation and decreased levels of repair products in Alzheimer's disease ventricular CSF
    • M. Lovell, S. Gabbita and W. Markesbery, Increased DNA oxidation and decreased levels of repair products in Alzheimer's disease ventricular CSF, J. Neurochem. 72 (1999), 771-776.
    • (1999) J. Neurochem. , vol.72 , pp. 771-776
    • Lovell, M.1    Gabbita, S.2    Markesbery, W.3
  • 38
    • 18844462415 scopus 로고    scopus 로고
    • Increased oxidative damage in nuclear and mitochondrial DNA in Alzheimer's disease
    • J. Wang, S. Xiong, C. Xie, W. Markesbery and M. Lovell, Increased oxidative damage in nuclear and mitochondrial DNA in Alzheimer's disease, J. Neurochem. 93 (2005), 953-962.
    • (2005) J. Neurochem. , vol.93 , pp. 953-962
    • Wang, J.1    Xiong, S.2    Xie, C.3    Markesbery, W.4    Lovell, M.5
  • 39
    • 0032902974 scopus 로고    scopus 로고
    • Oxidative alterations in Alzheimer's disease
    • W. Markesbery and J. Carney, Oxidative alterations in Alzheimer's disease, Brain Pathol 9 (1999), 133-146.
    • (1999) Brain Pathol , vol.9 , pp. 133-146
    • Markesbery, W.1    Carney, J.2
  • 40
    • 0034667741 scopus 로고    scopus 로고
    • Acrolein, a product of lipid peroxidation, inhibits glucose and glutamate uptake in primary neuronal cultures
    • M. Lovell, C. Xie and W. Markesbery, Acrolein, a product of lipid peroxidation, inhibits glucose and glutamate uptake in primary neuronal cultures, Free Radic. Biol. Med. 29 (2000), 714-720.
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 714-720
    • Lovell, M.1    Xie, C.2    Markesbery, W.3
  • 44
    • 12244281810 scopus 로고    scopus 로고
    • Oxidative stress precedes fibrillar deposition of Alzheimer's disease amyloid beta-peptide (1-42) in a transgenic Caenorhabditis elegans model
    • J. Drake, C. Link and D. Butterfield, Oxidative stress precedes fibrillar deposition of Alzheimer's disease amyloid beta-peptide (1-42) in a transgenic Caenorhabditis elegans model, Neurobiol. Aging 24 (2003), 415-420.
    • (2003) Neurobiol. Aging , vol.24 , pp. 415-420
    • Drake, J.1    Link, C.2    Butterfield, D.3
  • 46
    • 0029417023 scopus 로고
    • Apoptosis and increased generation of reactive oxygen species in Down's syndrome neurons in vitro
    • J. Busciglio and B. Yankner, Apoptosis and increased generation of reactive oxygen species in Down's syndrome neurons in vitro, Nature 378 (1995), 776-779.
    • (1995) Nature , vol.378 , pp. 776-779
    • Busciglio, J.1    Yankner, B.2
  • 47
    • 0037186074 scopus 로고    scopus 로고
    • Altered metabolism of amyloid-β precursor protein is associated with mitochondrial dysfunction in Down's syndrome
    • J. Busciglio, A. Pelsman, C. Wong, G. Pigino, M. Yuan, H. Mori and B. Yankner, Altered metabolism of amyloid-β precursor protein is associated with mitochondrial dysfunction in Down's syndrome, Neuron 33 (2002), 677-688.
    • (2002) Neuron , vol.33 , pp. 677-688
    • Busciglio, J.1    Pelsman, A.2    Wong, C.3    Pigino, G.4    Yuan, M.5    Mori, H.6    Yankner, B.7
  • 50
    • 21544477514 scopus 로고    scopus 로고
    • At least 2 distinct pathways generating reactive oxygen species mediate VCAM-1 induction by AGEs
    • G. Basta, G. Lazzerini, S. Del Turco, G. Ratto and R. DeCaterina, At least 2 distinct pathways generating reactive oxygen species mediate VCAM-1 induction by AGEs, Arterioscl. Thromb. Vasc. Biol. 25 (2005), 1401-1407.
    • (2005) Arterioscl. Thromb. Vasc. Biol. , vol.25 , pp. 1401-1407
    • Basta, G.1    Lazzerini, G.2    Del Turco, S.3    Ratto, G.4    DeCaterina, R.5
  • 51
    • 0037437192 scopus 로고    scopus 로고
    • Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells
    • H. Anandatheerthavarada, G. Biswas, M-A. Robin and N. Avadhani, Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells, J. Cell Biol. 161 (2003), 41-54.
    • (2003) J. Cell Biol. , vol.161 , pp. 41-54
    • Anandatheerthavarada, H.1    Biswas, G.2    Robin, M.-A.3    Avadhani, N.4
  • 52
    • 0033570145 scopus 로고    scopus 로고
    • Dual targeting of cytochrome P4502B1 to endoplasmic reticulum and mitochondria involves a novel signal activation by cyclic AMP-dependent phosphorylation at Ser128
    • H. Anandatheerthavarada, G. Biswas, J. Mullick, N. Babu, V. Sepuri, L. Otvos, D. Pain and N. Avadhani, Dual targeting of cytochrome P4502B1 to endoplasmic reticulum and mitochondria involves a novel signal activation by cyclic AMP-dependent phosphorylation at Ser128, EMBO J 18 (1999), 5494-5504.
    • (1999) EMBO J , vol.18 , pp. 5494-5504
    • Anandatheerthavarada, H.1    Biswas, G.2    Mullick, J.3    Babu, N.4    Sepuri, V.5    Otvos, L.6    Pain, D.7    Avadhani, N.8
  • 53
    • 0037431082 scopus 로고    scopus 로고
    • Aph-1, Pen-2 and nicastrin with presenilin generate an active gamma-secretase complex
    • B. De Strooper, Aph-1, Pen-2 and nicastrin with presenilin generate an active gamma-secretase complex, Neuron 38 (2003), 9-12.
    • (2003) Neuron , vol.38 , pp. 9-12
    • De Strooper, B.1
  • 54
    • 0037339735 scopus 로고    scopus 로고
    • Localization of presenilin-nicastrin complexes and activity to the trans-golgi network
    • R. Simian and J. Velhi, Localization of presenilin-nicastrin complexes and activity to the trans-golgi network, J. Neurochem. 84 (2003), 1143-1153.
    • (2003) J. Neurochem. , vol.84 , pp. 1143-1153
    • Simian, R.1    Velhi, J.2
  • 56
    • 14244268498 scopus 로고    scopus 로고
    • Gamma secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage
    • J. Chyung, D. Raper and D. Selkoe, Gamma secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage, J. Biol. Chem. 280 (2005), 4383-4392.
    • (2005) J. Biol. Chem. , vol.280 , pp. 4383-4392
    • Chyung, J.1    Raper, D.2    Selkoe, D.3
  • 58
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts
    • R. Ehehalt, P. Keller, C. Haass, C. Thiele and K. Simons, Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts, J. Cell Biol. 160 (2003), 113-123.
    • (2003) J. Cell Biol. , vol.160 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 62
    • 0028972233 scopus 로고
    • Intracellular accumulation of Aβ in cells expressing the Swedish mutant amyloid precursor protein
    • B. Martin, G. Schrader-Fischer, J. Busciglio, M. Duke, P. Paganetti and B. Yankner, Intracellular accumulation of Aβ in cells expressing the Swedish mutant amyloid precursor protein, J. Biol. Chem. 270 (1995), 26,727-26,730.
    • (1995) J. Biol. Chem. , vol.270
    • Martin, B.1    Schrader-Fischer, G.2    Busciglio, J.3    Duke, M.4    Paganetti, P.5    Yankner, B.6
  • 63
    • 0032895651 scopus 로고    scopus 로고
    • Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation
    • D. Chui, H. Tanahashi, K. Ozawa, F. Checler, O. Ueda, H. Suzuki, W. Araki, H. Inoue and K. Shirotani, Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation, Nat. Med. 5 (1999), 560-564.
    • (1999) Nat. Med. , vol.5 , pp. 560-564
    • Chui, D.1    Tanahashi, H.2    Ozawa, K.3    Checler, F.4    Ueda, O.5    Suzuki, H.6    Araki, W.7    Inoue, H.8    Shirotani, K.9
  • 64
    • 0032800818 scopus 로고    scopus 로고
    • Intracellular APP processing and Aβ production in Alzheimer disease
    • C. Wilson, R. Doms and V. Lee, Intracellular APP processing and Aβ production in Alzheimer disease, J. Neuropathol. Exp. Neurol. 58 (1999), 787-794.
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , pp. 787-794
    • Wilson, C.1    Doms, R.2    Lee, V.3
  • 65
    • 0033458064 scopus 로고    scopus 로고
    • Intracellular biology of Alzheimer's disease Aβ peptide
    • T. Hartmann, Intracellular biology of Alzheimer's disease Aβ peptide, Eur. Arch. Psychiatry Clin. Neurosci. 249 (1999), 291-298.
    • (1999) Eur. Arch. Psychiatry Clin. Neurosci. , vol.249 , pp. 291-298
    • Hartmann, T.1
  • 66
    • 0037013327 scopus 로고    scopus 로고
    • Intracellular Aβ42, but not extracellular soluble Aβ, induces neuronal apoptosis
    • P. Kienlen-Campard, S. Miolet, B. Tasiaux and J-N. Octave, Intracellular Aβ42, but not extracellular soluble Aβ, induces neuronal apoptosis, J. Biol. Chem. 277 (2002), 15,666-15,670.
    • (2002) J. Biol. Chem. , vol.277
    • Kienlen-Campard, P.1    Miolet, S.2    Tasiaux, B.3    Octave, J.-N.4
  • 67
    • 0034609516 scopus 로고    scopus 로고
    • The oligomerization of Aβ begins intracellularly in cells derived from human brain
    • D. Walsh, B. Tseng, R. Rydel, M. Podisny and D. Selkoe, The oligomerization of Aβ begins intracellularly in cells derived from human brain, Biochem 39 (2000), 10,831-10,839.
    • (2000) Biochem , vol.39
    • Walsh, D.1    Tseng, B.2    Rydel, R.3    Podisny, M.4    Selkoe, D.5
  • 68
    • 0034745017 scopus 로고    scopus 로고
    • Intraneuronal Aβ-amyloid precedes development of amyloid plaques in Down Syndrome
    • K. Gyure, R. Durham, W. Stewart, J. Smialek and I. Troncoso, Intraneuronal Aβ-amyloid precedes development of amyloid plaques in Down Syndrome, Arch. Pathol. Lab. Med. 125 (2001), 489-492.
    • (2001) Arch. Pathol. Lab. Med. , vol.125 , pp. 489-492
    • Gyure, K.1    Durham, R.2    Stewart, W.3    Smialek, J.4    Troncoso, I.5
  • 70
    • 0035159785 scopus 로고    scopus 로고
    • Intracellular mechanisms of amyloid accumulation and pathogenesis in Alzheimer's disease
    • C. Glabe, Intracellular mechanisms of amyloid accumulation and pathogenesis in Alzheimer's disease, J. Mol. Neurosci. 17 (2001), 137-145.
    • (2001) J. Mol. Neurosci. , vol.17 , pp. 137-145
    • Glabe, C.1
  • 71
    • 0033582159 scopus 로고    scopus 로고
    • Endoplasmic reticulum and trans-Golgi network generate distinct populations of Alzheimer β-amyloid peptides
    • J. Greenfield, J. Tsai, G. Gouras, B. Hai, G. Thinakaran, F. Checler, S. Sisodia, P. Greengard and H. Xu, Endoplasmic reticulum and trans-Golgi network generate distinct populations of Alzheimer β-amyloid peptides, PNAS 96 (1999), 742-747.
    • (1999) PNAS , vol.96 , pp. 742-747
    • Greenfield, J.1    Tsai, J.2    Gouras, G.3    Hai, B.4    Thinakaran, G.5    Checler, F.6    Sisodia, S.7    Greengard, P.8    Xu, H.9
  • 72
    • 0030769092 scopus 로고    scopus 로고
    • Aβ(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells
    • D. Cook, M. Forman, J. Sung, S. Leight, T. Iwatsubo, V. Lee and R. Doms, Aβ(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells, Nat. Med. 3 (1997), 1021-1023.
    • (1997) Nat. Med. , vol.3 , pp. 1021-1023
    • Cook, D.1    Forman, M.2    Sung, J.3    Leight, S.4    Iwatsubo, T.5    Lee, V.6    Doms, R.7
  • 74
    • 0030966774 scopus 로고    scopus 로고
    • Intracellular and secreted Alzheimer β-peptide species are generated by distinct mechanisms in cultured hippocampal neurons
    • P. Tienari, N. Ida, E. Ikonen, M. Simons, A. Weidemann, G. Multhaup, C. Masters, C. Dotti and K. Beyreuther, Intracellular and secreted Alzheimer β-peptide species are generated by distinct mechanisms in cultured hippocampal neurons, PNAS 94 (1997), 4125-4130.
    • (1997) PNAS , vol.94 , pp. 4125-4130
    • Tienari, P.1    Ida, N.2    Ikonen, E.3    Simons, M.4    Weidemann, A.5    Multhaup, G.6    Masters, C.7    Dotti, C.8    Beyreuther, K.9
  • 75
  • 76
    • 0033516554 scopus 로고    scopus 로고
    • Mutagenesis identifies new signals for βAPP endocytosis, turnover and the generation of secreted fragments, including Aβ42
    • R. Perez, S. Soriano, J. Hayes, B. Ostaszewski, W. Xia, D. Selkoe, X. Chen, G. Stokin and E. Koo, Mutagenesis identifies new signals for βAPP endocytosis, turnover and the generation of secreted fragments, including Aβ42, J. Biol. Chem. 274 (1999), 18,851-18,856.
    • (1999) J. Biol. Chem. , vol.274
    • Perez, R.1    Soriano, S.2    Hayes, J.3    Ostaszewski, B.4    Xia, W.5    Selkoe, D.6    Chen, X.7    Stokin, G.8    Koo, E.9
  • 77
    • 0034213718 scopus 로고    scopus 로고
    • High-level neuronal expression of Aβ(1-42) in wild-type human amyloid protein precursor transgenic mice: Synaptotoxicity without plaque formation
    • L. Mucke, E. Masliah, G. Yu, M. Mallory, E. Rockenstein, G. Tatsuno, K. Hu, D. Kholodenko, K. Johnson-Wood and L. McConlogue, High-level neuronal expression of Aβ(1-42) in wild-type human amyloid protein precursor transgenic mice: synaptotoxicity without plaque formation, J. Neurosci. 20 (2000), 4050-4058.
    • (2000) J. Neurosci. , vol.20 , pp. 4050-4058
    • Mucke, L.1    Masliah, E.2    Yu, G.3    Mallory, M.4    Rockenstein, E.5    Tatsuno, G.6    Hu, K.7    Kholodenko, D.8    Johnson-Wood, K.9    McConlogue, L.10
  • 78
    • 0034870805 scopus 로고    scopus 로고
    • Membrane-disordering effects of β-amyloid peptides
    • W. Muller, C. Kirsch and G. Eckert, Membrane-disordering effects of β-amyloid peptides, Biochem. Soc. Trans. 29 (2001), 617-623.
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 617-623
    • Muller, W.1    Kirsch, C.2    Eckert, G.3
  • 79
    • 0028649480 scopus 로고
    • The ability of Aβ(1-40) to form calcium channels proves a mechanism for neuronal death in Alzheimer's disease
    • N. Arispe, H. Pollard and E. Rojas, The ability of Aβ(1-40) to form calcium channels proves a mechanism for neuronal death in Alzheimer's disease, Ann. N. Y. Acad. Sci. 15 (1994), 256-266.
    • (1994) Ann. N. Y. Acad. Sci. , vol.15 , pp. 256-266
    • Arispe, N.1    Pollard, H.2    Rojas, E.3
  • 80
    • 0032526652 scopus 로고    scopus 로고
    • Loss of endosomal/lysosomal membrane impermeability is an early event in amyloid Aβ1-42 pathogenesis
    • A. Yang, D. Chandswangbhuvana, L. Margol and C. Glabe, Loss of endosomal/lysosomal membrane impermeability is an early event in amyloid Aβ1-42 pathogenesis, J. Neurosci. Res. 52 (1998), 691-698.
    • (1998) J. Neurosci. Res. , vol.52 , pp. 691-698
    • Yang, A.1    Chandswangbhuvana, D.2    Margol, L.3    Glabe, C.4
  • 83
    • 0031588987 scopus 로고    scopus 로고
    • Cloning and expression of cDNA for a newly identified isozyme of bovine liver 3-hydroxyacyl-CoA dehydrogenase and its import into mitochondria
    • S. Furuta, A. Kobayahsi, S. Miyazawa and T. Hashimoto, Cloning and expression of cDNA for a newly identified isozyme of bovine liver 3-hydroxyacyl-CoA dehydrogenase and its import into mitochondria, Biochim. Biophys. Acta 1350 (1997), 317-324.
    • (1997) Biochim. Biophys. Acta , vol.1350 , pp. 317-324
    • Furuta, S.1    Kobayahsi, A.2    Miyazawa, S.3    Hashimoto, T.4
  • 84
    • 0029880653 scopus 로고    scopus 로고
    • Two mitochondrial 3-hydroxyacyl-CoA dehydrogenases in bovine liver
    • A. Kobayashi, L. Jaing and T. Hashimoto, Two mitochondrial 3-hydroxyacyl-CoA dehydrogenases in bovine liver, J. Biochem. (Tokyo) 119 (1996), 775-782.
    • (1996) J. Biochem. (Tokyo) , vol.119 , pp. 775-782
    • Kobayashi, A.1    Jaing, L.2    Hashimoto, T.3
  • 85
    • 0034791854 scopus 로고    scopus 로고
    • Characterization and localization of human type 10 17β- hydroxysteroid dehydrogenase
    • X-Y. He, G. Merz, P. Mehta, H. Schulz and S-Y. Yang, Characterization and localization of human type 10 17β-hydroxysteroid dehydrogenase, Eur. J. Biochem. 268 (2001), 4899-4907.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4899-4907
    • He, X.-Y.1    Merz, G.2    Mehta, P.3    Schulz, H.4    Yang, S.-Y.5
  • 86
    • 0033667891 scopus 로고    scopus 로고
    • Progressive infantile neurodegeneration caused by 2-methyl-3- hydroxybutyryl-CoA dehydrogenase deficiency: A novel inborn error of branched-chain fatty acid and isoleucine metabolism
    • J. Zschocke, J. Ruiter, J. Brand, M. Lindner, G. Hoffmann, R. Wanders and E. Mayatepek, Progressive infantile neurodegeneration caused by 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency: a novel inborn error of branched-chain fatty acid and isoleucine metabolism, Ped. Res. 48 (2000), 852-855.
    • (2000) Ped. Res. , vol.48 , pp. 852-855
    • Zschocke, J.1    Ruiter, J.2    Brand, J.3    Lindner, M.4    Hoffmann, G.5    Wanders, R.6    Mayatepek, E.7
  • 88
    • 0345830473 scopus 로고    scopus 로고
    • 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency: Impaired catabolism of isoleucine presenting as neurodegenerative disease
    • J. Sass, R. Forstner and W. Sper, 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency: impaired catabolism of isoleucine presenting as neurodegenerative disease, Brain & Development 26 (2004), 12-14.
    • (2004) Brain & Development , vol.26 , pp. 12-14
    • Sass, J.1    Forstner, R.2    Sper, W.3
  • 89
    • 0031750831 scopus 로고    scopus 로고
    • Scully, an essential gene of Drosophila, is homologous to mammalian mitochondrial type II L-3-hydroxyacyl-CoA dehydrogenase/ABAD
    • L. Torroja, D. Ortuno-Sahagun, A. Ferrus, B. Hammerle and J. Barbas, Scully, an essential gene of Drosophila, is homologous to mammalian mitochondrial type II L-3-hydroxyacyl-CoA dehydrogenase/ABAD, J. Cell Biol. 141 (1998), 1009-1017.
    • (1998) J. Cell Biol. , vol.141 , pp. 1009-1017
    • Torroja, L.1    Ortuno-Sahagun, D.2    Ferrus, A.3    Hammerle, B.4    Barbas, J.5
  • 91
    • 0037047163 scopus 로고    scopus 로고
    • Interaction of intracellular beta-amyloid peptide with chaperone proteins
    • V. Fonte, V. Kapulkin, a. Taft, A. Fluet, D. Friedman and C. Link, Interaction of intracellular beta-amyloid peptide with chaperone proteins, PNAS 99 (2002), 9439-9444.
    • (2002) PNAS , vol.99 , pp. 9439-9444
    • Fonte, V.1    Kapulkin, V.2    Taft, A.3    Fluet, A.4    Friedman, D.5    Link, C.6
  • 94
    • 0036263973 scopus 로고    scopus 로고
    • Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi Nat
    • W. Li, S. Srinivasula, J. Chai, P. Li, J. Wu, Z. Zhang, E. Alnemri and Y. Shi, Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi Nat, Struct. Biol. 9 (2002), 436-441.
    • (2002) Struct. Biol. , vol.9 , pp. 436-441
    • Li, W.1    Srinivasula, S.2    Chai, J.3    Li, P.4    Wu, J.5    Zhang, Z.6    Alnemri, E.7    Shi, Y.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.