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Volumn 9, Issue 2, 2006, Pages 147-153

Mitochondrial abnormalities and oxidative imbalance in Alzheimer disease

Author keywords

Alzheimer disease; Cell cycle re entry; Mitochondria; Mitochondrial transport; Mitochondrial turnover; Oxidative stress

Indexed keywords

ALPHA TOCOPHEROL; ANTIINFLAMMATORY AGENT; CYTOCHROME C OXIDASE; FREE RADICAL; MITOCHONDRIAL DNA; OXYGEN RADICAL; SELEGILINE;

EID: 33746089859     PISSN: 13872877     EISSN: None     Source Type: Journal    
DOI: 10.3233/JAD-2006-9207     Document Type: Review
Times cited : (166)

References (75)
  • 1
    • 0030454478 scopus 로고    scopus 로고
    • Expression of the cyclin-dependent kinase inhibitor p16 in Alzheimer's disease
    • T. Arendt, L. Rodel, U. Gartner and M. Holzer, Expression of the cyclin-dependent kinase inhibitor p16 in Alzheimer's disease, Neuroreport 7 (1996), 3047-3049.
    • (1996) Neuroreport , vol.7 , pp. 3047-3049
    • Arendt, T.1    Rodel, L.2    Gartner, U.3    Holzer, M.4
  • 2
    • 0029920323 scopus 로고    scopus 로고
    • Static cytofluorometry and fluorescence morphology of mitochondria and DNA in proliferating fibroblasts
    • S. Barni, L. Sciola, A. Spano and P. Pippia, Static cytofluorometry and fluorescence morphology of mitochondria and DNA in proliferating fibroblasts, Biotech Histochem 71 (1996), 66-70.
    • (1996) Biotech Histochem , vol.71 , pp. 66-70
    • Barni, S.1    Sciola, L.2    Spano, A.3    Pippia, P.4
  • 3
    • 0027129818 scopus 로고
    • Vitamin E protects nerve cells from amyloid beta protein toxicity
    • C. Behl, J. Davis, G.M. Cole and D. Schubert, Vitamin E protects nerve cells from amyloid beta protein toxicity, Biochem Biophys Res Commun 186 (1992), 944-950.
    • (1992) Biochem Biophys Res Commun , vol.186 , pp. 944-950
    • Behl, C.1    Davis, J.2    Cole, G.M.3    Schubert, D.4
  • 4
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • C. Behl, J.B. Davis, R. Lesley and D. Schubert, Hydrogen peroxide mediates amyloid beta protein toxicity, Cell 77 (1994), 817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 5
    • 0034512488 scopus 로고    scopus 로고
    • The mitochondrial spiral. An adequate cause of dementia in the Alzheimer's syndrome
    • J.P. Blass, The mitochondrial spiral. An adequate cause of dementia in the Alzheimer's syndrome, Ann N Y Acad Sci 924 (2000), 170-183.
    • (2000) Ann N Y Acad Sci , vol.924 , pp. 170-183
    • Blass, J.P.1
  • 6
    • 0028936986 scopus 로고
    • Bioenergetic and oxidative stress in neurodegenerative diseases
    • A.C. Bowling and M.F. Beal, Bioenergetic and oxidative stress in neurodegenerative diseases, Life Sci 56 (1995), 1151-1171.
    • (1995) Life Sci , vol.56 , pp. 1151-1171
    • Bowling, A.C.1    Beal, M.F.2
  • 7
    • 0030000385 scopus 로고    scopus 로고
    • The role of anti-inflammatory drugs in the prevention and treatment of Alzheimer's disease
    • J.C. Breitner, The role of anti-inflammatory drugs in the prevention and treatment of Alzheimer's disease, Annu Rev Med 47 (1996), 401-411.
    • (1996) Annu Rev Med , vol.47 , pp. 401-411
    • Breitner, J.C.1
  • 8
    • 18244390483 scopus 로고    scopus 로고
    • Mitochondrial abnormalities in Alzheimer brain: Mechanistic implications
    • P. Bubber, V. Haroutunian, G. Fisch, J.P. Blass and G.E. Gibson, Mitochondrial abnormalities in Alzheimer brain: mechanistic implications, Ann Neurol 57 (2005), 695-703.
    • (2005) Ann Neurol , vol.57 , pp. 695-703
    • Bubber, P.1    Haroutunian, V.2    Fisch, G.3    Blass, J.P.4    Gibson, G.E.5
  • 10
    • 0028947294 scopus 로고
    • Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: Evidence for early up-regulation of the endosomal-lysosomal system
    • A.M. Cataldo, J.L. Barnett, S.A. Berman, J. Li, S. Quarless, S. Bursztajn, C. Lippa and R.A. Nixon, Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: evidence for early up-regulation of the endosomal-lysosomal system, Neuron 14 (1995), 671-680.
    • (1995) Neuron , vol.14 , pp. 671-680
    • Cataldo, A.M.1    Barnett, J.L.2    Berman, S.A.3    Li, J.4    Quarless, S.5    Bursztajn, S.6    Lippa, C.7    Nixon, R.A.8
  • 11
    • 0033869715 scopus 로고    scopus 로고
    • Endocytic pathway abnormalities precede amyloid beta deposition in sporadic Alzheimer's disease and Down syndrome: Differential effects of APOE genotype and presenilin mutations
    • A.M. Cataldo, C.M. Peterhoff, J.C. Troncoso, T. Gomez-Isla, B.T. Hyman and R.A. Nixon, Endocytic pathway abnormalities precede amyloid beta deposition in sporadic Alzheimer's disease and Down syndrome: differential effects of APOE genotype and presenilin mutations, Am J Pathol 157 (2000), 277-286.
    • (2000) Am J Pathol , vol.157 , pp. 277-286
    • Cataldo, A.M.1    Peterhoff, C.M.2    Troncoso, J.C.3    Gomez-Isla, T.4    Hyman, B.T.5    Nixon, R.A.6
  • 12
    • 3242668604 scopus 로고    scopus 로고
    • Alzheimer's brains harbor somatic mtDNA control-region mutations that suppress mitochondrial transcription and replication
    • P.E. Coskun, M.F. Beal and D.C. Wallace, Alzheimer's brains harbor somatic mtDNA control-region mutations that suppress mitochondrial transcription and replication, Proc Natl Acad Sci U S A 101 (2004), 10726-10731.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 10726-10731
    • Coskun, P.E.1    Beal, M.F.2    Wallace, D.C.3
  • 13
    • 0036127167 scopus 로고    scopus 로고
    • Hydroxynonenal inactivates cathepsin B by forming Michael adducts with active site residues
    • J.W. Crabb, J. O'Neil, M. Miyagi, K. West and H.F. Hoff, Hydroxynonenal inactivates cathepsin B by forming Michael adducts with active site residues, Protein Sci 11 (2002), 831-840.
    • (2002) Protein Sci , vol.11 , pp. 831-840
    • Crabb, J.W.1    O'Neil, J.2    Miyagi, M.3    West, K.4    Hoff, H.F.5
  • 16
    • 0030513943 scopus 로고    scopus 로고
    • Structural correlates of cognition in dementia: Quantification and assessment of synapse change
    • S.T. DeKosky, S.W. Scheff and S.D. Styren, Structural correlates of cognition in dementia: quantification and assessment of synapse change, Neurodegeneration 5 (1996), 417-421.
    • (1996) Neurodegeneration , vol.5 , pp. 417-421
    • DeKosky, S.T.1    Scheff, S.W.2    Styren, S.D.3
  • 17
    • 0032992466 scopus 로고    scopus 로고
    • Microtubule dysfunction by posttranslational nitrotyrosination of alpha-tubulin: A nitric oxide-dependent mechanism of cellular injury
    • J.P. Eiserich, A.G. Estevez, T.V. Bamberg, Y.Z. Ye, P.H. Chumley, J.S. Beckman and B.A. Freeman, Microtubule dysfunction by posttranslational nitrotyrosination of alpha-tubulin: a nitric oxide-dependent mechanism of cellular injury, Proc Natl Acad Sci USA 96 (1999), 6365-6370.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6365-6370
    • Eiserich, J.P.1    Estevez, A.G.2    Bamberg, T.V.3    Ye, Y.Z.4    Chumley, P.H.5    Beckman, J.S.6    Freeman, B.A.7
  • 18
    • 0027990369 scopus 로고
    • Modification of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal. Formation of cross-linked protein that inhibits the multicatalytic protease
    • B. Friguet, E.R. Stadtman and L.I. Szweda, Modification of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal. Formation of cross-linked protein that inhibits the multicatalytic protease, J Biol Chem 269 (1994), 21639-21643.
    • (1994) J Biol Chem , vol.269 , pp. 21639-21643
    • Friguet, B.1    Stadtman, E.R.2    Szweda, L.I.3
  • 19
    • 0032588815 scopus 로고    scopus 로고
    • Elevated expression of p21ras is an early event in Alzheimer's disease and precedes neurofibrillary degeneration
    • U. Gartner, M. Holzer and T. Arendt, Elevated expression of p21ras is an early event in Alzheimer's disease and precedes neurofibrillary degeneration, Neuroscience 91 (1999), 1-5.
    • (1999) Neuroscience , vol.91 , pp. 1-5
    • Gartner, U.1    Holzer, M.2    Arendt, T.3
  • 20
    • 0031737226 scopus 로고    scopus 로고
    • Abnormalities of mitochondrial enzymes in Alzheimer disease
    • G.E. Gibson, K.F. Sheu and J.P. 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.E.1    Sheu, K.F.2    Blass, J.P.3
  • 25
    • 0032506040 scopus 로고    scopus 로고
    • Selective inactivation of alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase: Reaction of lipoic acid with 4-hydroxy-2-nonenal
    • K.M. Humphries and L.I. Szweda, Selective inactivation of alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase: reaction of lipoic acid with 4-hydroxy-2-nonenal, Biochemistry 37 (1998), 15835-15841.
    • (1998) Biochemistry , vol.37 , pp. 15835-15841
    • Humphries, K.M.1    Szweda, L.I.2
  • 27
    • 0034131044 scopus 로고    scopus 로고
    • Impaired proteasome function in Alzheimer's disease
    • J.N. Keller, K.B. Hanni and W.R. Markesbery, Impaired proteasome function in Alzheimer's disease, J Neurochem 75 (2000), 436-439.
    • (2000) J Neurochem , vol.75 , pp. 436-439
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 28
    • 0034087369 scopus 로고    scopus 로고
    • Decreased levels of proteasome activity and proteasome expression in aging spinal cord
    • J.N. Keller, F.F. Huang and W.R. Markesbery, Decreased levels of proteasome activity and proteasome expression in aging spinal cord, Neuroscience 98 (2000), 149-156.
    • (2000) Neuroscience , vol.98 , pp. 149-156
    • Keller, J.N.1    Huang, F.F.2    Markesbery, W.R.3
  • 31
    • 0030774731 scopus 로고    scopus 로고
    • Inactivation of intracellular proteolysis and cathepsin B enzyme activity by dehydroascorbic acid and reactivation by dithiothreitol in perfused rat heart
    • T.D. Lockwood, Inactivation of intracellular proteolysis and cathepsin B enzyme activity by dehydroascorbic acid and reactivation by dithiothreitol in perfused rat heart, Biochem Pharmacol 54 (1997), 669-675.
    • (1997) Biochem Pharmacol , vol.54 , pp. 669-675
    • Lockwood, T.D.1
  • 32
    • 0029073455 scopus 로고
    • Elevated thiobarbituric acid-reactive substances and antioxidant enzyme activity in the brain in Alzheimer's disease
    • M.A. Lovell, W.D. Ehmann, S.M. Butler and W.R. Markesbery, Elevated thiobarbituric acid-reactive substances and antioxidant enzyme activity in the brain in Alzheimer's disease, Neurology 45 (1995), 1594-1601.
    • (1995) Neurology , vol.45 , pp. 1594-1601
    • Lovell, M.A.1    Ehmann, W.D.2    Butler, S.M.3    Markesbery, W.R.4
  • 33
    • 0030886976 scopus 로고    scopus 로고
    • Compromised mitochondrial function leads to increased cytosolic calcium and to activation of MAP kinases
    • Y. Luo, J.D. Bond and V.M. Ingram, Compromised mitochondrial function leads to increased cytosolic calcium and to activation of MAP kinases, Proc Natl Acad Sci USA 94 (1997), 9705-9710.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9705-9710
    • Luo, Y.1    Bond, J.D.2    Ingram, V.M.3
  • 36
    • 1842503057 scopus 로고    scopus 로고
    • Sources and mechanisms of cytoplasmic oxidative damage in Alzheimer's disease
    • M. Marlatt, H.G. Lee, G. Perry, M.A. Smith and X. Zhu, Sources and mechanisms of cytoplasmic oxidative damage in Alzheimer's disease, Acta Neurobiol Exp (Wars) 64 (2004), 81-87.
    • (2004) Acta Neurobiol Exp (Wars) , vol.64 , pp. 81-87
    • Marlatt, M.1    Lee, H.G.2    Perry, G.3    Smith, M.A.4    Zhu, X.5
  • 37
    • 0022480081 scopus 로고
    • Increased cerebral glucose-6-phosphate dehydrogenase activity in Alzheimer's disease may reflect oxidative stress
    • R.N. Martins, C.G. Harper, G.B. Stokes and C.L. Masters, Increased cerebral glucose-6-phosphate dehydrogenase activity in Alzheimer's disease may reflect oxidative stress, J Neurochem 46 (1986), 1042-1045.
    • (1986) J Neurochem , vol.46 , pp. 1042-1045
    • Martins, R.N.1    Harper, C.G.2    Stokes, G.B.3    Masters, C.L.4
  • 38
    • 0027511905 scopus 로고
    • The role of synaptic proteins in the pathogenesis of disorders of the central nervous system
    • E. Masliah and R. Terry, The role of synaptic proteins in the pathogenesis of disorders of the central nervous system, Brain Pathol 3 (1993), 77-85.
    • (1993) Brain Pathol , vol.3 , pp. 77-85
    • Masliah, E.1    Terry, R.2
  • 40
    • 0030921323 scopus 로고    scopus 로고
    • Abnormal expression of the cell cycle regulators P16 and CDK4 in Alzheimer's disease
    • A. McShea, P.L. Harris, K.R. Webster, A.F. Wahl and M.A. Smith, Abnormal expression of the cell cycle regulators P16 and CDK4 in Alzheimer's disease, Am J Pathol 150 (1997), 1933-1939.
    • (1997) Am J Pathol , vol.150 , pp. 1933-1939
    • McShea, A.1    Harris, P.L.2    Webster, K.R.3    Wahl, A.F.4    Smith, M.A.5
  • 41
    • 0033037948 scopus 로고    scopus 로고
    • Re-entry into the cell cycle: A mechanism for neurodegeneration in Alzheimer disease
    • A. McShea, A.F. Wahl and M.A. Smith, Re-entry into the cell cycle: a mechanism for neurodegeneration in Alzheimer disease, Med Hypotheses 52 (1999), 525-527.
    • (1999) Med Hypotheses , vol.52 , pp. 525-527
    • McShea, A.1    Wahl, A.F.2    Smith, M.A.3
  • 42
    • 0023140474 scopus 로고
    • Ubiquitin is a component of paired helical filaments in Alzheimer's disease
    • H. Mori, J. Kondo and Y. Ihara, Ubiquitin is a component of paired helical filaments in Alzheimer's disease, Science 235 (1987), 1641-1644.
    • (1987) Science , vol.235 , pp. 1641-1644
    • Mori, H.1    Kondo, J.2    Ihara, Y.3
  • 43
  • 44
    • 0031043049 scopus 로고    scopus 로고
    • Expression of cell division markers in the hippocampus in Alzheimer's disease and other neurodegenerative conditions
    • Z. Nagy, M.M. Esiri and A.D. Smith, Expression of cell division markers in the hippocampus in Alzheimer's disease and other neurodegenerative conditions, Acta Neuropathol (Berl) 93 (1997), 294-300.
    • (1997) Acta Neuropathol (Berl) , vol.93 , pp. 294-300
    • Nagy, Z.1    Esiri, M.M.2    Smith, A.D.3
  • 46
    • 0001521232 scopus 로고
    • Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains
    • G. Perry, R. Friedman, G. Shaw and V. Chau, Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains, Proc Natl Acad Sci USA 84 (1987), 3033-3036.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3033-3036
    • Perry, G.1    Friedman, R.2    Shaw, G.3    Chau, V.4
  • 47
    • 0033036818 scopus 로고    scopus 로고
    • Quinone reductase (NQO1), a sensitive redox indicator, is increased in Alzheimer's disease
    • A.K. Raina, D.J. Templeton, J.C. Deak, G. Perry and M.A. Smith, Quinone reductase (NQO1), a sensitive redox indicator, is increased in Alzheimer's disease, Redox Rep 4 (1999), 23-27.
    • (1999) Redox Rep , vol.4 , pp. 23-27
    • Raina, A.K.1    Templeton, D.J.2    Deak, J.C.3    Perry, G.4    Smith, M.A.5
  • 48
    • 0034661784 scopus 로고    scopus 로고
    • Cyclin' toward dementia: Cell cycle abnormalities and abortive oncogenesis in Alzheimer disease
    • A.K. Raina, X. Zhu, C.A. Rottkamp, M. Monteiro, A. Takeda and M.A. Smith, Cyclin' toward dementia: cell cycle abnormalities and abortive oncogenesis in Alzheimer disease, J Neurosci Res 61 (2000), 128-133.
    • (2000) J Neurosci Res , vol.61 , pp. 128-133
    • Raina, A.K.1    Zhu, X.2    Rottkamp, C.A.3    Monteiro, M.4    Takeda, A.5    Smith, M.A.6
  • 49
    • 27544484846 scopus 로고    scopus 로고
    • Are mitochondria critical in the pathogenesis of Alzheimer's disease?
    • P.H. Reddy and M.F. Beal, Are mitochondria critical in the pathogenesis of Alzheimer's disease? Brain Res Brain Res Rev 49 (2005), 618-632.
    • (2005) Brain Res Brain Res Rev , vol.49 , pp. 618-632
    • Reddy, P.H.1    Beal, M.F.2
  • 50
    • 0033569839 scopus 로고    scopus 로고
    • Increased neuronal glucose-6-phosphate dehydrogenase and sulfhydryl levels indicate reductive compensation to oxidative stress in Alzheimer disease
    • R.L. Russell, S.L. Siedlak, A.K. Raina, J.M. Bautista, M.A. Smith and G. Perry, Increased neuronal glucose-6-phosphate dehydrogenase and sulfhydryl levels indicate reductive compensation to oxidative stress in Alzheimer disease, Arch Biochem Biophys 370 (1999), 236-239.
    • (1999) Arch Biochem Biophys , vol.370 , pp. 236-239
    • Russell, R.L.1    Siedlak, S.L.2    Raina, A.K.3    Bautista, J.M.4    Smith, M.A.5    Perry, G.6
  • 53
    • 0030989545 scopus 로고    scopus 로고
    • 4-Hydroxynonenal-derived advanced lipid peroxidation end products are increased in Alzheimer's disease
    • L.M. Sayre, D.A. Zelasko, P.L. Harris, G. Perry, R.G. Salomon and M.A. Smith, 4-Hydroxynonenal-derived advanced lipid peroxidation end products are increased in Alzheimer's disease, J Neurochem 68 (1997), 2092-2097.
    • (1997) J Neurochem , vol.68 , pp. 2092-2097
    • Sayre, L.M.1    Zelasko, D.A.2    Harris, P.L.3    Perry, G.4    Salomon, R.G.5    Smith, M.A.6
  • 54
    • 0022524476 scopus 로고
    • Changes in cellular ploidy and autophagic responsiveness during rat liver carcinogenesis
    • P.O. Seglen, P.E. Schwarze and G. Saeter, Changes in cellular ploidy and autophagic responsiveness during rat liver carcinogenesis, Toxicol Pathol 14 (1986), 342-348.
    • (1986) Toxicol Pathol , vol.14 , pp. 342-348
    • Seglen, P.O.1    Schwarze, P.E.2    Saeter, G.3
  • 55
    • 0034603414 scopus 로고    scopus 로고
    • Vascular abnormalities: The insidious pathogenesis of Alzheimer's disease
    • J. Shi, G. Perry, M.A. Smith and R.P. Friedland, Vascular abnormalities: the insidious pathogenesis of Alzheimer's disease, Neurobiol Aging 21 (2000), 357-361.
    • (2000) Neurobiol Aging , vol.21 , pp. 357-361
    • Shi, J.1    Perry, G.2    Smith, M.A.3    Friedland, R.P.4
  • 57
    • 0029007478 scopus 로고
    • Carbonyl-related posttranslational modification of neurofilament protein in the neurofibrillary pathology of Alzheimer's disease
    • M.A. Smith, M. Rudnicka-Nawrot, P.L. Richey, D. Praprotnik, P. Mulvihill, C.A. Miller, L.M. Sayre and G. Perry, Carbonyl-related posttranslational modification of neurofilament protein in the neurofibrillary pathology of Alzheimer's disease, J Neurochem 64 (1995), 2660-2666.
    • (1995) J Neurochem , vol.64 , pp. 2660-2666
    • Smith, M.A.1    Rudnicka-Nawrot, M.2    Richey, P.L.3    Praprotnik, D.4    Mulvihill, P.5    Miller, C.A.6    Sayre, L.M.7    Perry, G.8
  • 60
    • 0030885482 scopus 로고    scopus 로고
    • Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
    • M.A. Smith, P.L. Harris, L.M. Sayre and G. Perry, Iron accumulation in Alzheimer disease is a source of redox-generated free radicals, Proc Natl Acad Sci USA 94 (1997), 9866-9868.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9866-9868
    • Smith, M.A.1    Harris, P.L.2    Sayre, L.M.3    Perry, G.4
  • 62
    • 0031064856 scopus 로고    scopus 로고
    • Developmental changes in calcium content of ultrastructurally distinct subcellular compartments of preimplantation human embryos
    • M. Sousa, A. Barros, J. Silva and J. Tesarik, Developmental changes in calcium content of ultrastructurally distinct subcellular compartments of preimplantation human embryos, Mol Hum Reprod 3 (1997), 83-90.
    • (1997) Mol Hum Reprod , vol.3 , pp. 83-90
    • Sousa, M.1    Barros, A.2    Silva, J.3    Tesarik, J.4
  • 64
    • 0033836580 scopus 로고    scopus 로고
    • In Alzheimer's disease, heme oxygenase is coincident with Alz50, an epitope of tau induced by 4-hydroxy-2-nonenal modification
    • A. Takeda, M.A. Smith, J. Avila, A. Nunomura, S.L. Siedlak, X. Zhu, G. Perry and L.M. Sayre, In Alzheimer's disease, heme oxygenase is coincident with Alz50, an epitope of tau induced by 4-hydroxy-2-nonenal modification, J Neurochem 75 (2000), 1234-1241.
    • (2000) J Neurochem , vol.75 , pp. 1234-1241
    • Takeda, A.1    Smith, M.A.2    Avila, J.3    Nunomura, A.4    Siedlak, S.L.5    Zhu, X.6    Perry, G.7    Sayre, L.M.8
  • 65
    • 24144438228 scopus 로고    scopus 로고
    • Differentiated Alzheimer's disease transmitochondrial cybrid cell lines exhibit reduced organelle movement
    • P.A. Trimmer and M.K. Borland, Differentiated Alzheimer's disease transmitochondrial cybrid cell lines exhibit reduced organelle movement, Antioxid Redox Signal 7 (2005), 1101-1109.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 1101-1109
    • Trimmer, P.A.1    Borland, M.K.2
  • 66
    • 0030062245 scopus 로고    scopus 로고
    • Mitotic mechanisms in Alzheimer's disease?
    • I. Vincent, M. Rosado and P. Davies, Mitotic mechanisms in Alzheimer's disease? J Cell Biol 132 (1996), 413-425.
    • (1996) J Cell Biol , vol.132 , pp. 413-425
    • Vincent, I.1    Rosado, M.2    Davies, P.3
  • 67
    • 0031006939 scopus 로고    scopus 로고
    • Aberrant expression of mitotic cdc2/cyclin B1 kinase in degenerating neurons of Alzheimer's disease brain
    • I. Vincent, G. Jicha, M. Rosado and D.W. Dickson, Aberrant expression of mitotic cdc2/cyclin B1 kinase in degenerating neurons of Alzheimer's disease brain, J Neurosci 17 (1997), 3588-3598.
    • (1997) J Neurosci , vol.17 , pp. 3588-3598
    • Vincent, I.1    Jicha, G.2    Rosado, M.3    Dickson, D.W.4
  • 68
    • 0031959242 scopus 로고    scopus 로고
    • Neurotransmitter regulation of MAP kinase signaling in striatal neurons in primary culture
    • S.R. Vincent, M. Sebben, A. Dumuis and J. Bockaert, Neurotransmitter regulation of MAP kinase signaling in striatal neurons in primary culture, Synapse 29 (1998), 29-36.
    • (1998) Synapse , vol.29 , pp. 29-36
    • Vincent, S.R.1    Sebben, M.2    Dumuis, A.3    Bockaert, J.4
  • 70
    • 0029076397 scopus 로고
    • Nonenzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid beta-peptide
    • S.D. Yan, S.F. Yan, X. Chen, J. Fu, M. Chen, P. Kuppusamy, M.A. Smith, G. Perry, G.C. Godman, P. Nawroth et al., Nonenzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid beta-peptide, Nat Med 1 (1995), 693-699.
    • (1995) Nat Med , vol.1 , pp. 693-699
    • Yan, S.D.1    Yan, S.F.2    Chen, X.3    Fu, J.4    Chen, M.5    Kuppusamy, P.6    Smith, M.A.7    Perry, G.8    Godman, G.C.9    Nawroth, P.10
  • 71
    • 0032814262 scopus 로고    scopus 로고
    • Cell cycle events in neurons. Proliferation or death?
    • X. Zhu, A.K. Raina and M.A. Smith, Cell cycle events in neurons. Proliferation or death? Am J Pathol 155 (1999), 327-329.
    • (1999) Am J Pathol , vol.155 , pp. 327-329
    • Zhu, X.1    Raina, A.K.2    Smith, M.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.