메뉴 건너뛰기




Volumn 8, Issue 6, 2009, Pages 492-511

Mitochondria as a therapeutic target in Alzheimer's disease and diabetes

Author keywords

Alzheimer's disease; Antioxidants; Diabetes; Mitochondria; MitoQ; MitoVitE; SS peptides

Indexed keywords

ACETYLCYSTEINE; ALPHA TOCOPHEROL; CELECOXIB; CREATINE; DOCOSAHEXAENOIC ACID; DONEPEZIL; FOLIC ACID; GLYCEROPHOSPHORYLCHOLINE; INSULIN; LEVACECARNINE; MINOCYCLINE; PHOSPHATIDYLSERINE; PLACEBO; PYRIDOXINE; RIVASTIGMINE; S ADENOSYLMETHIONINE; THIOCTIC ACID; UBIDECARENONE;

EID: 75849136180     PISSN: 18715273     EISSN: None     Source Type: Journal    
DOI: 10.2174/187152709789824651     Document Type: Review
Times cited : (41)

References (276)
  • 2
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • Selkoe, D.J. Translating cell biology into therapeutic advances in Alzheimer's disease. Nature, 1999, 399, A23-A31.
    • (1999) Nature , vol.399
    • Selkoe, D.J.1
  • 3
  • 4
    • 1842454125 scopus 로고    scopus 로고
    • Chemistry and biochemistry of type 2 diabetes
    • Ross, S.A.; Gulve, E.A.; Wang, M. Chemistry and biochemistry of type 2 diabetes. Chem. Rev., 2004, 104, 1255-1282.
    • (2004) Chem. Rev , vol.104 , pp. 1255-1282
    • Ross, S.A.1    Gulve, E.A.2    Wang, M.3
  • 5
    • 0027434987 scopus 로고
    • Neurotoxicity of human amylin in rat primary hippocampal cultures: Similarity to Alzheimer's disease amyloid-beta neurotoxicity
    • May, P.C.; Boggs, L.N.; Fuson, K.S. Neurotoxicity of human amylin in rat primary hippocampal cultures: similarity to Alzheimer's disease amyloid-beta neurotoxicity. J. Neurochem., 1993, 61, 2330-2333.
    • (1993) J. Neurochem , vol.61 , pp. 2330-2333
    • May, P.C.1    Boggs, L.N.2    Fuson, K.S.3
  • 6
    • 0031754613 scopus 로고    scopus 로고
    • Human amylin induces "apoptotic" pattern of gene expression concomitant with cortical neuronal apoptosis
    • Tucker, H.M.; Rydel, R.E.; Wright, S.; Estus, S. Human amylin induces "apoptotic" pattern of gene expression concomitant with cortical neuronal apoptosis. J. Neurochem., 1998, 71, 506-516.
    • (1998) J. Neurochem , vol.71 , pp. 506-516
    • Tucker, H.M.1    Rydel, R.E.2    Wright, S.3    Estus, S.4
  • 7
    • 44749083630 scopus 로고    scopus 로고
    • Human but not rat amylin shares neurotoxic properties with Abeta42 in long-term hippocampal and cortical cultures
    • Lim, Y.A.; Ittner, L.M.; Lim, Y.L.; Götz, J. Human but not rat amylin shares neurotoxic properties with Abeta42 in long-term hippocampal and cortical cultures. FEBS Lett., 2008, 582, 2188-2194.
    • (2008) FEBS Lett , vol.582 , pp. 2188-2194
    • Lim, Y.A.1    Ittner, L.M.2    Lim, Y.L.3    Götz, J.4
  • 9
    • 0036364543 scopus 로고    scopus 로고
    • Standards of medical care for patients with diabetes mellitus
    • American Diabetes Association
    • American Diabetes Association. Standards of medical care for patients with diabetes mellitus. Diabetes Care, 2002, 25, 213-229.
    • (2002) Diabetes Care , vol.25 , pp. 213-229
  • 10
    • 0000291879 scopus 로고
    • Psychologic tests applied in diabetic patients
    • Miles, W.R.; Root, H.F. Psychologic tests applied in diabetic patients. Arch. Intern. Med., 1922, 30, 767-777.
    • (1922) Arch. Intern. Med , vol.30 , pp. 767-777
    • Miles, W.R.1    Root, H.F.2
  • 11
    • 0031957582 scopus 로고    scopus 로고
    • Cognitive impairment in patients with type 1 (insulin-dependent) diabetes mellitus
    • Weinger, K.; Jacobson, A.M. Cognitive impairment in patients with type 1 (insulin-dependent) diabetes mellitus. CNS Drugs, 1998, 9, 233-252.
    • (1998) CNS Drugs , vol.9 , pp. 233-252
    • Weinger, K.1    Jacobson, A.M.2
  • 13
    • 0033301784 scopus 로고    scopus 로고
    • Dietary links to Alzheimer's disease: 1999 update
    • Grant, W.B. Dietary links to Alzheimer's disease: 1999 update. J. Alzheimers Dis., 1999, 1, 197-201.
    • (1999) J. Alzheimers Dis , vol.1 , pp. 197-201
    • Grant, W.B.1
  • 14
  • 15
    • 1242316296 scopus 로고    scopus 로고
    • Insulin and neurodegenerative disease: Shared and specific mechanisms
    • Craft, S.; Watson, G.S. Insulin and neurodegenerative disease: shared and specific mechanisms. Lancet Neurol., 2004, 3, 169-178.
    • (2004) Lancet Neurol , vol.3 , pp. 169-178
    • Craft, S.1    Watson, G.S.2
  • 16
    • 34249821079 scopus 로고    scopus 로고
    • Brain mitochondrial dysfunction as a link between Alzheimer's disease and diabetes
    • Moreira, P.I.; Santos, M.S.; Seiça, R.; Oliveira, C.R. Brain mitochondrial dysfunction as a link between Alzheimer's disease and diabetes. J. Neurol. Sci., 2007, 257, 206-214.
    • (2007) J. Neurol. Sci , vol.257 , pp. 206-214
    • Moreira, P.I.1    Santos, M.S.2    Seiça, R.3    Oliveira, C.R.4
  • 18
    • 0041833733 scopus 로고    scopus 로고
    • Pancreatic beta-cell loss and preservation in type 2 diabetes
    • Buchanan, T.A. Pancreatic beta-cell loss and preservation in type 2 diabetes. Clin. Ther., 2003, 25, B32-B46.
    • (2003) Clin. Ther , vol.25
    • Buchanan, T.A.1
  • 19
    • 38149042694 scopus 로고    scopus 로고
    • An overview of pancreatic beta-cell defects in human type 2 diabetes: Implications for treatment
    • Marchetti, P.; Dotta, F.; Lauro, D.; Purrello, F. An overview of pancreatic beta-cell defects in human type 2 diabetes: implications for treatment. Regul. Pept., 2008, 146, 4-11.
    • (2008) Regul. Pept , vol.146 , pp. 4-11
    • Marchetti, P.1    Dotta, F.2    Lauro, D.3    Purrello, F.4
  • 23
    • 0034707612 scopus 로고    scopus 로고
    • Is diabetes associated with cognitive impairment and cognitive decline among older women? Study of Osteoporotic Fractures Research Group
    • Gregg, E.W.; Yaffe, K.; Cauley, J.A.; Rolka, D.B.; Blackwell, T.L.; Narayan, K.M.; Cummings, S.R. Is diabetes associated with cognitive impairment and cognitive decline among older women? Study of Osteoporotic Fractures Research Group. Arch. Intern. Med., 2000, 160, 174-180.
    • (2000) Arch. Intern. Med , vol.160 , pp. 174-180
    • Gregg, E.W.1    Yaffe, K.2    Cauley, J.A.3    Rolka, D.B.4    Blackwell, T.L.5    Narayan, K.M.6    Cummings, S.R.7
  • 27
    • 0027193817 scopus 로고
    • Genetic mutations affecting human lipoproteins, their receptors, and their enzymes
    • Zannis V.I.; Kardassis D.; Zanni, E.E. Genetic mutations affecting human lipoproteins, their receptors, and their enzymes, Adv. Hum. Genet., 1993, 21, 145-319.
    • (1993) Adv. Hum. Genet , vol.21 , pp. 145-319
    • Zannis, V.I.1    Kardassis, D.2    Zanni, E.E.3
  • 31
    • 0036227542 scopus 로고    scopus 로고
    • Honolulu-Asia Aging Study. Type 2 diabetes, APOE gene, and the risk for dementia and related pathologies: The Honolulu-Asia Aging Study
    • Peila, R.; Rodriguez, B.L.; Launer, L.J. Honolulu-Asia Aging Study. Type 2 diabetes, APOE gene, and the risk for dementia and related pathologies: The Honolulu-Asia Aging Study. Diabetes, 2002, 51, 1256-1262.
    • (2002) Diabetes , vol.51 , pp. 1256-1262
    • Peila, R.1    Rodriguez, B.L.2    Launer, L.J.3
  • 34
    • 33847061307 scopus 로고    scopus 로고
    • The effect of borderline diabetes on the risk of dementia and Alzheimer's disease
    • Xu, W.; Qiu, C.; Winblad, B.; Fratiglioni, L. The effect of borderline diabetes on the risk of dementia and Alzheimer's disease. Diabetes, 2007, 56, 211-216.
    • (2007) Diabetes , vol.56 , pp. 211-216
    • Xu, W.1    Qiu, C.2    Winblad, B.3    Fratiglioni, L.4
  • 36
    • 9844229370 scopus 로고    scopus 로고
    • Association between features of the insulin resistance syndrome and Alzheimer's disease independently of apolipoprotein E4 phenotype: Cross sectional population based study
    • Kuusisto, J.; Koivisto, K.; Mykkanen, L.; Helkala, E.L.; Vanhanen, M.; Hanninen, T.; Kervinen, K.; Kesaniemi, Y.A.; Riekkinen, P.J.; Laakso, M. Association between features of the insulin resistance syndrome and Alzheimer's disease independently of apolipoprotein E4 phenotype: cross sectional population based study. BMJ, 1997, 315, 1045-1049.
    • (1997) BMJ , vol.315 , pp. 1045-1049
    • Kuusisto, J.1    Koivisto, K.2    Mykkanen, L.3    Helkala, E.L.4    Vanhanen, M.5    Hanninen, T.6    Kervinen, K.7    Kesaniemi, Y.A.8    Riekkinen, P.J.9    Laakso, M.10
  • 37
    • 5344256250 scopus 로고    scopus 로고
    • Hyperinsulinemia and risk of Alzheimer disease
    • Luchsinger, J.A.; Tang, M.X.; Shea, S.; Mayeux, R. Hyperinsulinemia and risk of Alzheimer disease. Neurology, 2004, 63, 1187-1192.
    • (2004) Neurology , vol.63 , pp. 1187-1192
    • Luchsinger, J.A.1    Tang, M.X.2    Shea, S.3    Mayeux, R.4
  • 39
    • 75849122299 scopus 로고    scopus 로고
    • Profenno, L.A.; Porsteinsson, A.P.; Faraone, S.V. meta-analysis of Alzheimer's disease risk with obesity, diabetes, and related disorders. Biol. Psychiatry, 2009, [Epub ahead of print].
    • Profenno, L.A.; Porsteinsson, A.P.; Faraone, S.V. meta-analysis of Alzheimer's disease risk with obesity, diabetes, and related disorders. Biol. Psychiatry, 2009, [Epub ahead of print].
  • 42
    • 0034603512 scopus 로고    scopus 로고
    • The role of cerebral ischemia in Alzheimer's disease
    • Kalaria, R.N. The role of cerebral ischemia in Alzheimer's disease. Neurobiol. Aging, 2000, 21, 321-330.
    • (2000) Neurobiol. Aging , vol.21 , pp. 321-330
    • Kalaria, R.N.1
  • 43
    • 0031897103 scopus 로고    scopus 로고
    • Harris, M.I.; Flegal, K.M.; Cowie, C.C.; Eberhardt, M.S.; Goldstein, D.E.; Little, R.R.; Wiedmeyer, H.M.; Byrd-Holt, D.D. Prevalence of diabetes, impaired fasting glucose, and impaired glucose tolerance in U.S. adults. The Third National Health and Nutrition Examination Survey, 1988-1994. Diabetes Care, 1998, 21, 518-524.
    • Harris, M.I.; Flegal, K.M.; Cowie, C.C.; Eberhardt, M.S.; Goldstein, D.E.; Little, R.R.; Wiedmeyer, H.M.; Byrd-Holt, D.D. Prevalence of diabetes, impaired fasting glucose, and impaired glucose tolerance in U.S. adults. The Third National Health and Nutrition Examination Survey, 1988-1994. Diabetes Care, 1998, 21, 518-524.
  • 44
    • 0036062604 scopus 로고    scopus 로고
    • Metabolic sensors: Viewing glucosensing neurons from a broader perspective
    • Levin, B.E. Metabolic sensors: viewing glucosensing neurons from a broader perspective. Physiol. Behav., 2002, 76, 397-401.
    • (2002) Physiol. Behav , vol.76 , pp. 397-401
    • Levin, B.E.1
  • 45
    • 0021278836 scopus 로고
    • Glucose responding neurons in the nucleus tractus solitarius of the rat: In vitro study
    • Mizuno, Y.; Oomura, Y. Glucose responding neurons in the nucleus tractus solitarius of the rat: in vitro study. Brain Res., 1984, 307, 109-116.
    • (1984) Brain Res , vol.307 , pp. 109-116
    • Mizuno, Y.1    Oomura, Y.2
  • 46
    • 0022397729 scopus 로고
    • Actions of feeding-relevant agents on hypothalamic glucose-responsive neurons in vitro
    • Kow, L.M.; Pfaff, D.W. Actions of feeding-relevant agents on hypothalamic glucose-responsive neurons in vitro. Brain Res. Bull., 1985, 15, 509-513.
    • (1985) Brain Res. Bull , vol.15 , pp. 509-513
    • Kow, L.M.1    Pfaff, D.W.2
  • 47
    • 0028101988 scopus 로고
    • Extracellular glucose concentration in mammalian brain: Continuous monitoring of changes during increased neuronal activity and upon limitation in oxygen supply in normo-, hypo-, and hyperglycemic animals
    • Silver, I.A.; Erecińska, M. Extracellular glucose concentration in mammalian brain: continuous monitoring of changes during increased neuronal activity and upon limitation in oxygen supply in normo-, hypo-, and hyperglycemic animals. J. Neurosci., 1994, 14, 5068-5076.
    • (1994) J. Neurosci , vol.14 , pp. 5068-5076
    • Silver, I.A.1    Erecińska, M.2
  • 48
    • 0034714313 scopus 로고    scopus 로고
    • Glucose-regulated dopamine release from substantia nigra neurons
    • Levin, B.E. Glucose-regulated dopamine release from substantia nigra neurons. Brain Res., 2000, 874, 158-164.
    • (2000) Brain Res , vol.874 , pp. 158-164
    • Levin, B.E.1
  • 49
    • 63749097442 scopus 로고    scopus 로고
    • Fuel utilization by hypothalamic neurons: Roles for ROS
    • Horvath, T.L.; Andrews, Z.B.; Diano, S. Fuel utilization by hypothalamic neurons: roles for ROS. Trends Endocrinol. Metab., 2009, 20, 78-87.
    • (2009) Trends Endocrinol. Metab , vol.20 , pp. 78-87
    • Horvath, T.L.1    Andrews, Z.B.2    Diano, S.3
  • 50
    • 0025162079 scopus 로고
    • Glucose-induced excitation of hypothalamic neurones is mediated by ATP-sensitive K+ channels
    • Ashford, M.L.; Boden, P.R.; Treherne, J.M. Glucose-induced excitation of hypothalamic neurones is mediated by ATP-sensitive K+ channels. Pflugers Arch., 1990, 415, 479-483.
    • (1990) Pflugers Arch , vol.415 , pp. 479-483
    • Ashford, M.L.1    Boden, P.R.2    Treherne, J.M.3
  • 52
    • 0032829063 scopus 로고    scopus 로고
    • Hypothalamic glucose sensor: Similarities to and differences from pancreatic beta-cell mechanisms
    • Yang, X.J.; Kow, L.M.; Funabashi, T.; Mobbs, C.V. Hypothalamic glucose sensor: similarities to and differences from pancreatic beta-cell mechanisms. Diabetes, 1999, 48, 1763-1772.
    • (1999) Diabetes , vol.48 , pp. 1763-1772
    • Yang, X.J.1    Kow, L.M.2    Funabashi, T.3    Mobbs, C.V.4
  • 53
    • 0037052544 scopus 로고    scopus 로고
    • Ablation of insulin-producing neurons in flies: Growth and diabetic phenotypes
    • Rulifson, E.J.; Kim, S.K.; Nusse, R. Ablation of insulin-producing neurons in flies: growth and diabetic phenotypes. Science, 2002, 296, 1118-1120.
    • (2002) Science , vol.296 , pp. 1118-1120
    • Rulifson, E.J.1    Kim, S.K.2    Nusse, R.3
  • 54
    • 0037470501 scopus 로고    scopus 로고
    • The endocrine regulation of aging by insulin-like signals
    • Tatar, M.; Bartke, A.; Antebi, A. The endocrine regulation of aging by insulin-like signals. Science, 2003, 299, 1346-1351.
    • (2003) Science , vol.299 , pp. 1346-1351
    • Tatar, M.1    Bartke, A.2    Antebi, A.3
  • 55
    • 57049125529 scopus 로고    scopus 로고
    • Defective insulin signaling pathway and increased glycogen synthase kinase-3 activity in the brain of diabetic mice: Parallels with Alzheimer's disease and correction by insulin
    • Jolivalt, C.G.; Lee, C.A.; Beiswenger, K.K.; Smith, J.L.; Orlov, M.; Torrance, M.A.; Masliah, E. Defective insulin signaling pathway and increased glycogen synthase kinase-3 activity in the brain of diabetic mice: parallels with Alzheimer's disease and correction by insulin. J. Neurosci. Res., 2008, 86, 3265-3274.
    • (2008) J. Neurosci. Res , vol.86 , pp. 3265-3274
    • Jolivalt, C.G.1    Lee, C.A.2    Beiswenger, K.K.3    Smith, J.L.4    Orlov, M.5    Torrance, M.A.6    Masliah, E.7
  • 56
    • 0030748390 scopus 로고    scopus 로고
    • Insulin and insulin-like growth factor-1 regulate tau phosphorylation in cultured human neurons
    • Hong, M.; Lee, V.M. Insulin and insulin-like growth factor-1 regulate tau phosphorylation in cultured human neurons. J. Biol. Chem., 1997, 272, 19547-19553.
    • (1997) J. Biol. Chem , vol.272 , pp. 19547-19553
    • Hong, M.1    Lee, V.M.2
  • 59
    • 0034329543 scopus 로고    scopus 로고
    • Phosphorylation of human tau protein by microtubule-associated kinases: GSK3beta and cdk5 are key participants
    • Flaherty, D.B.; Soria, J.P.; Tomasiewicz, H.G.; Wood, J.G. Phosphorylation of human tau protein by microtubule-associated kinases: GSK3beta and cdk5 are key participants. J. Neurosci. Res., 2000, 62, 463-472.
    • (2000) J. Neurosci. Res , vol.62 , pp. 463-472
    • Flaherty, D.B.1    Soria, J.P.2    Tomasiewicz, H.G.3    Wood, J.G.4
  • 60
    • 23044481208 scopus 로고    scopus 로고
    • The effect of insulin deficiency on tau and neurofilament in the insulin knockout mouse
    • Schechter, R.; Beju, D.; Miller, K.E. The effect of insulin deficiency on tau and neurofilament in the insulin knockout mouse. Biochem. Biophys. Res. Commun., 2005, 334, 979-986.
    • (2005) Biochem. Biophys. Res. Commun , vol.334 , pp. 979-986
    • Schechter, R.1    Beju, D.2    Miller, K.E.3
  • 61
    • 33845515523 scopus 로고    scopus 로고
    • Tau is hyperphosphorylated at multiple sites in mouse brain in vivo after streptozotocin-induced insulin deficiency
    • Clodfelder-Miller, B.J.; Zmijewska, A.A.; Johnson, G.V.; Jope, R.S. Tau is hyperphosphorylated at multiple sites in mouse brain in vivo after streptozotocin-induced insulin deficiency. Diabetes, 2006, 55, 3320-3325.
    • (2006) Diabetes , vol.55 , pp. 3320-3325
    • Clodfelder-Miller, B.J.1    Zmijewska, A.A.2    Johnson, G.V.3    Jope, R.S.4
  • 63
    • 0031913246 scopus 로고    scopus 로고
    • Mechanism of activation and function of protein kinase B
    • Alessi, D.R.; Cohen, P. Mechanism of activation and function of protein kinase B. Curr. Opin. Genet. Dev., 1998, 8, 55-62.
    • (1998) Curr. Opin. Genet. Dev , vol.8 , pp. 55-62
    • Alessi, D.R.1    Cohen, P.2
  • 64
    • 0034653608 scopus 로고    scopus 로고
    • The PI3K-PDK1 connection: More than just a road to PKB
    • Vanhaesebroeck, A.; Alessi, D.R. The PI3K-PDK1 connection: more than just a road to PKB. Biochem. J., 2000, 346, 561-576.
    • (2000) Biochem. J , vol.346 , pp. 561-576
    • Vanhaesebroeck, A.1    Alessi, D.R.2
  • 65
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross, D.A.; Alessi, D.R.; Cohen, P.; Andjelkovich, M.; Hemmings, B.A. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature, 1995, 378, 785-789.
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 66
    • 0038187674 scopus 로고    scopus 로고
    • GSK-3alpha regulates production of Alzheimer's disease amyloid-beta peptides
    • Phiel, C.J.; Wilson, C.A.; Lee, V.M.; Klein, P.S. GSK-3alpha regulates production of Alzheimer's disease amyloid-beta peptides. Nature, 2003, 423, 435-439.
    • (2003) Nature , vol.423 , pp. 435-439
    • Phiel, C.J.1    Wilson, C.A.2    Lee, V.M.3    Klein, P.S.4
  • 67
    • 0034012017 scopus 로고    scopus 로고
    • Insulin regulates soluble amyloid precursor protein release via phosphatidyl inositol 3 kinase-dependent pathway
    • Solano, D.C.; Sironi, M.; Bonfini, C.; Solerte, S.B.; Govoni, S.; Racchi, M. Insulin regulates soluble amyloid precursor protein release via phosphatidyl inositol 3 kinase-dependent pathway. FASEB J., 2000, 14, 1015-1022.
    • (2000) FASEB J , vol.14 , pp. 1015-1022
    • Solano, D.C.1    Sironi, M.2    Bonfini, C.3    Solerte, S.B.4    Govoni, S.5    Racchi, M.6
  • 68
    • 0035871641 scopus 로고    scopus 로고
    • Stimulation of beta-amyloid precursor protein trafficking by insulin reduces intraneuronal beta-amyloid and requires mitogen-activated protein kinase signaling
    • Gasparini, L.; Gouras, G.K.; Wang, R.; Gross, R.S.; Beal, M.F.; Greengard, P.; Xu, H. Stimulation of beta-amyloid precursor protein trafficking by insulin reduces intraneuronal beta-amyloid and requires mitogen-activated protein kinase signaling. J. Neurosci., 2001, 21, 2561-2570.
    • (2001) J. Neurosci , vol.21 , pp. 2561-2570
    • Gasparini, L.1    Gouras, G.K.2    Wang, R.3    Gross, R.S.4    Beal, M.F.5    Greengard, P.6    Xu, H.7
  • 69
    • 1842785179 scopus 로고    scopus 로고
    • Glucose metabolism and insulin receptor signal transduction in Alzheimer disease
    • Hoyer, S. Glucose metabolism and insulin receptor signal transduction in Alzheimer disease. Eur. J. Pharmacol., 2004, 490, 115-125.
    • (2004) Eur. J. Pharmacol , vol.490 , pp. 115-125
    • Hoyer, S.1
  • 71
    • 37049008884 scopus 로고    scopus 로고
    • Phosphatidylinositol-3-kinase activation blocks amyloid beta-induced neurotoxicity
    • Lee, K.Y.; Koh, S.H.; Noh, M.Y.; Kim, S.H.; Lee, Y.J. Phosphatidylinositol-3-kinase activation blocks amyloid beta-induced neurotoxicity. Toxicology, 2008, 243, 43-50.
    • (2008) Toxicology , vol.243 , pp. 43-50
    • Lee, K.Y.1    Koh, S.H.2    Noh, M.Y.3    Kim, S.H.4    Lee, Y.J.5
  • 72
    • 0031574345 scopus 로고    scopus 로고
    • Amyloid precursor protein potentiates the neurotrophic activity of NGF
    • Wallace, W.C.; Akar, C.A.; Lyons, W.E. Amyloid precursor protein potentiates the neurotrophic activity of NGF. Mol. Brain Res., 1997, 52, 201-212.
    • (1997) Mol. Brain Res , vol.52 , pp. 201-212
    • Wallace, W.C.1    Akar, C.A.2    Lyons, W.E.3
  • 73
    • 0031574238 scopus 로고    scopus 로고
    • Amyloid precursor protein requires the insulin signalling pathway for neurotrophic activity
    • Wallace, W.C.; Akar, C.A.; Lyons, W.E.; Kole, H.K.; Egan, J.E.; Wolozin, B. Amyloid precursor protein requires the insulin signalling pathway for neurotrophic activity. Mol. Brain Res., 1997, 52, 213-227.
    • (1997) Mol. Brain Res , vol.52 , pp. 213-227
    • Wallace, W.C.1    Akar, C.A.2    Lyons, W.E.3    Kole, H.K.4    Egan, J.E.5    Wolozin, B.6
  • 74
    • 0035282739 scopus 로고    scopus 로고
    • Characterization of the neurotrophic interaction between nerve growth factor and secreted alpha-amyloid precursor protein
    • Luo, J.J.; Wallace, M.S.; Hawver, D.B.; Kusiak, J.W.; Wallace, W.C. Characterization of the neurotrophic interaction between nerve growth factor and secreted alpha-amyloid precursor protein. J. Neurosci. Res., 2001, 63, 410-420.
    • (2001) J. Neurosci. Res , vol.63 , pp. 410-420
    • Luo, J.J.1    Wallace, M.S.2    Hawver, D.B.3    Kusiak, J.W.4    Wallace, W.C.5
  • 76
    • 0042822110 scopus 로고    scopus 로고
    • An insulin-degrading enzyme inhibitor decreases amylin degradation, increases amylin-induced cytotoxicity, and increases amyloid formation in insulinoma cell cultures
    • Bennett, R.G.; Hamel, F.G.; Duckworth, W.C. An insulin-degrading enzyme inhibitor decreases amylin degradation, increases amylin-induced cytotoxicity, and increases amyloid formation in insulinoma cell cultures. Diabetes, 2003, 52, 2315-2320.
    • (2003) Diabetes , vol.52 , pp. 2315-2320
    • Bennett, R.G.1    Hamel, F.G.2    Duckworth, W.C.3
  • 77
    • 0028176821 scopus 로고
    • Alzheimer's beta-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme
    • Kurochkin, I.V.; Goto, S. Alzheimer's beta-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme. FEBS Lett., 1994, 345, 33-37.
    • (1994) FEBS Lett , vol.345 , pp. 33-37
    • Kurochkin, I.V.1    Goto, S.2
  • 78
    • 0031044352 scopus 로고    scopus 로고
    • Degradation of Alzheimer's beta-amyloid protein by human and rat brain peptidases: Involvement of insulin-degrading enzyme
    • McDermott, J.R.; Gibson, A.M. Degradation of Alzheimer's beta-amyloid protein by human and rat brain peptidases: involvement of insulin-degrading enzyme. Neurochem. Res., 1997, 22, 49-56.
    • (1997) Neurochem. Res , vol.22 , pp. 49-56
    • McDermott, J.R.1    Gibson, A.M.2
  • 80
    • 22244456767 scopus 로고    scopus 로고
    • Insulysin: An allosteric enzyme as a target for Alzheimer's disease
    • Song, E.S.; Hersh, L.B. Insulysin: an allosteric enzyme as a target for Alzheimer's disease. J. Mol. Neurosci., 2005, 25, 201-206.
    • (2005) J. Mol. Neurosci , vol.25 , pp. 201-206
    • Song, E.S.1    Hersh, L.B.2
  • 82
    • 0034161516 scopus 로고    scopus 로고
    • Neurons regulate extracellular levels of amyloid beta-protein via proteolysis by insulin-degrading enzyme
    • Vekrellis, K.; Ye, Z.; Qiu, W.Q.; Walsh, D.; Hartley, D.; Chesneau, V.; Rosner, M.R.; Selkoe, D.J. Neurons regulate extracellular levels of amyloid beta-protein via proteolysis by insulin-degrading enzyme. J. Neurosci., 2000, 20, 1657-1665.
    • (2000) J. Neurosci , vol.20 , pp. 1657-1665
    • Vekrellis, K.1    Ye, Z.2    Qiu, W.Q.3    Walsh, D.4    Hartley, D.5    Chesneau, V.6    Rosner, M.R.7    Selkoe, D.J.8
  • 83
    • 0037134505 scopus 로고    scopus 로고
    • Insulin-degrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD)
    • Edbauer, D.; Willem, M.; Lammich, S.; Steiner, H.; Haass, C. Insulin-degrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD). J. Biol. Chem., 2002, 277, 13389-13393.
    • (2002) J. Biol. Chem , vol.277 , pp. 13389-13393
    • Edbauer, D.1    Willem, M.2    Lammich, S.3    Steiner, H.4    Haass, C.5
  • 84
    • 0034038036 scopus 로고    scopus 로고
    • Degradation of soluble amyloid beta-peptides 1-40, 1-42, and the Dutch variant 1-40Q by insulin degrading enzyme from Alzheimer disease and control brains
    • Perez, A.; Morelli, L.; Cresto, J.C.; Castano, E.M. Degradation of soluble amyloid beta-peptides 1-40, 1-42, and the Dutch variant 1-40Q by insulin degrading enzyme from Alzheimer disease and control brains. Neurochem. Res., 2000, 25, 247-255.
    • (2000) Neurochem. Res , vol.25 , pp. 247-255
    • Perez, A.1    Morelli, L.2    Cresto, J.C.3    Castano, E.M.4
  • 85
    • 0037219221 scopus 로고    scopus 로고
    • Cook, D.G.; Leverenz, J.B.; McMillan, P.J.; Kulstad, J.J.; Ericksen, S.; Roth, R.A.; Schellenberg, G.D.; Jin, L.W.; Kovacina, K.S.; Craft, S. Reduced hippocampal insulin-degrading enzyme in late-onset Alzheimer's disease is associated with the apolipoprotein E-epsilon4 allele. Am. J. Pathol., 2003, 162, 313-319.
    • Cook, D.G.; Leverenz, J.B.; McMillan, P.J.; Kulstad, J.J.; Ericksen, S.; Roth, R.A.; Schellenberg, G.D.; Jin, L.W.; Kovacina, K.S.; Craft, S. Reduced hippocampal insulin-degrading enzyme in late-onset Alzheimer's disease is associated with the apolipoprotein E-epsilon4 allele. Am. J. Pathol., 2003, 162, 313-319.
  • 87
    • 11244276934 scopus 로고    scopus 로고
    • Insulin-degrading enzyme in brain microvessels: Proteolysis of amyloid {beta} vasculotropic variants and reduced activity in cerebral amyloid angiopathy
    • Morelli, L.; Llovera, R.E.; Mathov, I.; Lue, L.F.; Frangione, B.; Ghiso, J.; Castano, E.M. Insulin-degrading enzyme in brain microvessels: proteolysis of amyloid {beta} vasculotropic variants and reduced activity in cerebral amyloid angiopathy. J. Biol. Chem., 2004, 279, 56004-56013.
    • (2004) J. Biol. Chem , vol.279 , pp. 56004-56013
    • Morelli, L.1    Llovera, R.E.2    Mathov, I.3    Lue, L.F.4    Frangione, B.5    Ghiso, J.6    Castano, E.M.7
  • 88
    • 13644266898 scopus 로고    scopus 로고
    • Age- and region-dependent alterations in Abeta-degrading enzymes: Implications for Abeta-induced disorders
    • Caccamo, A.; Oddo, S.; Sugarman, M.C.; Akbari, Y.; LaFerla, F.M. Age- and region-dependent alterations in Abeta-degrading enzymes: implications for Abeta-induced disorders. Neurobiol. Aging, 2005, 26, 645-654.
    • (2005) Neurobiol. Aging , vol.26 , pp. 645-654
    • Caccamo, A.1    Oddo, S.2    Sugarman, M.C.3    Akbari, Y.4    LaFerla, F.M.5
  • 89
    • 67849110360 scopus 로고    scopus 로고
    • Effects of 4-hydroxynonenal and amyloid-beta on expression and activity of endothelin converting enzyme and insulin degrading enzyme in SH-SY5Y cells
    • Epub ahead of print
    • Wang, R.; Wang, S.; Malter, J.S.; Wang, D.S. Effects of 4-hydroxynonenal and amyloid-beta on expression and activity of endothelin converting enzyme and insulin degrading enzyme in SH-SY5Y cells. J. Alzheimers Dis., 2009, [Epub ahead of print].
    • (2009) J. Alzheimers Dis
    • Wang, R.1    Wang, S.2    Malter, J.S.3    Wang, D.S.4
  • 90
    • 67650544970 scopus 로고    scopus 로고
    • Insulin receptor dysfunction impairs cellular clearance of neurotoxic oligomeric Abeta
    • Zhao, W.Q.; Lacor, P.N.; Chen, H., Lambert, M.P.; Quon, M.J.; Krafft, G.A.; Klein, W.L. Insulin receptor dysfunction impairs cellular clearance of neurotoxic oligomeric Abeta. J. Biol. Chem., 2009, 284, 18742-18753.
    • (2009) J. Biol. Chem , vol.284 , pp. 18742-18753
    • Zhao, W.Q.1    Lacor, P.N.2    Chen, H.3    Lambert, M.P.4    Quon, M.J.5    Krafft, G.A.6    Klein, W.L.7
  • 91
    • 0018090354 scopus 로고
    • Insulin receptors are widely distributed in the central nervous system of the rat
    • Havrankova, J.; Roth, J.; Brownstein, M. Insulin receptors are widely distributed in the central nervous system of the rat. Nature, 1978, 272, 827-829.
    • (1978) Nature , vol.272 , pp. 827-829
    • Havrankova, J.1    Roth, J.2    Brownstein, M.3
  • 94
    • 0025847968 scopus 로고
    • Insulin receptors in the central nervous system: Localization, signalling mechanisms and functional aspects
    • Unger, J.W.; Livingston, J.N.; Moss, A.M. Insulin receptors in the central nervous system: localization, signalling mechanisms and functional aspects. Prog. Neurobiol., 1991, 36, 343-362.
    • (1991) Prog. Neurobiol , vol.36 , pp. 343-362
    • Unger, J.W.1    Livingston, J.N.2    Moss, A.M.3
  • 96
    • 0033664539 scopus 로고    scopus 로고
    • Insulin receptors and insulin action in the brain: Review and clinical implications
    • Schulingkamp, R.J.; Pagano, T.C.; Hung, D.; Raffa, R.B. Insulin receptors and insulin action in the brain: review and clinical implications. Neurosci. Biobehav. Rev., 2000, 24, 855-872.
    • (2000) Neurosci. Biobehav. Rev , vol.24 , pp. 855-872
    • Schulingkamp, R.J.1    Pagano, T.C.2    Hung, D.3    Raffa, R.B.4
  • 97
    • 1842721011 scopus 로고    scopus 로고
    • Brain Energy Metabolism
    • Squire, L.R, Bloom, F.E, McConnell, S.K, Roberts, J.L, Spitzer, N.C, Zigmond, M.J, Eds, Academic Press: San Diego
    • Magistretti, P.J. Brain Energy Metabolism. In: Fundamental Neuroscience; Squire, L.R.; Bloom, F.E.; McConnell, S.K.; Roberts, J.L.; Spitzer, N.C.; Zigmond, M.J., Eds.; Academic Press: San Diego, 2003, pp. 339-360.
    • (2003) Fundamental Neuroscience , pp. 339-360
    • Magistretti, P.J.1
  • 98
    • 0027361094 scopus 로고
    • Saturable transport of insulin from plasma into the central nervous system of dogs in vivo: A mechanism for regulated insulin delivery to the brain
    • Baura, G.D.; Foster, D.M.; Porte, D.; Jr.; Kahn, S.E.; Bergman, R.N.; Cobelli, C.; Schwartz, M.W. Saturable transport of insulin from plasma into the central nervous system of dogs in vivo: a mechanism for regulated insulin delivery to the brain. J. Clin. Invest., 1993, 92, 1824-1830.
    • (1993) J. Clin. Invest , vol.92 , pp. 1824-1830
    • Baura, G.D.1    Foster, D.M.2    Porte Jr., D.3    Kahn, S.E.4    Bergman, R.N.5    Cobelli, C.6    Schwartz, M.W.7
  • 99
    • 0030664286 scopus 로고    scopus 로고
    • Transport of insulin across the blood-brain barrier: Saturability at euglycemic doses of insulin
    • Banks, W.A.; Jaspan, J.B.; Huang, W.; Kastin, A.J. Transport of insulin across the blood-brain barrier: saturability at euglycemic doses of insulin. Peptides, 1997, 18, 1423-1429.
    • (1997) Peptides , vol.18 , pp. 1423-1429
    • Banks, W.A.1    Jaspan, J.B.2    Huang, W.3    Kastin, A.J.4
  • 100
    • 0028080101 scopus 로고
    • Glutamate uptake into astrocytes stimulates aerobic glycolysis: A mechanism coupling neuronal activity to glucose utilization
    • Pellerin, L.; Magistretti, P.J. Glutamate uptake into astrocytes stimulates aerobic glycolysis: a mechanism coupling neuronal activity to glucose utilization. Proc. Natl. Acad. Sci. USA, 1994, 91, 10625-10629.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10625-10629
    • Pellerin, L.1    Magistretti, P.J.2
  • 101
    • 0033664539 scopus 로고    scopus 로고
    • Insulin receptors and insulin action in the brain: Review and clinical implications
    • Schulingkamp, R.J.; Pagano, T.C.; Hung, D.; Raffa, R.B. Insulin receptors and insulin action in the brain: review and clinical implications. Neurosci. Biobehav. Rev., 2000, 24, 855-872.
    • (2000) Neurosci. Biobehav. Rev , vol.24 , pp. 855-872
    • Schulingkamp, R.J.1    Pagano, T.C.2    Hung, D.3    Raffa, R.B.4
  • 103
    • 0027321678 scopus 로고
    • Immunological analysis of glucose transporters expressed in different regions of the rat brain and central nervous system
    • Brant, A.M.; Jess, T.J.; Milligan, G.; Brown, C.M.; Gould, G.W. Immunological analysis of glucose transporters expressed in different regions of the rat brain and central nervous system. Biochem. Biophys. Res. Commun., 1993, 192, 1297-1302.
    • (1993) Biochem. Biophys. Res. Commun , vol.192 , pp. 1297-1302
    • Brant, A.M.1    Jess, T.J.2    Milligan, G.3    Brown, C.M.4    Gould, G.W.5
  • 104
    • 0032487335 scopus 로고    scopus 로고
    • Immunocytochemical localization of the insulin-responsive glucose transporter 4 (GLUT4) in the rat central nervous system
    • El Messari, S.; Leloup, C.; Quignon, M.; Brisorgueil, M.J.; Penicaud, L.; Arluison, M. Immunocytochemical localization of the insulin-responsive glucose transporter 4 (GLUT4) in the rat central nervous system. J. Comp. Neurol., 1998, 399, 492-512.
    • (1998) J. Comp. Neurol , vol.399 , pp. 492-512
    • El Messari, S.1    Leloup, C.2    Quignon, M.3    Brisorgueil, M.J.4    Penicaud, L.5    Arluison, M.6
  • 105
    • 0033199378 scopus 로고    scopus 로고
    • Insulin-sensitive GLUT4 glucose transporters are colocalized with GLUT3-expressing cells and demonstrate a chemically distinct neuron-specific localization in rat brain
    • Apelt, J.; Mehlhorn, G.; Schliebs, R. Insulin-sensitive GLUT4 glucose transporters are colocalized with GLUT3-expressing cells and demonstrate a chemically distinct neuron-specific localization in rat brain. J. Neurosci. Res., 1999, 57, 693-705.
    • (1999) J. Neurosci. Res , vol.57 , pp. 693-705
    • Apelt, J.1    Mehlhorn, G.2    Schliebs, R.3
  • 106
    • 0034681328 scopus 로고    scopus 로고
    • GLUTX1, a novel mammalian glucose transporter expressed in the central nervous system and insulin-sensitive tissues
    • Ibberson, M.; Uldry, M.; Thorens, B. GLUTX1, a novel mammalian glucose transporter expressed in the central nervous system and insulin-sensitive tissues. J. Biol. Chem., 2000, 275, 4607-4612.
    • (2000) J. Biol. Chem , vol.275 , pp. 4607-4612
    • Ibberson, M.1    Uldry, M.2    Thorens, B.3
  • 108
    • 0034128197 scopus 로고    scopus 로고
    • Diabetes downregulates GLUT1 expression in the retina and its microvessels but not in the cerebral cortex or its microvessels
    • Badr, G.A.; Tang, J.; Ismail-Beigi, F.; Kern, T.S. Diabetes downregulates GLUT1 expression in the retina and its microvessels but not in the cerebral cortex or its microvessels. Diabetes, 2000, 49, 1016-1021.
    • (2000) Diabetes , vol.49 , pp. 1016-1021
    • Badr, G.A.1    Tang, J.2    Ismail-Beigi, F.3    Kern, T.S.4
  • 109
    • 0019787087 scopus 로고
    • Blood-brain glucose transfer: Repression in chronic hyperglycemia
    • Gjedde, A.; Crone, C. Blood-brain glucose transfer: repression in chronic hyperglycemia. Science, 1981, 214, 456-457.
    • (1981) Science , vol.214 , pp. 456-457
    • Gjedde, A.1    Crone, C.2
  • 110
    • 0029153836 scopus 로고
    • Down-regulation of blood-brain glucose transport in the hyperglycemic nonobese diabetic mouse
    • Cornford, E.M.; Hyman, S.; Cornford, M.E.; Clare-Salzler, M. Down-regulation of blood-brain glucose transport in the hyperglycemic nonobese diabetic mouse. Neurochem. Res., 1995, 20, 869-873.
    • (1995) Neurochem. Res , vol.20 , pp. 869-873
    • Cornford, E.M.1    Hyman, S.2    Cornford, M.E.3    Clare-Salzler, M.4
  • 111
    • 0032809478 scopus 로고    scopus 로고
    • Cerebrometabolic aspects of delirium in relationship to dementia
    • Blass, J.P.; Gibson, G.E. Cerebrometabolic aspects of delirium in relationship to dementia. Dement. Geriatr. Cogn. Disord., 1999, 10, 335-338.
    • (1999) Dement. Geriatr. Cogn. Disord , vol.10 , pp. 335-338
    • Blass, J.P.1    Gibson, G.E.2
  • 112
    • 0034103586 scopus 로고    scopus 로고
    • Inherent abnormalities in energy metabolism in Alzheimer disease. Interaction with cerebrovascular compromise
    • Blass, J.P.; Sheu, R.K.; Gibson, G.E. Inherent abnormalities in energy metabolism in Alzheimer disease. Interaction with cerebrovascular compromise. Ann. N. Y. Acad. Sci., 2000, 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
  • 114
    • 0028326937 scopus 로고
    • Alterations of cerebral metabolism in probable Alzheimer's disease: A preliminary study
    • Pettegrew, J.W.; Panchalingam, K.; Klunk, W.E.; McClure, R.J.; Muenz, L.R. Alterations of cerebral metabolism in probable Alzheimer's disease: a preliminary study. Neurobiol. Aging, 1994, 15, 117-132.
    • (1994) Neurobiol. Aging , vol.15 , pp. 117-132
    • Pettegrew, J.W.1    Panchalingam, K.2    Klunk, W.E.3    McClure, R.J.4    Muenz, L.R.5
  • 117
    • 0032239618 scopus 로고    scopus 로고
    • Risk factors for Alzheimer's disease during aging. Impacts of glucose/energy metabolism
    • Hoyer, S. Risk factors for Alzheimer's disease during aging. Impacts of glucose/energy metabolism. J. Neural Transm. Suppl., 1998, 54, 187-194.
    • (1998) J. Neural Transm. Suppl , vol.54 , pp. 187-194
    • Hoyer, S.1
  • 118
    • 0029655453 scopus 로고    scopus 로고
    • Plasma membrane fragility in dystrophic neurites in senile plaques of Alzheimer's disease: An index of oxidative stress
    • Praprotnik, D.; Smith, M.A.; Richey, P.L.; Vinters, H.V.; Perry, G. Plasma membrane fragility in dystrophic neurites in senile plaques of Alzheimer's disease: an index of oxidative stress. Acta Neuropathol. (Berl.), 1996, 91, 1-5.
    • (1996) Acta Neuropathol. (Berl.) , vol.91 , pp. 1-5
    • Praprotnik, D.1    Smith, M.A.2    Richey, P.L.3    Vinters, H.V.4    Perry, G.5
  • 119
    • 0030049915 scopus 로고    scopus 로고
    • Filament heterogeneity within the dystrophic neurites of senile plaques suggests blockage of fast axonal transport in Alzheimer's disease
    • Praprotnik, D.; Smith, M.A.; Richey, P.L.; Vinters, H.V.; Perry, G. Filament heterogeneity within the dystrophic neurites of senile plaques suggests blockage of fast axonal transport in Alzheimer's disease. Acta Neuropathol. (Berl.), 1996, 91, 226-235.
    • (1996) Acta Neuropathol. (Berl.) , vol.91 , pp. 226-235
    • Praprotnik, D.1    Smith, M.A.2    Richey, P.L.3    Vinters, H.V.4    Perry, G.5
  • 121
    • 0141705362 scopus 로고    scopus 로고
    • Perry, G.; Nunomura, A.; Raina, A.K,.; Aliev, G.; Siedlak, S.L.; Harris, P.L.; Casadesus, G.; Petersen, R.B.; Bligh-Glover, W.; Balraj, E.; Petot, G.J.; Smith, M.A. A metabolic basis for Alzheimer disease. Neurochem. Res., 2003, 28, 1549-1552.
    • Perry, G.; Nunomura, A.; Raina, A.K,.; Aliev, G.; Siedlak, S.L.; Harris, P.L.; Casadesus, G.; Petersen, R.B.; Bligh-Glover, W.; Balraj, E.; Petot, G.J.; Smith, M.A. A metabolic basis for Alzheimer disease. Neurochem. Res., 2003, 28, 1549-1552.
  • 124
    • 38049050725 scopus 로고    scopus 로고
    • Decreased glucose transporters correlate to abnormal hyperphosphorylation of tau in Alzheimer disease
    • Liu, Y.; Liu, F.; Iqbal, K.; Grundke-Iqbal, I.; Gong, C.X. Decreased glucose transporters correlate to abnormal hyperphosphorylation of tau in Alzheimer disease. FEBS Lett., 2008, 582, 359-364.
    • (2008) FEBS Lett , vol.582 , pp. 359-364
    • Liu, Y.1    Liu, F.2    Iqbal, K.3    Grundke-Iqbal, I.4    Gong, C.X.5
  • 125
    • 67650072530 scopus 로고    scopus 로고
    • Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease
    • Liu, F.; Shi, J.; Tanimukai, H.; Gu, J.; Gu, J.; Grundke-Iqbal, I.; Iqbal, K.; Gong, C.X. Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease. Brain, 2009, 132, 1820-1832.
    • (2009) Brain , vol.132 , pp. 1820-1832
    • Liu, F.1    Shi, J.2    Tanimukai, H.3    Gu, J.4    Gu, J.5    Grundke-Iqbal, I.6    Iqbal, K.7    Gong, C.X.8
  • 127
    • 0027971421 scopus 로고
    • Cognitive declines correlate with decreased cortical volume and perfusion in dementia of Alzheimer type
    • Obara, K.; Meyer, J.S.; Mortel, K.F.; Muramatsu, K. Cognitive declines correlate with decreased cortical volume and perfusion in dementia of Alzheimer type. J. Neurol. Sci., 1994, 127, 96-102.
    • (1994) J. Neurol. Sci , vol.127 , pp. 96-102
    • Obara, K.1    Meyer, J.S.2    Mortel, K.F.3    Muramatsu, K.4
  • 128
    • 44449131492 scopus 로고    scopus 로고
    • SMART Study Group. Diabetes increases atrophy and vascular lesions on brain MRI in patients with symptomatic arterial disease
    • Tiehuis, A.M.; van der Graaf, Y.; Visseren, F.L.; Vincken, K.L.; Biessels, G.J.; Appelman, A.P.; Kappelle, L.J.; Mali, W.P.; SMART Study Group. Diabetes increases atrophy and vascular lesions on brain MRI in patients with symptomatic arterial disease. Stroke, 2008, 39, 1600-1603.
    • (2008) Stroke , vol.39 , pp. 1600-1603
    • Tiehuis, A.M.1    van der Graaf, Y.2    Visseren, F.L.3    Vincken, K.L.4    Biessels, G.J.5    Appelman, A.P.6    Kappelle, L.J.7    Mali, W.P.8
  • 130
    • 33845209331 scopus 로고    scopus 로고
    • Changing cerebral blood flow velocity by transcranial Doppler during head up tilt in patients with diabetes mellitus
    • Asil, T.; Utku, U.; Balci, K.; Uzunca, I. Changing cerebral blood flow velocity by transcranial Doppler during head up tilt in patients with diabetes mellitus. Clin. Neurol. Neurosurg., 2007, 109, 1-6.
    • (2007) Clin. Neurol. Neurosurg , vol.109 , pp. 1-6
    • Asil, T.1    Utku, U.2    Balci, K.3    Uzunca, I.4
  • 131
    • 66249116626 scopus 로고    scopus 로고
    • Preclinical evidence of Alzheimer changes: Convergent cerebrospinal fluid biomarker and fluorodeoxyglucose positron emission tomography findings
    • Petrie, E.C.; Cross, D.J.; Galasko, D.; Schellenberg, G.D.; Raskind, M.A.; Peskind, E.R.; Minoshima, S. Preclinical evidence of Alzheimer changes: convergent cerebrospinal fluid biomarker and fluorodeoxyglucose positron emission tomography findings. Arch. Neurol., 2009, 66, 632-637.
    • (2009) Arch. Neurol , vol.66 , pp. 632-637
    • Petrie, E.C.1    Cross, D.J.2    Galasko, D.3    Schellenberg, G.D.4    Raskind, M.A.5    Peskind, E.R.6    Minoshima, S.7
  • 134
    • 0020685951 scopus 로고
    • Decreased pyruvate dehydrogenase complex activity in Huntington and Alzheimer brain
    • Sorbi, S.; Bird, E.D.; Blass, J.P. Decreased pyruvate dehydrogenase complex activity in Huntington and Alzheimer brain. Ann. Neurol., 1983, 13, 72-78.
    • (1983) Ann. Neurol , vol.13 , pp. 72-78
    • Sorbi, S.1    Bird, E.D.2    Blass, J.P.3
  • 135
    • 0030723048 scopus 로고    scopus 로고
    • Brain energy metabolizing enzymes in Alzheimer's disease: Alpha-ketoglutarate dehydrogenase complex and cytochrome oxidase
    • Kish, S.J. Brain energy metabolizing enzymes in Alzheimer's disease: alpha-ketoglutarate dehydrogenase complex and cytochrome oxidase. Ann. NY Acad. Sci., 1997, 826, 218-228.
    • (1997) Ann. NY Acad. Sci , vol.826 , pp. 218-228
    • Kish, S.J.1
  • 137
    • 18244390483 scopus 로고    scopus 로고
    • Mitochondrial abnormalities in Alzheimer brain: Mechanistic implications
    • Bubber, P.; Haroutunian, V.; Fisch, G.; Blass, J.P.; Gibson, G.E. Mitochondrial abnormalities in Alzheimer brain: mechanistic implications. Ann. Neurol., 2005, 57, 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
  • 138
    • 0034671429 scopus 로고    scopus 로고
    • Inhibition of Krebs cycle enzymes by hydrogen peroxide: A key role of α-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress
    • Tretter, L.; Adam-Vizi, V. Inhibition of Krebs cycle enzymes by hydrogen peroxide: a key role of α-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress. J. Neurosci., 2000, 20, 8972-8979.
    • (2000) J. Neurosci , vol.20 , pp. 8972-8979
    • Tretter, L.1    Adam-Vizi, V.2
  • 139
    • 0018826694 scopus 로고
    • Coenzyme A-acetylating enzymes in Alzheimer's disease: Possible cholinergic 'compartment' of pyruvate dehydrogenase
    • Perry, E.K.; Perry, R.H.; Tomlinson, B.E.; Blessed, G.; Gibson, P.H. Coenzyme A-acetylating enzymes in Alzheimer's disease: possible cholinergic 'compartment' of pyruvate dehydrogenase. Neurosci. Lett., 1980, 18, 105-110.
    • (1980) Neurosci. Lett , vol.18 , pp. 105-110
    • Perry, E.K.1    Perry, R.H.2    Tomlinson, B.E.3    Blessed, G.4    Gibson, P.H.5
  • 140
    • 0032405857 scopus 로고    scopus 로고
    • Reduced levels of cholesterol, phospholipids, and fatty acids in cerebrospinal fluid of Alzheimer disease patients are not related to apolipoprotein E4
    • Mulder, M.; Ravid, R.; Swaab, D.F.; de Kloet, E.R.; Haasdijk, E.D.; Julk, J.; van der Boom, J.; Havekes, L.M. Reduced levels of cholesterol, phospholipids, and fatty acids in cerebrospinal fluid of Alzheimer disease patients are not related to apolipoprotein E4. Alzheimer Dis. Assoc. Disord., 1998, 12, 198-203.
    • (1998) Alzheimer Dis. Assoc. Disord , vol.12 , pp. 198-203
    • Mulder, M.1    Ravid, R.2    Swaab, D.F.3    de Kloet, E.R.4    Haasdijk, E.D.5    Julk, J.6    van der Boom, J.7    Havekes, L.M.8
  • 141
    • 0026781603 scopus 로고
    • Oxidative energy metabolism in Alzheimer brain. Studies in early-onset and late-onset cases
    • Hoyer, S. Oxidative energy metabolism in Alzheimer brain. Studies in early-onset and late-onset cases. Mol. Chem. Neuropathol., 1992, 16, 207-224.
    • (1992) Mol. Chem. Neuropathol , vol.16 , pp. 207-224
    • Hoyer, S.1
  • 145
    • 0028110234 scopus 로고
    • Cortical cytochrome oxidase activity is reduced in Alzheimer's disease
    • Mutisya, E.M.; Bowling, A.C.; Beal, M.F. Cortical cytochrome oxidase activity is reduced in Alzheimer's disease. J. Neurochem., 1994, 63, 2179-2184.
    • (1994) J. Neurochem , vol.63 , pp. 2179-2184
    • Mutisya, E.M.1    Bowling, A.C.2    Beal, M.F.3
  • 146
    • 0028948660 scopus 로고
    • Distribution of brain cytochrome oxidase activity in various neurodegenerative diseases
    • Chagnon, P.; Bétard, C.; Robitaille, Y.; Cholette, A.; Gauvreau, D. Distribution of brain cytochrome oxidase activity in various neurodegenerative diseases. Neuroreport, 1995, 6, 711-715.
    • (1995) Neuroreport , vol.6 , pp. 711-715
    • Chagnon, P.1    Bétard, C.2    Robitaille, Y.3    Cholette, A.4    Gauvreau, D.5
  • 148
    • 0024448458 scopus 로고
    • Human cells lacking mtDNA: Repopulation with exogenous mitochondria by complementation
    • King, M.P.; Attardi, G. Human cells lacking mtDNA: repopulation with exogenous mitochondria by complementation. Science, 1989, 246, 500-503.
    • (1989) Science , vol.246 , pp. 500-503
    • King, M.P.1    Attardi, G.2
  • 149
    • 12644257598 scopus 로고    scopus 로고
    • Davis, R.E.; Miller, S.; Hermstadt, C.; Ghosh, S.S.; Fahy, E.; Shinobu, L.A.; Galasko, D.; Thal, L.J.; Beal, M.F.; Howell, N.; Parker, W.D.; Jr. Mutations in mitochondrial cytochrome c oxidase genes segregate with late-onset Alzheimer's disease. Proc. Natl. Acad. Sci. USA, 1997, 94, 4526-4531.
    • Davis, R.E.; Miller, S.; Hermstadt, C.; Ghosh, S.S.; Fahy, E.; Shinobu, L.A.; Galasko, D.; Thal, L.J.; Beal, M.F.; Howell, N.; Parker, W.D.; Jr. Mutations in mitochondrial cytochrome c oxidase genes segregate with late-onset Alzheimer's disease. Proc. Natl. Acad. Sci. USA, 1997, 94, 4526-4531.
  • 151
    • 3042513691 scopus 로고    scopus 로고
    • Mitochondria dysfunction of Alzheimer's disease cybrids enhances Abeta toxicity
    • Cardoso, S.M.; Santana, I.; Swerdlow, R.H.; Oliveira, C.R. Mitochondria dysfunction of Alzheimer's disease cybrids enhances Abeta toxicity. J. Neurochem., 2004, 89, 1417-1426.
    • (2004) J. Neurochem , vol.89 , pp. 1417-1426
    • Cardoso, S.M.1    Santana, I.2    Swerdlow, R.H.3    Oliveira, C.R.4
  • 152
    • 22544477523 scopus 로고    scopus 로고
    • Drug-associated mitochondrial toxicity and its detection
    • Amacher, D.E. Drug-associated mitochondrial toxicity and its detection. Curr. Med. Chem., 2005, 12, 1829-1839.
    • (2005) Curr. Med. Chem , vol.12 , pp. 1829-1839
    • Amacher, D.E.1
  • 153
    • 34249788738 scopus 로고    scopus 로고
    • Mitochondria, metabolic disturbances, oxidative stress and the kynurenine system, with focus on neurodegenerative disorders
    • Sas, K.; Robotka, H.; Toldi, J.; Vécsei, L. Mitochondria, metabolic disturbances, oxidative stress and the kynurenine system, with focus on neurodegenerative disorders. J. Neurol. Sci., 2007, 257, 221-239.
    • (2007) J. Neurol. Sci , vol.257 , pp. 221-239
    • Sas, K.1    Robotka, H.2    Toldi, J.3    Vécsei, L.4
  • 154
    • 67649687039 scopus 로고    scopus 로고
    • An integrative view of the role of oxidative stress, mitochondria and insulin in Alzheimer's disease
    • Moreira, P.I.; Duarte, A.I.; Santos, M.S.; Rego, A.C.; Oliveira, C.R. An integrative view of the role of oxidative stress, mitochondria and insulin in Alzheimer's disease. J. Alzheimers Dis., 2009, 16, 741-761.
    • (2009) J. Alzheimers Dis , vol.16 , pp. 741-761
    • Moreira, P.I.1    Duarte, A.I.2    Santos, M.S.3    Rego, A.C.4    Oliveira, C.R.5
  • 155
    • 0036224781 scopus 로고    scopus 로고
    • Xanthine oxidase is involved in free radical production in type 1 diabetes: Protection by allopurinol
    • Desco, M.C.; Asensi, M.; Marquez, R.; Martinez-Valls, J.; Vento, M.; Pallardo, F.V. Xanthine oxidase is involved in free radical production in type 1 diabetes: protection by allopurinol. Diabetes, 2002, 51, 1118-1124.
    • (2002) Diabetes , vol.51 , pp. 1118-1124
    • Desco, M.C.1    Asensi, M.2    Marquez, R.3    Martinez-Valls, J.4    Vento, M.5    Pallardo, F.V.6
  • 157
    • 0025732948 scopus 로고
    • Role of oxidative stress in development of complications in diabetes
    • Baynes, J.W. Role of oxidative stress in development of complications in diabetes. Diabetes, 1991, 40, 405-412.
    • (1991) Diabetes , vol.40 , pp. 405-412
    • Baynes, J.W.1
  • 158
    • 0343674519 scopus 로고    scopus 로고
    • Oxidative stress and HNE conjugation of GLUT3 are increased in the hippocampus of diabetic rats subjected to stress
    • Reagan, L.P.; Magarinos, A.M.; Yee, D.K.; Swzeda, L.I.; Van Bueren, A.; McCall, A.L.; McEwen, B.S. Oxidative stress and HNE conjugation of GLUT3 are increased in the hippocampus of diabetic rats subjected to stress. Brain Res., 2000, 862, 292-300.
    • (2000) Brain Res , vol.862 , pp. 292-300
    • Reagan, L.P.1    Magarinos, A.M.2    Yee, D.K.3    Swzeda, L.I.4    Van Bueren, A.5    McCall, A.L.6    McEwen, B.S.7
  • 159
    • 66649095843 scopus 로고    scopus 로고
    • Development of selective axonopathy in adult sensory neurons isolated from diabetic rats: Role of glucose-induced oxidative stress
    • Zherebitskaya, E.; Akude, E.; Smith, D.R.; Fernyhough, P. Development of selective axonopathy in adult sensory neurons isolated from diabetic rats: role of glucose-induced oxidative stress. Diabetes, 2009, 58, 1356-1364.
    • (2009) Diabetes , vol.58 , pp. 1356-1364
    • Zherebitskaya, E.1    Akude, E.2    Smith, D.R.3    Fernyhough, P.4
  • 160
    • 0036796875 scopus 로고    scopus 로고
    • Oxidative stress and stress-activated signaling pathways: A unifying hypothesis of type 2 diabetes
    • Evans, J.L.; Goldfine, I.D.; Maddux, B.A.; Grodsky, G.M. Oxidative stress and stress-activated signaling pathways: a unifying hypothesis of type 2 diabetes. Endocr. Rev., 2002, 23, 599-622.
    • (2002) Endocr. Rev , vol.23 , pp. 599-622
    • Evans, J.L.1    Goldfine, I.D.2    Maddux, B.A.3    Grodsky, G.M.4
  • 162
    • 33751233521 scopus 로고    scopus 로고
    • Oxidative burden in prediabetic and diabetic individuals: Evidence from plasma coenzyme Q(10)
    • Lim, S.C.; Tan, H.H.; Goh, S.K.; Subramaniam, T.; Sum, C.F.; Tan, I.K.; Lee, B.L.; Ong, C.N. Oxidative burden in prediabetic and diabetic individuals: evidence from plasma coenzyme Q(10). Diabet. Med., 2006, 23, 1344-1349.
    • (2006) Diabet. Med , vol.23 , pp. 1344-1349
    • Lim, S.C.1    Tan, H.H.2    Goh, S.K.3    Subramaniam, T.4    Sum, C.F.5    Tan, I.K.6    Lee, B.L.7    Ong, C.N.8
  • 163
    • 0030667861 scopus 로고    scopus 로고
    • Dehydroepiandrosterone administration prevents the oxidative damage induced by acute hyperglycemia in rats
    • Aragno, M.; Brignardello, E.; Tamagno, E.; Gatto, V.; Danni, O.; Boccuzzi, G. Dehydroepiandrosterone administration prevents the oxidative damage induced by acute hyperglycemia in rats. J. Endocrinol., 1997, 155, 233-240.
    • (1997) J. Endocrinol , vol.155 , pp. 233-240
    • Aragno, M.1    Brignardello, E.2    Tamagno, E.3    Gatto, V.4    Danni, O.5    Boccuzzi, G.6
  • 164
    • 0037222391 scopus 로고    scopus 로고
    • Oxidative injury and apoptosis of dorsal root ganglion neurons in chronic experimental diabetic neuropathy
    • Schmeichel, A.M.; Schmelzer, J.D.; Low, P.A. Oxidative injury and apoptosis of dorsal root ganglion neurons in chronic experimental diabetic neuropathy. Diabetes, 2003, 52, 165-71.
    • (2003) Diabetes , vol.52 , pp. 165-171
    • Schmeichel, A.M.1    Schmelzer, J.D.2    Low, P.A.3
  • 165
    • 33746881744 scopus 로고    scopus 로고
    • Mitochondria in DRG neurons undergo hyperglycemic mediated injury through Bim, Bax and the fission protein Drp1
    • Leinninger, G.M.; Backus, C.; Sastry, A.M.; Yi, Y.B.; Wang, C.W.; Feldman, E.L. Mitochondria in DRG neurons undergo hyperglycemic mediated injury through Bim, Bax and the fission protein Drp1. Neurobiol. Dis., 2006, 23, 11-22.
    • (2006) Neurobiol. Dis , vol.23 , pp. 11-22
    • Leinninger, G.M.1    Backus, C.2    Sastry, A.M.3    Yi, Y.B.4    Wang, C.W.5    Feldman, E.L.6
  • 166
    • 46749156297 scopus 로고    scopus 로고
    • Mitochondrial fission mediates high glucose-induced cell death through elevated production of reactive oxygen species
    • Yu, T.; Sheu, S.S.; Robotham, J.L.; Yoon, Y. Mitochondrial fission mediates high glucose-induced cell death through elevated production of reactive oxygen species. Cardiovasc. Res., 2008, 79, 341-351.
    • (2008) Cardiovasc. Res , vol.79 , pp. 341-351
    • Yu, T.1    Sheu, S.S.2    Robotham, J.L.3    Yoon, Y.4
  • 167
    • 14744294296 scopus 로고    scopus 로고
    • Insulin protects against amyloid β-peptide toxicity in brain mitochondria of diabetic rats
    • Moreira, P.I.; Santos, M.S.; Sena, C.; Seiça, R.; Oliveira, C.R. Insulin protects against amyloid β-peptide toxicity in brain mitochondria of diabetic rats. Neurobiol. Dis., 2005, 18, 628-637.
    • (2005) Neurobiol. Dis , vol.18 , pp. 628-637
    • Moreira, P.I.1    Santos, M.S.2    Sena, C.3    Seiça, R.4    Oliveira, C.R.5
  • 168
    • 0025286523 scopus 로고
    • The participation of coenzyme Q in free radical production and antioxidation
    • Beyer, R.E. The participation of coenzyme Q in free radical production and antioxidation. Free Radic. Biol. Med., 1990, 8, 545-565.
    • (1990) Free Radic. Biol. Med , vol.8 , pp. 545-565
    • Beyer, R.E.1
  • 169
    • 0029042393 scopus 로고
    • Biochemical, physiological and medical aspects of ubiquinone function
    • Ernster, L.; Dallner, G. Biochemical, physiological and medical aspects of ubiquinone function. Biochim. Biophys. Acta, 1995, 1271, 195-204.
    • (1995) Biochim. Biophys. Acta , vol.1271 , pp. 195-204
    • Ernster, L.1    Dallner, G.2
  • 170
    • 0033626607 scopus 로고    scopus 로고
    • Ubiquinone (coenzyme Q10) and complex I in mitochondrial oxidative disorder of Parkinson's disease
    • Ebadi, M.; Muralikrishnan, D.; Pellett, L.J.; Murphy, T.; Drees, K. Ubiquinone (coenzyme Q10) and complex I in mitochondrial oxidative disorder of Parkinson's disease. Proc. West. Pharmacol. Soc., 2000, 43, 55-63.
    • (2000) Proc. West. Pharmacol. Soc , vol.43 , pp. 55-63
    • Ebadi, M.1    Muralikrishnan, D.2    Pellett, L.J.3    Murphy, T.4    Drees, K.5
  • 171
    • 0030046495 scopus 로고    scopus 로고
    • Mitochondria and diabetes. Genetic, biochemical, and clinical implications of the cellular energy circuit
    • Gerbitz, K.D.; Gempel, K.; Brdiczka, D. Mitochondria and diabetes. Genetic, biochemical, and clinical implications of the cellular energy circuit. Diabetes, 1996, 45, 113-126.
    • (1996) Diabetes , vol.45 , pp. 113-126
    • Gerbitz, K.D.1    Gempel, K.2    Brdiczka, D.3
  • 172
    • 0032976998 scopus 로고    scopus 로고
    • Functional and morphological abnormalities of mitochondria harboring the tRNA (Leu) (UUR) mutation in mitochondrial DNA derived from patients with maternally inherited diabetes and deafness (MIDD) and progressive kidney disease
    • van den Ouweland, J.M.; Maechler, P.; Wollheim, C.B.; Attardi, G.; Maassen, J.A. Functional and morphological abnormalities of mitochondria harboring the tRNA (Leu) (UUR) mutation in mitochondrial DNA derived from patients with maternally inherited diabetes and deafness (MIDD) and progressive kidney disease. Diabetologia, 1999, 42, 485-492.
    • (1999) Diabetologia , vol.42 , pp. 485-492
    • van den Ouweland, J.M.1    Maechler, P.2    Wollheim, C.B.3    Attardi, G.4    Maassen, J.A.5
  • 173
    • 0023235492 scopus 로고
    • Treatment of patients with non-insulin dependent diabetes mellitus: Diabetic control and insulin secretion and action after different treatment modalities
    • Hollenbeck, C.B.; Reaven, G.M. Treatment of patients with non-insulin dependent diabetes mellitus: diabetic control and insulin secretion and action after different treatment modalities. Diabet. Med., 1987, 4, 311-316.
    • (1987) Diabet. Med , vol.4 , pp. 311-316
    • Hollenbeck, C.B.1    Reaven, G.M.2
  • 174
    • 0038321341 scopus 로고    scopus 로고
    • Increased vulnerability of brain mitochondria in diabetic (Goto-Kakizaki) rats with aging and amyloid-beta exposure
    • Moreira, P.I.; Santos, M.S.; Moreno, A.M.; Seiça, R.; Oliveira, C.R. Increased vulnerability of brain mitochondria in diabetic (Goto-Kakizaki) rats with aging and amyloid-beta exposure. Diabetes, 2003, 52, 1449-1456.
    • (2003) Diabetes , vol.52 , pp. 1449-1456
    • Moreira, P.I.1    Santos, M.S.2    Moreno, A.M.3    Seiça, R.4    Oliveira, C.R.5
  • 175
    • 12244299849 scopus 로고    scopus 로고
    • Increase of glial fibrillary acidic protein and S-100B in hippocampus and cortex of diabetic rats: Effects of vitamin E
    • Baydas, G.; Nedzvetskii, V.S.; Tuzcu, M.; Yasar, A.; Kirichenko, S.V. Increase of glial fibrillary acidic protein and S-100B in hippocampus and cortex of diabetic rats: effects of vitamin E. Eur. J. Pharmacol., 2003, 462, 67-71.
    • (2003) Eur. J. Pharmacol , vol.462 , pp. 67-71
    • Baydas, G.1    Nedzvetskii, V.S.2    Tuzcu, M.3    Yasar, A.4    Kirichenko, S.V.5
  • 176
    • 33748293101 scopus 로고    scopus 로고
    • Upregulation of glyoxalase fails to normalize methylglyoxal levels: A possible mechanism for biochemical changes in diabetic mouse lense
    • Staniszewska, M.M.; Nagaraj, R.H. Upregulation of glyoxalase fails to normalize methylglyoxal levels: a possible mechanism for biochemical changes in diabetic mouse lense. Mol. Cell Biochem., 2006, 288, 29-36.
    • (2006) Mol. Cell Biochem , vol.288 , pp. 29-36
    • Staniszewska, M.M.1    Nagaraj, R.H.2
  • 178
    • 67649695176 scopus 로고    scopus 로고
    • Involvement of toxic AGEs (TAGE) in the pathogenesis of diabetic vascular complications and Alzheimer's disease
    • Takeuchi, M.; Yamagishi, S. Involvement of toxic AGEs (TAGE) in the pathogenesis of diabetic vascular complications and Alzheimer's disease. J. Alzheimers Dis., 2009, 16, 845-858.
    • (2009) J. Alzheimers Dis , vol.16 , pp. 845-858
    • Takeuchi, M.1    Yamagishi, S.2
  • 180
    • 0028831997 scopus 로고
    • Calcium signaling
    • Clapham, D.E. Calcium signaling. Cell, 1995, 80, 259-268.
    • (1995) Cell , vol.80 , pp. 259-268
    • Clapham, D.E.1
  • 181
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Drögue, W. Free radicals in the physiological control of cell function. Physiol. Rev., 2002, 82, 47-95.
    • (2002) Physiol. Rev , vol.82 , pp. 47-95
    • Drögue, W.1
  • 182
    • 70349105567 scopus 로고    scopus 로고
    • Mitochondrial permeability transition pore opening as a promising therapeutic target in cardiac diseases
    • Javadov, S.; Karmazyn, M.; Escobales, N. Mitochondrial permeability transition pore opening as a promising therapeutic target in cardiac diseases. J. Pharmacol. Exp. Ther., 2009, 330, 670-678.
    • (2009) J. Pharmacol. Exp. Ther , vol.330 , pp. 670-678
    • Javadov, S.1    Karmazyn, M.2    Escobales, N.3
  • 183
    • 0028651951 scopus 로고
    • Calcium hypothesis of Alzheimer's disease and brain aging
    • Khachaturian, Z.S. Calcium hypothesis of Alzheimer's disease and brain aging. Ann. NY Acad. Sci., 1994, 747, 1-11.
    • (1994) Ann. NY Acad. Sci , vol.747 , pp. 1-11
    • Khachaturian, Z.S.1
  • 184
    • 0034780525 scopus 로고    scopus 로고
    • Diabetes-induced changes in calcium homeostasis and the effects of calcium channel blockers in rat and mice nociceptive neurons
    • Kostyuk, E.; Voitenko, N.; Kruglikov, I.; Shmigol, A.; Shishkin, V.; Efimov, A.; Kostyuk, P. Diabetes-induced changes in calcium homeostasis and the effects of calcium channel blockers in rat and mice nociceptive neurons. Diabetologia, 2001, 44, 1302-1309.
    • (2001) Diabetologia , vol.44 , pp. 1302-1309
    • Kostyuk, E.1    Voitenko, N.2    Kruglikov, I.3    Shmigol, A.4    Shishkin, V.5    Efimov, A.6    Kostyuk, P.7
  • 185
    • 0031884263 scopus 로고    scopus 로고
    • Reactive, degenerative, and proliferative Schwann cell responses in experimental galactose and human diabetic neuropathy
    • Kalichman, M.W.; Powell, H.C.; Mizisin, A.P. Reactive, degenerative, and proliferative Schwann cell responses in experimental galactose and human diabetic neuropathy. Acta Neuropathol. (Berl.), 1998, 95, 47-56.
    • (1998) Acta Neuropathol. (Berl.) , vol.95 , pp. 47-56
    • Kalichman, M.W.1    Powell, H.C.2    Mizisin, A.P.3
  • 186
    • 0031018374 scopus 로고    scopus 로고
    • Neuropathology and blood flow of nerve, spinal roots and dorsal root ganglia in longstanding diabetic rats
    • Sasaki, H.; Schmelzer, J.D.; Zollman, P.J.; Low, P.A. Neuropathology and blood flow of nerve, spinal roots and dorsal root ganglia in longstanding diabetic rats. Acta Neuropathol. (Berl.), 1997, 93, 118-128.
    • (1997) Acta Neuropathol. (Berl.) , vol.93 , pp. 118-128
    • Sasaki, H.1    Schmelzer, J.D.2    Zollman, P.J.3    Low, P.A.4
  • 191
    • 0037437192 scopus 로고    scopus 로고
    • Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells
    • Anandatheerthavarada, H.K.; Biswas, G.; Robin, M.A.; Avadhani, N.G. Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells. J. Cell Biol., 2003, 161, 41-54.
    • (2003) J. Cell Biol , vol.161 , pp. 41-54
    • Anandatheerthavarada, H.K.1    Biswas, G.2    Robin, M.A.3    Avadhani, N.G.4
  • 192
    • 9144260111 scopus 로고    scopus 로고
    • Alternative translation initiation generates a novel isoform of insulin-degrading enzyme targeted to mitochondria
    • Leissring, M.A.; Farris, W.; Wu, X.; Christodoulou, D.C.; Haigis, M.C.; Guarente, L.; Selkoe, D.J. Alternative translation initiation generates a novel isoform of insulin-degrading enzyme targeted to mitochondria. Biochem. J., 2004, 383, 439-446.
    • (2004) Biochem. J , vol.383 , pp. 439-446
    • Leissring, M.A.1    Farris, W.2    Wu, X.3    Christodoulou, D.C.4    Haigis, M.C.5    Guarente, L.6    Selkoe, D.J.7
  • 193
    • 19944373389 scopus 로고    scopus 로고
    • Hansson, C.A.; Frykman, S.; Farmery, M.R.; Tjernberg, L.O.; Nilsberth, C; Pursglove, S.E.; Ito, A.; Winblad, B.; Cowburn, R.F.; Thyberg, J.; Ankarcrona, M. Nicastrin, presenilin, APH-1, and PEN-2 form active gamma-secretase complexes in mitochondria. J. Biol. Chem., 2004, 279, 51654-51660.
    • Hansson, C.A.; Frykman, S.; Farmery, M.R.; Tjernberg, L.O.; Nilsberth, C; Pursglove, S.E.; Ito, A.; Winblad, B.; Cowburn, R.F.; Thyberg, J.; Ankarcrona, M. Nicastrin, presenilin, APH-1, and PEN-2 form active gamma-secretase complexes in mitochondria. J. Biol. Chem., 2004, 279, 51654-51660.
  • 194
    • 0035378322 scopus 로고    scopus 로고
    • Functional mitochondria are required for amyloid beta-mediated neurotoxicity
    • Cardoso, S.M.; Santos, S.; Swerdlow, R.H.; Oliveira, C.R. Functional mitochondria are required for amyloid beta-mediated neurotoxicity. FASEB J., 2001, 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
  • 195
    • 0032104130 scopus 로고    scopus 로고
    • Mitochondrial function impairment induced by amyloid beta-peptide on PC12 cells
    • Pereira, C.; Santos, M.S.; Oliveira, C. Mitochondrial function impairment induced by amyloid beta-peptide on PC12 cells. Neuroreport, 1998, 9, 1749-1755.
    • (1998) Neuroreport , vol.9 , pp. 1749-1755
    • Pereira, C.1    Santos, M.S.2    Oliveira, C.3
  • 196
    • 0033022771 scopus 로고    scopus 로고
    • Involvement of oxidative stress on the impairment of energy metabolism induced by Abeta peptides on PC12 cells: Protection by antioxidants
    • Pereira, C.; Santos, M.S.; Oliveira, C. Involvement of oxidative stress on the impairment of energy metabolism induced by Abeta peptides on PC12 cells: protection by antioxidants. Neurobiol. Dis., 1999, 6, 209-219.
    • (1999) Neurobiol. Dis , vol.6 , pp. 209-219
    • Pereira, C.1    Santos, M.S.2    Oliveira, C.3
  • 200
    • 26244447857 scopus 로고    scopus 로고
    • CoQ10 therapy attenuates amyloid beta-peptide toxicity in brain mitochondria isolated from aged diabetic rats
    • Moreira, P.I.; Santos, M.S.; Sena, C.; Nunes, E.; Seiça, R.; Oliveira, C.R. CoQ10 therapy attenuates amyloid beta-peptide toxicity in brain mitochondria isolated from aged diabetic rats. Exp. Neurol., 2005, 196, 112-119.
    • (2005) Exp. Neurol , vol.196 , pp. 112-119
    • Moreira, P.I.1    Santos, M.S.2    Sena, C.3    Nunes, E.4    Seiça, R.5    Oliveira, C.R.6
  • 201
    • 0035780141 scopus 로고    scopus 로고
    • Amyloid beta-peptide promotes permeability transition pore in brain mitochondria
    • Moreira, P.I.; Santos, M.S.; Moreno, A.; Oliveira, C. Amyloid beta-peptide promotes permeability transition pore in brain mitochondria. Biosci. Rep., 2001, 21, 789-800.
    • (2001) Biosci. Rep , vol.21 , pp. 789-800
    • Moreira, P.I.1    Santos, M.S.2    Moreno, A.3    Oliveira, C.4
  • 202
    • 0037100213 scopus 로고    scopus 로고
    • Effect of amyloid beta-peptide on permeability transition pore: A comparative study
    • Moreira, P.I.; Santos, M.S.; Moreno, A.; Rego, A.C.; Oliveira, C. Effect of amyloid beta-peptide on permeability transition pore: a comparative study. J. Neurosci. Res., 2002, 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
  • 203
    • 0028233494 scopus 로고    scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • Behl, C.; Davies, J.B.; Lesley, R.; Schubert, D. Hydrogen peroxide mediates amyloid beta protein toxicity. Cell, 1997, 77, 817-827.
    • (1997) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davies, J.B.2    Lesley, R.3    Schubert, D.4
  • 204
    • 0035696298 scopus 로고    scopus 로고
    • Inhibition of catalase activity with 3-amino-triaz-ole enhances the cytotoxicity of the Alzheimer's amyloid-β peptide
    • Milton, N.G.N. Inhibition of catalase activity with 3-amino-triaz-ole enhances the cytotoxicity of the Alzheimer's amyloid-β peptide. Neurotoxicology, 2001, 22, 767-774.
    • (2001) Neurotoxicology , vol.22 , pp. 767-774
    • Milton, N.G.N.1
  • 205
    • 0038271638 scopus 로고    scopus 로고
    • Effect of insulin on human skeletal muscle mitochondrial ATP production, protein synthesis, and mRNA transcripts
    • Stump, C.S.; Short, K.R.; Bigelow, M.L.; Schimke, J.M.; Nair, K.S. Effect of insulin on human skeletal muscle mitochondrial ATP production, protein synthesis, and mRNA transcripts. Proc. Natl. Acad. Sci. USA, 2003, 100, 7996-8001.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7996-8001
    • Stump, C.S.1    Short, K.R.2    Bigelow, M.L.3    Schimke, J.M.4    Nair, K.S.5
  • 206
    • 0035651021 scopus 로고    scopus 로고
    • Tissue-specific regulation of mitochondrial and cytoplasmic protein synthesis rates by insulin
    • Boirie, Y.; Short, K.R.; Ahlman, B.; Charlton, M.; Nair, K.S. Tissue-specific regulation of mitochondrial and cytoplasmic protein synthesis rates by insulin. Diabetes, 2001, 50, 2652-2658.
    • (2001) Diabetes , vol.50 , pp. 2652-2658
    • Boirie, Y.1    Short, K.R.2    Ahlman, B.3    Charlton, M.4    Nair, K.S.5
  • 207
    • 3042751024 scopus 로고    scopus 로고
    • Insulin-like growth factor type 1 prevents hyperglycemia-induced uncoupling protein 3 down-regulation and oxidative stress
    • Gustafsson, H.; Soderdahl, T.; Jonsson, G.; Bratteng, J.O.; Forsby, A. Insulin-like growth factor type 1 prevents hyperglycemia-induced uncoupling protein 3 down-regulation and oxidative stress. J. Neurosci. Res., 2004, 77, 285-291.
    • (2004) J. Neurosci. Res , vol.77 , pp. 285-291
    • Gustafsson, H.1    Soderdahl, T.2    Jonsson, G.3    Bratteng, J.O.4    Forsby, A.5
  • 208
    • 0041765665 scopus 로고    scopus 로고
    • Insulin prevents depolarization of the mitochondrial inner membrane in sensory neurons of type 1 diabetic rats in the presence of sustained hyperglycemia
    • Huang, T.J.; Price, S.A.; Chilton, L.; Calcutt, N.A.; Tomlinson, D.R.; Verkhratsky, A.; Fernyhough, P. Insulin prevents depolarization of the mitochondrial inner membrane in sensory neurons of type 1 diabetic rats in the presence of sustained hyperglycemia. Diabetes, 2003, 52, 2129-2136.
    • (2003) Diabetes , vol.52 , pp. 2129-2136
    • Huang, T.J.1    Price, S.A.2    Chilton, L.3    Calcutt, N.A.4    Tomlinson, D.R.5    Verkhratsky, A.6    Fernyhough, P.7
  • 209
    • 65549099294 scopus 로고    scopus 로고
    • Insulin-like growth factor-1 receptor activation prevents high glucose-induced mitochondrial dysfunction, cytochrome-c release and apoptosis
    • Li, Y.; Wu, H.; Khardori, R.; Song, Y.H.; Lu, Y.W.; Geng, Y.J. Insulin-like growth factor-1 receptor activation prevents high glucose-induced mitochondrial dysfunction, cytochrome-c release and apoptosis. Biochem. Biophys. Res. Commun., 2009, 384, 259-264.
    • (2009) Biochem. Biophys. Res. Commun , vol.384 , pp. 259-264
    • Li, Y.1    Wu, H.2    Khardori, R.3    Song, Y.H.4    Lu, Y.W.5    Geng, Y.J.6
  • 210
    • 0035951395 scopus 로고    scopus 로고
    • Insulin-like growth factor-1 protects H9c2 cardiac myoblasts from oxidative stress-induced apoptosis via phosphatidylinositol 3-kinase and extracellular signal-regulated kinase pathways
    • Hong, F.; Kwon, S.J.; Jhun, B.S.; Kim, S.S.; Ha, J.; Kim, S.J.; Sohn, N.W.; Kang, C.; Kang, I. Insulin-like growth factor-1 protects H9c2 cardiac myoblasts from oxidative stress-induced apoptosis via phosphatidylinositol 3-kinase and extracellular signal-regulated kinase pathways. Life Sci., 2001, 68, 1095-1105.
    • (2001) Life Sci , vol.68 , pp. 1095-1105
    • Hong, F.1    Kwon, S.J.2    Jhun, B.S.3    Kim, S.S.4    Ha, J.5    Kim, S.J.6    Sohn, N.W.7    Kang, C.8    Kang, I.9
  • 211
    • 0032886133 scopus 로고    scopus 로고
    • Insulin-like growth factor-I protects myoblasts from apoptosis but requires other factors to stimulate proliferation
    • Napier, J.R.; Thomas, M.F.; Sharma, M.; Hodgkinson, S.C.; Blass, J.J. Insulin-like growth factor-I protects myoblasts from apoptosis but requires other factors to stimulate proliferation. J. Endocrinol., 1999, 163, 63-68.
    • (1999) J. Endocrinol , vol.163 , pp. 63-68
    • Napier, J.R.1    Thomas, M.F.2    Sharma, M.3    Hodgkinson, S.C.4    Blass, J.J.5
  • 212
    • 33644623231 scopus 로고    scopus 로고
    • Insulin neuroprotection against oxidative stress in cortical neurons - involvement of uric acid and glutathione antioxidant defenses
    • Duarte, A.I.; Santos, M.S.; Oliveira, C.R.; Rego, A.C. Insulin neuroprotection against oxidative stress in cortical neurons - involvement of uric acid and glutathione antioxidant defenses. Free Radic. Biol. Med., 2005, 39, 876-889.
    • (2005) Free Radic. Biol. Med , vol.39 , pp. 876-889
    • Duarte, A.I.1    Santos, M.S.2    Oliveira, C.R.3    Rego, A.C.4
  • 213
    • 43549087343 scopus 로고    scopus 로고
    • Insulin neuroprotection against oxidative stress is mediated by Akt and GSK-3beta signaling pathways and changes in protein expression
    • Duarte, A.I.; Santos, P.; Oliveira, C.R.; Santos, M.S.; Rego, A.C. Insulin neuroprotection against oxidative stress is mediated by Akt and GSK-3beta signaling pathways and changes in protein expression. Biochim. Biophys. Acta, 2008, 1783, 994-1002.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 994-1002
    • Duarte, A.I.1    Santos, P.2    Oliveira, C.R.3    Santos, M.S.4    Rego, A.C.5
  • 214
    • 0035869351 scopus 로고    scopus 로고
    • Insulin-like growth factor I (IGF-I) protects cells from apoptosis by Alzheimer's V642I mutant amyloid precursor protein through IGF-I receptor in an IGF-binding protein-sensitive manner
    • Niikura, T.; Hashimoto, Y.; Okamoto, T.; Abe, Y.; Yasukawa, T.; Kawasumi, M.; Hiraki, T.; Kita, Y.; Terashita, K.; Kouyama, K.; Nishimoto, I. Insulin-like growth factor I (IGF-I) protects cells from apoptosis by Alzheimer's V642I mutant amyloid precursor protein through IGF-I receptor in an IGF-binding protein-sensitive manner. J. Neurosci., 2001, 21, 1902-1910.
    • (2001) J. Neurosci , vol.21 , pp. 1902-1910
    • Niikura, T.1    Hashimoto, Y.2    Okamoto, T.3    Abe, Y.4    Yasukawa, T.5    Kawasumi, M.6    Hiraki, T.7    Kita, Y.8    Terashita, K.9    Kouyama, K.10    Nishimoto, I.11
  • 216
    • 67349086876 scopus 로고    scopus 로고
    • Conversion to dementia in mild cognitive impairment is associated with decline of N-actylaspartate and creatine as revealed by magnetic resonance spectroscopy
    • Pilatus; U.; Lais, C.; Rochmont, A.D.; Kratzsch, T.; Frölich, L.; Maurer, K.; Zanella, F.E.; Lanfermann, H.; Pantel, J. Conversion to dementia in mild cognitive impairment is associated with decline of N-actylaspartate and creatine as revealed by magnetic resonance spectroscopy. Psychiatry Res., 2009, 173, 1-7.
    • (2009) Psychiatry Res , vol.173 , pp. 1-7
    • Pilatus, U.1    Lais, C.2    Rochmont, A.D.3    Kratzsch, T.4    Frölich, L.5    Maurer, K.6    Zanella, F.E.7    Lanfermann, H.8    Pantel, J.9
  • 220
    • 0034737380 scopus 로고    scopus 로고
    • Neuroprotective effects of creatine administration against NMDA and malonate toxicity
    • Malcon, C.; Kaddurah-Daouk, R.; Beal, M.F. Neuroprotective effects of creatine administration against NMDA and malonate toxicity. Brain Res., 2000, 860, 195-198.
    • (2000) Brain Res , vol.860 , pp. 195-198
    • Malcon, C.1    Kaddurah-Daouk, R.2    Beal, M.F.3
  • 221
    • 0033767740 scopus 로고    scopus 로고
    • Dietary supplement creatine protects against traumatic brain injury
    • Sullivan, P.G.; Geiger, J.D.; Mattson, M.P.; Scheff, S.W. Dietary supplement creatine protects against traumatic brain injury. Ann. Neurol., 2000, 48, 723-729.
    • (2000) Ann. Neurol , vol.48 , pp. 723-729
    • Sullivan, P.G.1    Geiger, J.D.2    Mattson, M.P.3    Scheff, S.W.4
  • 223
    • 33745685235 scopus 로고    scopus 로고
    • Creatine supplementation increases soleus muscle creatine content and lowers the insulinogenic index in an animal model of inherited type 2 diabetes
    • Op't Eijnde, B.; Jijakli, H.; Hespel, P.; Malaisse, W.J. Creatine supplementation increases soleus muscle creatine content and lowers the insulinogenic index in an animal model of inherited type 2 diabetes. Int. J. Mol. Med., 2006, 17, 1077-1084.
    • (2006) Int. J. Mol. Med , vol.17 , pp. 1077-1084
    • Op't Eijnde, B.1    Jijakli, H.2    Hespel, P.3    Malaisse, W.J.4
  • 225
    • 55849122639 scopus 로고    scopus 로고
    • Mitochondrial biology and oxidative stress in Parkinson disease pathogenesis
    • Henchcliffe, C.; Beal, M.F. Mitochondrial biology and oxidative stress in Parkinson disease pathogenesis. Nat. Clin. Pract. Neurol., 2008, 4, 600-609.
    • (2008) Nat. Clin. Pract. Neurol , vol.4 , pp. 600-609
    • Henchcliffe, C.1    Beal, M.F.2
  • 227
    • 41349108666 scopus 로고    scopus 로고
    • Long-term creatine supplementation is safe in aged patients with Parkinson disease
    • Bender, A.; Samtleben, W.; Elstner, M.; Klopstock, T. Long-term creatine supplementation is safe in aged patients with Parkinson disease. Nutr. Res., 2008, 28, 172-178.
    • (2008) Nutr. Res , vol.28 , pp. 172-178
    • Bender, A.1    Samtleben, W.2    Elstner, M.3    Klopstock, T.4
  • 228
    • 44649153832 scopus 로고    scopus 로고
    • A pilot clinical trial of creatine and minocycline in early Parkinson disease: 18-month results
    • NINDS NET-PD Investigators
    • NINDS NET-PD Investigators. A pilot clinical trial of creatine and minocycline in early Parkinson disease: 18-month results. Clin. Neuropharmacol., 2008, 31, 141-150.
    • (2008) Clin. Neuropharmacol , vol.31 , pp. 141-150
  • 229
    • 57649187103 scopus 로고    scopus 로고
    • Mitochondria and Huntington's disease pathogenesis: Insight from genetic and chemical models
    • Browne, S.E. Mitochondria and Huntington's disease pathogenesis: insight from genetic and chemical models. Ann. NY Acad. Sci., 2008, 1147, 358-382.
    • (2008) Ann. NY Acad. Sci , vol.1147 , pp. 358-382
    • Browne, S.E.1
  • 232
    • 48349092132 scopus 로고    scopus 로고
    • Gordon, P.H.; Cheung, Y.K.; Levin, B.; Andrews, H.; Doorish, C.; Macarthur, R.B.; Montes, J.; Bednarz, K.; Florence, J.; Rowin, J.; Boylan, K.; Mozaffar, T.; Tandan, R.; Mitsumoto, H.; Kelvin, E.A.; Chapin, J.; Bedlack, R.; Rivner, M.; McCluskey, L.F.; Pestronk, A.; Graves, M.; Sorenson, E.J.; Barohn, R.J.; Belsh, J.M.; Lou, J.S.; Levine, T.; Saperstein, D.; Miller, R.G.; Scelsa, S.N. Combination Drug Selection Trial Study Group. A novel, efficient, randomized selection trial comparing combinations of drug therapy for ALS. Amyotroph. Lateral Scler., 2008, 9, 212-222.
    • Gordon, P.H.; Cheung, Y.K.; Levin, B.; Andrews, H.; Doorish, C.; Macarthur, R.B.; Montes, J.; Bednarz, K.; Florence, J.; Rowin, J.; Boylan, K.; Mozaffar, T.; Tandan, R.; Mitsumoto, H.; Kelvin, E.A.; Chapin, J.; Bedlack, R.; Rivner, M.; McCluskey, L.F.; Pestronk, A.; Graves, M.; Sorenson, E.J.; Barohn, R.J.; Belsh, J.M.; Lou, J.S.; Levine, T.; Saperstein, D.; Miller, R.G.; Scelsa, S.N. Combination Drug Selection Trial Study Group. A novel, efficient, randomized selection trial comparing combinations of drug therapy for ALS. Amyotroph. Lateral Scler., 2008, 9, 212-222.
  • 237
    • 48449104125 scopus 로고    scopus 로고
    • A combination of nutriments improves mitochondrial biogenesis and function in skeletal muscle of type 2 diabetic Goto-Kakizaki rats
    • Shen, W.; Hao, J.; Tian, C.; Ren, J.; Yang, L.; Li, X.; Luo, C.; Cotma, C.W.; Liu, J. A combination of nutriments improves mitochondrial biogenesis and function in skeletal muscle of type 2 diabetic Goto-Kakizaki rats. PLoS ONE, 2008, 3, e2328.
    • (2008) PLoS ONE , vol.3
    • Shen, W.1    Hao, J.2    Tian, C.3    Ren, J.4    Yang, L.5    Li, X.6    Luo, C.7    Cotma, C.W.8    Liu, J.9
  • 238
    • 42149171377 scopus 로고    scopus 로고
    • The antioxidant alpha-lipoic acid improves endothelial dysfunction induced by acute hyperglycaemia during OGTT in impaired glucose tolerance
    • Xiang, G.D.; Sun, H.L.; Zhao, L.S.; Hou, J.; Yue, L.; Xu, L. The antioxidant alpha-lipoic acid improves endothelial dysfunction induced by acute hyperglycaemia during OGTT in impaired glucose tolerance. Clin. Endocrinol. (Oxf), 2008, 68, 716-723.
    • (2008) Clin. Endocrinol. (Oxf) , vol.68 , pp. 716-723
    • Xiang, G.D.1    Sun, H.L.2    Zhao, L.S.3    Hou, J.4    Yue, L.5    Xu, L.6
  • 240
    • 38449099641 scopus 로고    scopus 로고
    • Alpha-lipoic acid as a new treatment option for Alzheimer's disease - a 48 months follow-up analysis
    • Hager, K.; Kenklies, M.; McAfoose, J.; Engel, J., Münch, G. Alpha-lipoic acid as a new treatment option for Alzheimer's disease - a 48 months follow-up analysis. J. Neural Transm. Suppl., 2007, 72, 189-193.
    • (2007) J. Neural Transm. Suppl , vol.72 , pp. 189-193
    • Hager, K.1    Kenklies, M.2    McAfoose, J.3    Engel, J.4    Münch, G.5
  • 241
    • 34848890388 scopus 로고    scopus 로고
    • Lipoic acid and N-acetyl cysteine decrease mitochondrial-related oxidative stress in Alzheimer disease patient fibroblasts
    • Moreira, P.I.; Harris, P.L.R.; Zhu, X.; Santos, M.S.; Oliveira, C.R.; Smith, M.A.; Perry, G. Lipoic acid and N-acetyl cysteine decrease mitochondrial-related oxidative stress in Alzheimer disease patient fibroblasts. J. Alzheimer Dis., 2007, 12, 195-206.
    • (2007) J. Alzheimer Dis , vol.12 , pp. 195-206
    • Moreira, P.I.1    Harris, P.L.R.2    Zhu, X.3    Santos, M.S.4    Oliveira, C.R.5    Smith, M.A.6    Perry, G.7
  • 242
    • 1042290476 scopus 로고    scopus 로고
    • (R)-alpha-lipoic acid reverses the age-related loss in GSH redox status in post-mitotic tissues: Evidence for increased cysteine requirement for GSH synthesis
    • Suh, J.H.; Wang, H.; Liu, R.M.; Liu, J.; Hagen, T.M. (R)-alpha-lipoic acid reverses the age-related loss in GSH redox status in post-mitotic tissues: evidence for increased cysteine requirement for GSH synthesis. Arch. Biochem. Biophys., 2004, 423, 126-135.
    • (2004) Arch. Biochem. Biophys , vol.423 , pp. 126-135
    • Suh, J.H.1    Wang, H.2    Liu, R.M.3    Liu, J.4    Hagen, T.M.5
  • 243
    • 0035968856 scopus 로고    scopus 로고
    • Lipoic acid improves survival in transgenic mouse models of Huntington's disease
    • Andreassen, O.A.; Ferrante, R.J.; Dedeoglu, A.; Beal, M.F. Lipoic acid improves survival in transgenic mouse models of Huntington's disease. Neuroreport, 2001, 12, 3371-3373.
    • (2001) Neuroreport , vol.12 , pp. 3371-3373
    • Andreassen, O.A.1    Ferrante, R.J.2    Dedeoglu, A.3    Beal, M.F.4
  • 247
    • 58649103550 scopus 로고    scopus 로고
    • Dietary supplementation with a combination of alpha-lipoic acid, acetyl-L-carnitine, glycerophosphocoline, docosahexaenoic acid, and phosphatidylserine reduces oxidative damage to murine brain and improves cognitive performance
    • Suchy, J.; Chan, A.; Shea, T.B. Dietary supplementation with a combination of alpha-lipoic acid, acetyl-L-carnitine, glycerophosphocoline, docosahexaenoic acid, and phosphatidylserine reduces oxidative damage to murine brain and improves cognitive performance. Nutr. Res., 2009, 29, 70-74.
    • (2009) Nutr. Res , vol.29 , pp. 70-74
    • Suchy, J.1    Chan, A.2    Shea, T.B.3
  • 248
    • 36248976538 scopus 로고    scopus 로고
    • Effects of dietary supplementation with N-acetyl cysteine, acetyl-L-carnitine and S-adenosyl methionine on cognitive performance and aggression in normal mice and mice expressing human ApoE4
    • Chan, A.; Shea, T.B. Effects of dietary supplementation with N-acetyl cysteine, acetyl-L-carnitine and S-adenosyl methionine on cognitive performance and aggression in normal mice and mice expressing human ApoE4. Neuromol. Med., 2007, 9, 64-69.
    • (2007) Neuromol. Med , vol.9 , pp. 64-69
    • Chan, A.1    Shea, T.B.2
  • 249
    • 58149191631 scopus 로고    scopus 로고
    • Efficacy of a vitamin/nutriceutical formulation for early-stage Alzheimer's disease: A 1-year, open-label pilot study with an 16-month caregiver extension
    • Chan, A.; Paskavitz, J.; Remington, R.; Rasmussen, S.; Shea, T.B. Efficacy of a vitamin/nutriceutical formulation for early-stage Alzheimer's disease: a 1-year, open-label pilot study with an 16-month caregiver extension. Am. J. Alzheimers Dis. Other Dement., 2009, 23, 571-85.
    • (2009) Am. J. Alzheimers Dis. Other Dement , vol.23 , pp. 571-585
    • Chan, A.1    Paskavitz, J.2    Remington, R.3    Rasmussen, S.4    Shea, T.B.5
  • 250
    • 63349096757 scopus 로고    scopus 로고
    • Efficacy of a vitamin/nutriceutical formulation for moderate-stage to later-stage Alzheimer's disease: A placebo-controlled pilot study
    • Remington, R.; Chan, A.; Paskavitz, J.; Shea, T.B. Efficacy of a vitamin/nutriceutical formulation for moderate-stage to later-stage Alzheimer's disease: a placebo-controlled pilot study. Am. J. Alzheimers Dis. Other Dement., 2009, 24, 27-33.
    • (2009) Am. J. Alzheimers Dis. Other Dement , vol.24 , pp. 27-33
    • Remington, R.1    Chan, A.2    Paskavitz, J.3    Shea, T.B.4
  • 251
    • 0038681645 scopus 로고    scopus 로고
    • Effects of acetyl-Lcarnitine in Alzheimer's disease patients unresponsive to acetylcholinesterase inhibitors
    • Bianchetti, A.; Rozzini, R.; Trabucchi, M. Effects of acetyl-Lcarnitine in Alzheimer's disease patients unresponsive to acetylcholinesterase inhibitors. Curr. Med. Res. Opin., 2003, 19, 350-353.
    • (2003) Curr. Med. Res. Opin , vol.19 , pp. 350-353
    • Bianchetti, A.1    Rozzini, R.2    Trabucchi, M.3
  • 252
    • 0037347231 scopus 로고    scopus 로고
    • Meta-analysis of double blind randomized controlled clinical trials of acetyl-L-carnitine versus placebo in the treatment of mild cognitive impairment and mild Alzheimer's disease
    • Montgomery, S.A.; Thal, L.J.; Amrein, R. Meta-analysis of double blind randomized controlled clinical trials of acetyl-L-carnitine versus placebo in the treatment of mild cognitive impairment and mild Alzheimer's disease. Int. Clin. Psychopharmacol., 2003, 18, 61-71.
    • (2003) Int. Clin. Psychopharmacol , vol.18 , pp. 61-71
    • Montgomery, S.A.1    Thal, L.J.2    Amrein, R.3
  • 254
    • 42949122109 scopus 로고    scopus 로고
    • Coenzyme Q10 attenuates beta-amyloid pathology in the aged transgenic mice with Alzheimer presenilin 1 mutation
    • Yang, X.; Yang, Y.; Li, G.; Wang, J.; Yang, E.S. Coenzyme Q10 attenuates beta-amyloid pathology in the aged transgenic mice with Alzheimer presenilin 1 mutation. J. Mol. Neurosci., 2008, 34, 165-171.
    • (2008) J. Mol. Neurosci , vol.34 , pp. 165-171
    • Yang, X.1    Yang, Y.2    Li, G.3    Wang, J.4    Yang, E.S.5
  • 255
    • 38349117774 scopus 로고    scopus 로고
    • Supplementation of coenzyme Q10 and alpha-tocopherol lowers glycated hemoglobin level and lipid peroxidation in pancreas of diabetic rats
    • Sena, C,M.; Nunes, E.; Gomes, A.; Santos, M.S.; Proença, T.; Martins, M.I.; Seiça, R.M. Supplementation of coenzyme Q10 and alpha-tocopherol lowers glycated hemoglobin level and lipid peroxidation in pancreas of diabetic rats. Nutr. Res., 2008, 28, 113-121.
    • (2008) Nutr. Res , vol.28 , pp. 113-121
    • Sena, C.M.1    Nunes, E.2    Gomes, A.3    Santos, M.S.4    Proença, T.5    Martins, M.I.6    Seiça, R.M.7
  • 257
    • 29944435940 scopus 로고    scopus 로고
    • Effect of coenzyme Q10 on catalase activity and other antioxidant parameters in streptozotocin-induced diabetic rats
    • Modi, K.; Santani, D.D.; Goyal, R.K.; Bhatt, P.A. Effect of coenzyme Q10 on catalase activity and other antioxidant parameters in streptozotocin-induced diabetic rats. Biol. Trace Elem. Res., 2006, 109, 25-34.
    • (2006) Biol. Trace Elem. Res , vol.109 , pp. 25-34
    • Modi, K.1    Santani, D.D.2    Goyal, R.K.3    Bhatt, P.A.4
  • 258
    • 0343986284 scopus 로고    scopus 로고
    • Drug delivery to mitochondria: The key to mitochondrial medicine
    • Murphy, M.P.; Smith, R.A. Drug delivery to mitochondria: the key to mitochondrial medicine. Adv. Drug Deliv. Rev., 2000, 41, 235-250.
    • (2000) Adv. Drug Deliv. Rev , vol.41 , pp. 235-250
    • Murphy, M.P.1    Smith, R.A.2
  • 261
    • 0348136710 scopus 로고    scopus 로고
    • Mitochondria targeted antioxidants protect Friedreich Ataxia fibroblasts from endogenous oxidative stress more effectively than untargeted antioxidants
    • Jauslin, M.L.; Meier, T.; Smith, R.A.; Murphy, M.P. Mitochondria targeted antioxidants protect Friedreich Ataxia fibroblasts from endogenous oxidative stress more effectively than untargeted antioxidants. FASEB J., 2003, 17, 1972-1974.
    • (2003) FASEB J , vol.17 , pp. 1972-1974
    • Jauslin, M.L.1    Meier, T.2    Smith, R.A.3    Murphy, M.P.4
  • 262
    • 23644441470 scopus 로고    scopus 로고
    • Mitochondrially targeted vitamin E and vitamin E mitigate ethanol-mediated effects on cerebellar granule cell antioxidant defense systems
    • Siler-Marsiglio, K.I.; Pan, Q.; Paiva, M.; Madorsky, I.; Khurana, N.C.; Heaton, M.B. Mitochondrially targeted vitamin E and vitamin E mitigate ethanol-mediated effects on cerebellar granule cell antioxidant defense systems. Brain Res., 2005, 1052, 202-211.
    • (2005) Brain Res , vol.1052 , pp. 202-211
    • Siler-Marsiglio, K.I.1    Pan, Q.2    Paiva, M.3    Madorsky, I.4    Khurana, N.C.5    Heaton, M.B.6
  • 263
    • 0026580678 scopus 로고
    • The mode of action of lipid-soluble antioxidants in biological membranes: Relationship between the effects of ubiquinol and vitamin E as inhibitors of lipid peroxidation in submitochondrial particles
    • Ernster, L.; Forsmark, P.; Nordenbrand, K. The mode of action of lipid-soluble antioxidants in biological membranes: relationship between the effects of ubiquinol and vitamin E as inhibitors of lipid peroxidation in submitochondrial particles. Biofactors, 1992, 3, 241-248.
    • (1992) Biofactors , vol.3 , pp. 241-248
    • Ernster, L.1    Forsmark, P.2    Nordenbrand, K.3
  • 265
    • 0037593888 scopus 로고    scopus 로고
    • Redox regulation of cAMPresponsive element-binding protein and induction of manganous superoxide dismutase in nerve growth factor-dependent cell survival
    • Bedogni, B.; Pani, G.; Colavitti, R.; Riccio, A.; Borrello, S.; Murphy, M.; Smith, R.; Eboli, M.L.; Galeotti, T. Redox regulation of cAMPresponsive element-binding protein and induction of manganous superoxide dismutase in nerve growth factor-dependent cell survival. J. Biol. Chem., 2003, 278, 16510-16519.
    • (2003) J. Biol. Chem , vol.278 , pp. 16510-16519
    • Bedogni, B.1    Pani, G.2    Colavitti, R.3    Riccio, A.4    Borrello, S.5    Murphy, M.6    Smith, R.7    Eboli, M.L.8    Galeotti, T.9
  • 266
    • 4444315545 scopus 로고    scopus 로고
    • Supplementation of endothelial cells with mitochondria-targeted antioxidants inhibit peroxide-induced mitochondrial iron uptake, oxidative damage, and apoptosis
    • Dhanasekaran, A.; Kotamraju, S.; Kalivendi, S.V.; Matsunaga, T.; Shang, T.; Keszler, A.; Joseph, J.; Kalyanaramank B. Supplementation of endothelial cells with mitochondria-targeted antioxidants inhibit peroxide-induced mitochondrial iron uptake, oxidative damage, and apoptosis. J. Biol. Chem., 2004, 279, 37575-37587.
    • (2004) J. Biol. Chem , vol.279 , pp. 37575-37587
    • Dhanasekaran, A.1    Kotamraju, S.2    Kalivendi, S.V.3    Matsunaga, T.4    Shang, T.5    Keszler, A.6    Joseph, J.7    Kalyanaramank, B.8
  • 267
    • 38349010994 scopus 로고    scopus 로고
    • Is antioxidant potential of the mitochondrial targeted ubiquinone derivative MitoQ conserved in cells lacking mtDNA?
    • Lu, C.; Zhang, D.; Whiteman, M.; Armstrong, J.S. Is antioxidant potential of the mitochondrial targeted ubiquinone derivative MitoQ conserved in cells lacking mtDNA? Antioxid. Redox Signal., 2008, 10, 651-660.
    • (2008) Antioxid. Redox Signal , vol.10 , pp. 651-660
    • Lu, C.1    Zhang, D.2    Whiteman, M.3    Armstrong, J.S.4
  • 268
    • 33646349444 scopus 로고    scopus 로고
    • Mitochondrial oxidative damage in aging and Alzheimer's disease: Implications for mitochondrially targeted antioxidant therapeutics
    • Reddy, P.H. Mitochondrial oxidative damage in aging and Alzheimer's disease: implications for mitochondrially targeted antioxidant therapeutics. J. Biomed. Biotechnol., 2006, 3, 31372.
    • (2006) J. Biomed. Biotechnol , vol.3 , pp. 31372
    • Reddy, P.H.1
  • 269
    • 33748201552 scopus 로고    scopus 로고
    • Mitochondria-targeted peptide antioxidants: Novel neuroprotective agents
    • Szeto, H.H. Mitochondria-targeted peptide antioxidants: novel neuroprotective agents. AAPS J., 2006, 8, E521-E531.
    • (2006) AAPS J , vol.8
    • Szeto, H.H.1
  • 270
    • 0037215549 scopus 로고    scopus 로고
    • Transcellular transport of a highly polar 3+ net charge opioid tetrapeptide
    • Zhao, K.; Luo, G.; Zhao, G.M.; Schiller, P.W.; Szeto, H.H. Transcellular transport of a highly polar 3+ net charge opioid tetrapeptide. J. Pharmacol. Exp. Ther., 2003, 304, 425-432.
    • (2003) J. Pharmacol. Exp. Ther , vol.304 , pp. 425-432
    • Zhao, K.1    Luo, G.2    Zhao, G.M.3    Schiller, P.W.4    Szeto, H.H.5
  • 271
    • 4544370680 scopus 로고    scopus 로고
    • Cell-permeable peptide antioxidants targeted to inner mitochondrial membrane inhibit mitochondrial swelling, oxidative cell death, and reperfusion injury
    • Zhao, K.; Zhao, G.M.; Wu, D.; Soong, Y.; Birk, A.V.; Schiller, P.W.; Szeto, H.H. Cell-permeable peptide antioxidants targeted to inner mitochondrial membrane inhibit mitochondrial swelling, oxidative cell death, and reperfusion injury. J. Biol. Chem., 2004, 279, 34682-34690.
    • (2004) J. Biol. Chem , vol.279 , pp. 34682-34690
    • Zhao, K.1    Zhao, G.M.2    Wu, D.3    Soong, Y.4    Birk, A.V.5    Schiller, P.W.6    Szeto, H.H.7
  • 272
    • 38349010993 scopus 로고    scopus 로고
    • Mitochondria-targeted cytoprotective peptides for ischemia-reperfusion injury
    • Szeto, H.H. Mitochondria-targeted cytoprotective peptides for ischemia-reperfusion injury. Antioxid. Redox Signal., 2008, 10, 601-619.
    • (2008) Antioxid. Redox Signal , vol.10 , pp. 601-619
    • Szeto, H.H.1
  • 273
    • 27744516094 scopus 로고    scopus 로고
    • Mitochondria-targeted peptide prevents mitochondrial depolarization and apoptosis induced by tert-butyl hydroperoxide in neuronal cell lines
    • Zhao; K.; Luo, G.; Giannelli, S.; Szeto, H.H. Mitochondria-targeted peptide prevents mitochondrial depolarization and apoptosis induced by tert-butyl hydroperoxide in neuronal cell lines. Biochem. Pharmacol., 2005, 70, 1796-1806.
    • (2005) Biochem. Pharmacol , vol.70 , pp. 1796-1806
    • Zhao, K.1    Luo, G.2    Giannelli, S.3    Szeto, H.H.4
  • 274
    • 33746397617 scopus 로고    scopus 로고
    • Cell-permeable peptide antioxidants as a novel therapeutic approach in a mouse model of amyotrophic lateral sclerosis
    • Petri, S.; Kiaei, M.; Damiano, M.; Hiller, A.; Wille, E.; Manfredi, G.; Calingasan, N.Y.; Szeto, H.H.; Beal, M.F. Cell-permeable peptide antioxidants as a novel therapeutic approach in a mouse model of amyotrophic lateral sclerosis. J. Neurochem., 2006, 98, 1141-1148.
    • (2006) J. Neurochem , vol.98 , pp. 1141-1148
    • Petri, S.1    Kiaei, M.2    Damiano, M.3    Hiller, A.4    Wille, E.5    Manfredi, G.6    Calingasan, N.Y.7    Szeto, H.H.8    Beal, M.F.9
  • 275
    • 68949213947 scopus 로고    scopus 로고
    • Mitochondria targeted peptides protect against 1-methyl-4-phenyl-1,2,3,6- tetrahydropyridine neurotoxicity
    • Epub ahead of print
    • Yang, L.; Zhao, K.; Calingasan, N.Y.; Luo, G.; Szeto, H.H.; Beal, F. Mitochondria targeted peptides protect against 1-methyl-4-phenyl-1,2,3,6- tetrahydropyridine neurotoxicity. Antioxid. Redox Signal., 2009, [Epub ahead of print].
    • (2009) Antioxid. Redox Signal
    • Yang, L.1    Zhao, K.2    Calingasan, N.Y.3    Luo, G.4    Szeto, H.H.5    Beal, F.6
  • 276
    • 33845979877 scopus 로고    scopus 로고
    • Mitochondrial targeting with antioxidant peptide SS-31 prevents mitochondrial depolarization, reduces islet cell apoptosis, increases islet cell yield, and improves post-transplantation function
    • Thomas, D.A.; Stauffer, C.; Zhao, K.; Yang, H.; Sharma, V.K.; Szeto, H.H.; Suthanthiran, M. Mitochondrial targeting with antioxidant peptide SS-31 prevents mitochondrial depolarization, reduces islet cell apoptosis, increases islet cell yield, and improves post-transplantation function. J. Am. Soc. Nephrol., 2007, 18, 213-222.
    • (2007) J. Am. Soc. Nephrol , vol.18 , pp. 213-222
    • Thomas, D.A.1    Stauffer, C.2    Zhao, K.3    Yang, H.4    Sharma, V.K.5    Szeto, H.H.6    Suthanthiran, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.