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Volumn 2015, Issue , 2015, Pages

Diabetes and alzheimer disease, two overlapping pathologies with the same background: Oxidative stress

Author keywords

[No Author keywords available]

Indexed keywords

INSULIN; OXIDATIVE STRESS; PATHOLOGY;

EID: 84924565894     PISSN: 19420900     EISSN: 19420994     Source Type: Journal    
DOI: 10.1155/2015/985845     Document Type: Review
Times cited : (103)

References (272)
  • 1
    • 84924625656 scopus 로고    scopus 로고
    • Diabetes, fact sheet no. 312
    • World Health Organization, Ed. World Health Organization
    • World Health Organization, "Diabetes, fact sheet no. 312," in WHO Media Centre, Fact Sheets, World Health Organization, Ed., vol. 2014, World Health Organization, 2014.
    • (2014) WHO Media Centre, Fact Sheets , vol.2014
  • 2
    • 77952771512 scopus 로고    scopus 로고
    • Alzheimer's disease international world Alzheimer report 2014. Dementia and risk reduction
    • Alzheimer's Disease International, Ed. Alzheimer's Disease International, London, UK
    • M. Prince, E. Albanese, M. Guerchet, and M. Prina, "Alzheimer's disease international world Alzheimer report 2014. Dementia and risk reduction," in Alzheimer's Disease International World Alzheimer, Alzheimer's Disease International, Ed., p. 104, Alzheimer's Disease International, London, UK, 2014.
    • (2014) Alzheimer's Disease International World Alzheimer , pp. 104
    • Prince, M.1    Albanese, E.2    Guerchet, M.3    Prina, M.4
  • 3
    • 84899414414 scopus 로고    scopus 로고
    • Diabetes mellitus and the risk of Alzheimer's disease: A nationwide population-based study
    • C. C. Huang, C. M. Chung, H. B. Leu et al., "Diabetes mellitus and the risk of Alzheimer's disease: a nationwide population-based study," PLoS ONE, vol. 9, no. 1, Article ID e87095, 2014.
    • (2014) PLoS ONE , vol.9 , Issue.1
    • Huang, C.C.1    Chung, C.M.2    Leu, H.B.3
  • 4
    • 15244351255 scopus 로고    scopus 로고
    • Impaired insulin and insulin-like growth factor expression and signaling mechanisms in Alzheimer's disease-is this type 3 diabetes?
    • E. Steen, B. M. Terry, E. J. Rivera et al., "Impaired insulin and insulin-like growth factor expression and signaling mechanisms in Alzheimer's disease-is this type 3 diabetes?" Journal of Alzheimer's Disease, vol. 7, no. 1, pp. 63-80, 2005.
    • (2005) Journal of Alzheimer's Disease , vol.7 , Issue.1 , pp. 63-80
    • Steen, E.1    Terry, B.M.2    Rivera, E.J.3
  • 7
    • 2442421194 scopus 로고    scopus 로고
    • Is oxidative stress the pathogenic mechanism underlying insulin resistance, diabetes, and cardiovascular disease? The common soil hypothesis revisited
    • A. Ceriello and E. Motz, "Is oxidative stress the pathogenic mechanism underlying insulin resistance, diabetes, and cardiovascular disease? The common soil hypothesis revisited," Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 24, no. 5, pp. 816-823, 2004.
    • (2004) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.24 , Issue.5 , pp. 816-823
    • Ceriello, A.1    Motz, E.2
  • 8
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • M. Brownlee, "Biochemistry and molecular cell biology of diabetic complications," Nature, vol. 414, no. 6865, pp. 813-820, 2001.
    • (2001) Nature , vol.414 , Issue.6865 , pp. 813-820
    • Brownlee, M.1
  • 10
    • 0023913225 scopus 로고
    • The involvement of aldose reductase in diabetic complications
    • J. H. Kinoshita and C. Nishimura, "The involvement of aldose reductase in diabetic complications," Diabetes/Metabolism Reviews, vol. 4, no. 4, pp. 323-337, 1988.
    • (1988) Diabetes/Metabolism Reviews , vol.4 , Issue.4 , pp. 323-337
    • Kinoshita, J.H.1    Nishimura, C.2
  • 11
    • 56649112649 scopus 로고    scopus 로고
    • Hyperglycemia not hypoglycemia alters neuronal dendrites and impairs spatial memory
    • J. I. Malone, S. Hanna, S. Saporta et al., "Hyperglycemia not hypoglycemia alters neuronal dendrites and impairs spatial memory," Pediatric Diabetes, vol. 9, no. 6, pp. 531-539, 2008.
    • (2008) Pediatric Diabetes , vol.9 , Issue.6 , pp. 531-539
    • Malone, J.I.1    Hanna, S.2    Saporta, S.3
  • 14
    • 0037305028 scopus 로고    scopus 로고
    • Alzheimer's disease and total plasma aminothiols
    • A. McCaddon, P. Hudson, D. Hill et al., "Alzheimer's disease and total plasma aminothiols," Biological Psychiatry, vol. 53, no. 3, pp. 254-260, 2003.
    • (2003) Biological Psychiatry , vol.53 , Issue.3 , pp. 254-260
    • McCaddon, A.1    Hudson, P.2    Hill, D.3
  • 15
    • 84901911564 scopus 로고    scopus 로고
    • The emerging role of glutathione in Alzheimer's disease
    • S. Saharan and P. K. Mandai, "The emerging role of glutathione in Alzheimer's disease," Journal of Alzheimer's Disease, vol. 40, pp. 519-529, 2014.
    • (2014) Journal of Alzheimer's Disease , vol.40 , pp. 519-529
    • Saharan, S.1    Mandai, P.K.2
  • 16
    • 48249094537 scopus 로고    scopus 로고
    • Reducing oxidative stress in patients with type 2 diabetes mellitus: A primary care call to action
    • J. Unger, "Reducing oxidative stress in patients with type 2 diabetes mellitus: a primary care call to action," Insulin, vol. 3, no. 3, pp. 176-184, 2008.
    • (2008) Insulin , vol.3 , Issue.3 , pp. 176-184
    • Unger, J.1
  • 18
    • 79951696287 scopus 로고    scopus 로고
    • Glutathione synthesis is diminished in patients with uncontrolled diabetes and restored by dietary supplementation with cysteine and glycine
    • R. V. Sekhar, S. V. Mckay, S. G Patel et al, "Glutathione synthesis is diminished in patients with uncontrolled diabetes and restored by dietary supplementation with cysteine and glycine," Diabetes Care, vol. 34, no. 1, pp. 162-167, 2011.
    • (2011) Diabetes Care , vol.34 , Issue.1 , pp. 162-167
    • Sekhar, R.V.1    Mckay, S.V.2    Patel, S.G.3
  • 20
    • 35148870841 scopus 로고    scopus 로고
    • Paradoxical upregulation of glutamatergic presynaptic boutons during mild cognitive impairment
    • K. F. S. Bell, D. A. Bennett, and A. C. Cuello, "Paradoxical upregulation of glutamatergic presynaptic boutons during mild cognitive impairment," The Journal of Neuroscience, vol. 27, no. 40, pp. 10810-10817, 2007
    • (2007) The Journal of Neuroscience , vol.27 , Issue.40 , pp. 10810-10817
    • Bell, K.F.S.1    Bennett, D.A.2    Cuello, A.C.3
  • 21
    • 84856718797 scopus 로고    scopus 로고
    • Alzheimer's disease: Pathological mechanisms and the beneficial role of melatonin
    • S. A. Rosales-Corral, D. Acuna-Castroviejo, A. Coto-Montes et al., "Alzheimer's disease: pathological mechanisms and the beneficial role of melatonin," Journal of Pineal Research, vol. 52, no. 2, pp. 167-202, 2012.
    • (2012) Journal of Pineal Research , vol.52 , Issue.2 , pp. 167-202
    • Rosales-Corral, S.A.1    Acuna-Castroviejo, D.2    Coto-Montes, A.3
  • 22
    • 34248174912 scopus 로고    scopus 로고
    • System xc- and glutamate transporter inhibition mediates microglial toxicity to oligodendrocytes
    • M. Domercq, M. V. Sanchez-Gomez, C. Sherwin, E. Etxebarria, R. Fern, and C. Matute, "System xc- and glutamate transporter inhibition mediates microglial toxicity to oligodendrocytes," The Journal of Immunology, vol. 178, no. 10, pp. 6549-6556, 2007.
    • (2007) The Journal of Immunology , vol.178 , Issue.10 , pp. 6549-6556
    • Domercq, M.1    Sanchez-Gomez, M.V.2    Sherwin, C.3    Etxebarria, E.4    Fern, R.5    Matute, C.6
  • 23
    • 79959596092 scopus 로고    scopus 로고
    • Fisetin lowers methylglyoxal dependent protein glycation and limits the complications of diabetes
    • P. Maher, R. Dargusch, J. L. Ehren, S. Okada, K. Sharma, and D. Schubert, "Fisetin lowers methylglyoxal dependent protein glycation and limits the complications of diabetes," PLoS ONE, vol. 6, no. 6, Article ID e21226, 2011.
    • (2011) PLoS ONE , vol.6 , Issue.6
    • Maher, P.1    Dargusch, R.2    Ehren, J.L.3    Okada, S.4    Sharma, K.5    Schubert, D.6
  • 24
    • 84867308972 scopus 로고    scopus 로고
    • Participation of antioxidant and cholinergic system in protective effect of naringenin against type-2 diabetes-induced memory dysfunction in rats
    • A. Rahigude, P. Bhutada, S. Kaulaskar, M. Aswar, and K. Otari, "Participation of antioxidant and cholinergic system in protective effect of naringenin against type-2 diabetes-induced memory dysfunction in rats," Neuroscience, vol. 226, pp. 62-72, 2012.
    • (2012) Neuroscience , vol.226 , pp. 62-72
    • Rahigude, A.1    Bhutada, P.2    Kaulaskar, S.3    Aswar, M.4    Otari, K.5
  • 25
    • 84858152480 scopus 로고    scopus 로고
    • Oxidative stress, glutathione status, sirtuin and cellular stress response in type 2 diabetes
    • V. Calabrese, C. Cornelius, V. Leso et al., "Oxidative stress, glutathione status, sirtuin and cellular stress response in type 2 diabetes," Biochimica et Biophysica Acta: Molecular Basis of Disease, vol. 1822, no. 5, pp. 729-736, 2012.
    • (2012) Biochimica et Biophysica Acta: Molecular Basis of Disease , vol.1822 , Issue.5 , pp. 729-736
    • Calabrese, V.1    Cornelius, C.2    Leso, V.3
  • 27
    • 26844519964 scopus 로고    scopus 로고
    • Diabetes causes inhibition of glucose-6-phosphate dehydrogenase via activation of PKA, which contributes to oxidative stress in rat kidney cortex
    • Y. Xu, B. W. Osborne, and R. C. Stanton, "Diabetes causes inhibition of glucose-6-phosphate dehydrogenase via activation of PKA, which contributes to oxidative stress in rat kidney cortex," The American Journal of Physiology-Renal Physiology, vol. 289, no. 5, pp. F1040-F1047, 2005.
    • (2005) The American Journal of Physiology-Renal Physiology , vol.289 , Issue.5 , pp. F1040-F1047
    • Xu, Y.1    Osborne, B.W.2    Stanton, R.C.3
  • 28
    • 0033198043 scopus 로고    scopus 로고
    • CAMP-dependent protein kinase phosphorylations on Tau in Alzheimer's disease
    • G. A. Jicha, C. Weaver, E. Lane et al., "cAMP-dependent protein kinase phosphorylations on Tau in Alzheimer's disease," The Journal of Neuroscience, vol. 19, no. 17, pp. 7486-7494, 1999.
    • (1999) The Journal of Neuroscience , vol.19 , Issue.17 , pp. 7486-7494
    • Jicha, G.A.1    Weaver, C.2    Lane, E.3
  • 29
    • 67849099654 scopus 로고    scopus 로고
    • Biphasic effects of forskolin on tau phosphorylation and spatial memory in rats
    • Q. Tian, J. X. Zhang, Y. Zhang et al., "Biphasic effects of forskolin on tau phosphorylation and spatial memory in rats," Journal of Alzheimer's Disease, vol. 17, no. 3, pp. 631-642, 2009.
    • (2009) Journal of Alzheimer's Disease , vol.17 , Issue.3 , pp. 631-642
    • Tian, Q.1    Zhang, J.X.2    Zhang, Y.3
  • 31
    • 84908376973 scopus 로고    scopus 로고
    • Homocysteine and cytosolic GSH depletion induce apoptosis and oxidative toxicity through cytosolic calcium overload in the hippocampus of aged mice: Involvement of TRPM2 and TRPV1 channels
    • I. S. Ovey and M. Naziroglu, "Homocysteine and cytosolic GSH depletion induce apoptosis and oxidative toxicity through cytosolic calcium overload in the hippocampus of aged mice: involvement of TRPM2 and TRPV1 channels," Neuroscience, vol. 284, pp. 225-233, 2015.
    • (2015) Neuroscience , vol.284 , pp. 225-233
    • Ovey, I.S.1    Naziroglu, M.2
  • 32
    • 44649198605 scopus 로고    scopus 로고
    • Insulin receptor signaling regulates synapse number, dendritic plasticity, and circuit function in vivo
    • S. L. Chiu, C. M. Chen, and H. T. Cline, "Insulin receptor signaling regulates synapse number, dendritic plasticity, and circuit function in vivo," Neuron, vol. 58, no. 5, pp. 708-719, 2008.
    • (2008) Neuron , vol.58 , Issue.5 , pp. 708-719
    • Chiu, S.L.1    Chen, C.M.2    Cline, H.T.3
  • 33
    • 7444232547 scopus 로고    scopus 로고
    • Glycation-induced inactivation of NADP(+)-dependent isocitrate dehydrogenase: Implications for diabetes and aging
    • I. S. Kil, J. H. Lee, A. H. Shin, and J. W. Park, "Glycation-induced inactivation of NADP(+)-dependent isocitrate dehydrogenase: Implications for diabetes and aging," Free Radical Biology and Medicine, vol. 37, no. 11, pp. 1765-1778, 2004.
    • (2004) Free Radical Biology and Medicine , vol.37 , Issue.11 , pp. 1765-1778
    • Kil, I.S.1    Lee, J.H.2    Shin, A.H.3    Park, J.W.4
  • 35
    • 1642377274 scopus 로고    scopus 로고
    • Impaired mitochondrial activity in the insulin-resistant offspring of patients with type 2 diabetes
    • K. E Petersen, S. Dufour, D. Befroy, R. Garcia, and G. I. Shulman, "Impaired mitochondrial activity in the insulin-resistant offspring of patients with type 2 diabetes," The New England Journal of Medicine, vol. 350, no. 7, pp. 664-671, 2004.
    • (2004) The New England Journal of Medicine , vol.350 , Issue.7 , pp. 664-671
    • Petersen, K.E.1    Dufour, S.2    Befroy, D.3    Garcia, R.4    Shulman, G.I.5
  • 36
    • 0030009314 scopus 로고    scopus 로고
    • BCL-2 expression or antioxidants prevent hyperglycemia-induced formation of intracellular advanced glycation endproducts in bovine endothelial cells
    • I. Giardino, D. Edelstein, and M. Brownlee, "BCL-2 expression or antioxidants prevent hyperglycemia-induced formation of intracellular advanced glycation endproducts in bovine endothelial cells," The Journal of Clinical Investigation, vol. 97, no. 6, pp. 1422-1428, 1996.
    • (1996) The Journal of Clinical Investigation , vol.97 , Issue.6 , pp. 1422-1428
    • Giardino, I.1    Edelstein, D.2    Brownlee, M.3
  • 37
    • 0034643340 scopus 로고    scopus 로고
    • Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage
    • T. Nishikawa, D. Edelstein, X L. Du et al., "Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage," Nature, vol. 404, no. 6779, pp. 787-790, 2000.
    • (2000) Nature , vol.404 , Issue.6779 , pp. 787-790
    • Nishikawa, T.1    Edelstein, D.2    Du, X.L.3
  • 38
    • 84863847452 scopus 로고    scopus 로고
    • Aldose reductase, oxidative stress, and diabetic mellitus
    • W. H. Tang, K. A. Martin, and J. Hwa, "Aldose reductase, oxidative stress, and diabetic mellitus," Frontiers in Pharmacology, vol. 3, article 87, 2012.
    • (2012) Frontiers in Pharmacology , vol.3
    • Tang, W.H.1    Martin, K.A.2    Hwa, J.3
  • 39
    • 0010435350 scopus 로고    scopus 로고
    • Postnatal development of malic enzyme isoforms in rat brain
    • A. Teelken and J. Korf, Eds. Springer, Boston, MA, USA
    • R. Vogel, H. Wiesinger, and B. Hamprecht, "Postnatal development of malic enzyme isoforms in rat brain," in Neurochemistry, A. Teelken and J. Korf, Eds., pp. 765-769, Springer, Boston, MA, USA, 1997
    • (1997) Neurochemistry , pp. 765-769
    • Vogel, R.1    Wiesinger, H.2    Hamprecht, B.3
  • 40
    • 0018829349 scopus 로고
    • Mitochondrial malic enzymes. An association between NAD(P)+-dependent malic enzyme and cell renewal in Sprague-Dawley rat tissues
    • W. O. Nagel, R. T. Dauchy, and L. A. Sauer, "Mitochondrial malic enzymes. An association between NAD(P)+-dependent malic enzyme and cell renewal in Sprague-Dawley rat tissues," The Journal of Biological Chemistry, vol. 255, no. 9, pp. 3849-3854, 1980.
    • (1980) The Journal of Biological Chemistry , vol.255 , Issue.9 , pp. 3849-3854
    • Nagel, W.O.1    Dauchy, R.T.2    Sauer, L.A.3
  • 41
    • 0027465673 scopus 로고
    • Purification of cytosolic malic enzyme from bovine brain, generation of monoclonal antibodies, and immunocytochemical localization of the enzyme in glial cells of neural primary cultures
    • G. M. Kurz, H. Wiesinger, and B. Hamprecht, "Purification of cytosolic malic enzyme from bovine brain, generation of monoclonal antibodies, and immunocytochemical localization of the enzyme in glial cells of neural primary cultures," Journal of Neurochemistry, vol. 60, no. 4, pp. 1467-1474, 1993.
    • (1993) Journal of Neurochemistry , vol.60 , Issue.4 , pp. 1467-1474
    • Kurz, G.M.1    Wiesinger, H.2    Hamprecht, B.3
  • 42
    • 0032524879 scopus 로고    scopus 로고
    • Malic enzyme isoforms in astrocytes: Comparative study on activities in rat brain tissue and astroglia-rich primary cultures
    • R. Vogel, B. Hamprecht, and H. Wiesinger, "Malic enzyme isoforms in astrocytes: comparative study on activities in rat brain tissue and astroglia-rich primary cultures," Neuroscience Letters, vol. 247, no. 2-3, pp. 123-126, 1998.
    • (1998) Neuroscience Letters , vol.247 , Issue.2-3 , pp. 123-126
    • Vogel, R.1    Hamprecht, B.2    Wiesinger, H.3
  • 43
    • 0016818582 scopus 로고
    • Enzymes of glucose metabolism and of the citrate cleavage pathway in adipose tissue of normal and diabetic subjects
    • F. Belfiore, A. M. Rabuazzo, E. Napoli, V. Borzi, and L. Lo Vecchio, "Enzymes of glucose metabolism and of the citrate cleavage pathway in adipose tissue of normal and diabetic subjects," Diabetes, vol. 24, no. 10, pp. 865-873, 1975.
    • (1975) Diabetes , vol.24 , Issue.10 , pp. 865-873
    • Belfiore, F.1    Rabuazzo, A.M.2    Napoli, E.3    Borzi, V.4    Lo Vecchio, L.5
  • 44
    • 0028860813 scopus 로고
    • Localization of thioredoxin in the rat brain and functional implications
    • A. Lippoldt, C. A. Padilla, H. Gerst et al., "Localization of thioredoxin in the rat brain and functional implications," The Journal of Neuroscience, vol. 15, no. 10, pp. 6747-6756, 1995.
    • (1995) The Journal of Neuroscience , vol.15 , Issue.10 , pp. 6747-6756
    • Lippoldt, A.1    Padilla, C.A.2    Gerst, H.3
  • 45
    • 84878786543 scopus 로고    scopus 로고
    • Oxidative modification of lipoic acid by HNE in alzheimer disease brain
    • S. S. Hardas, R. Sultana, A. M. Clark et al., "Oxidative modification of lipoic acid by HNE in alzheimer disease brain," Redox Biology, vol. 1, no. 1, pp. 80-85, 2013.
    • (2013) Redox Biology , vol.1 , Issue.1 , pp. 80-85
    • Hardas, S.S.1    Sultana, R.2    Clark, A.M.3
  • 46
    • 17744367054 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein is stimulated by glucose through a carbohydrate response element and induces beta-cell apoptosis
    • A. H. Minn, C. Hafele, and A. Shalev, "Thioredoxin-interacting protein is stimulated by glucose through a carbohydrate response element and induces beta-cell apoptosis," Endocrinology, vol. 146, no. 5, pp. 2397-2405, 2005.
    • (2005) Endocrinology , vol.146 , Issue.5 , pp. 2397-2405
    • Minn, A.H.1    Hafele, C.2    Shalev, A.3
  • 47
    • 42449110310 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein. A critical link between glucose toxicity and β-cell apoptosis
    • J. Chen, G Saxena, I. N. Mungrue, A. J. Lusis, and A. Shalev, "Thioredoxin-interacting protein. A critical link between glucose toxicity and β-cell apoptosis," Diabetes, vol. 57, no. 4, pp. 938-944, 2008.
    • (2008) Diabetes , vol.57 , Issue.4 , pp. 938-944
    • Chen, J.1    Saxena, G.2    Mungrue, I.N.3    Lusis, A.J.4    Shalev, A.5
  • 48
    • 84859504173 scopus 로고    scopus 로고
    • Induction of thioredoxin-interacting protein is mediated by oxidative stress, calcium, and glucose after brain injury in mice
    • G. S. Kim, J. E. Jung, P. Narasimhan, H. Sakata, and P. H. Chan, "Induction of thioredoxin-interacting protein is mediated by oxidative stress, calcium, and glucose after brain injury in mice," Neurobiology of Disease, vol. 46, no. 2, pp. 440-449, 2012.
    • (2012) Neurobiology of Disease , vol.46 , Issue.2 , pp. 440-449
    • Kim, G.S.1    Jung, J.E.2    Narasimhan, P.3    Sakata, H.4    Chan, P.H.5
  • 49
    • 84864682160 scopus 로고    scopus 로고
    • IREla induces thioredoxin-interacting protein to activate the NLRP3 inflammasome and promote programmed cell death under irremediable ER stress
    • A. G Lerner, J. P. Upton, P. V. K. Praveen et al., "IREla induces thioredoxin-interacting protein to activate the NLRP3 inflammasome and promote programmed cell death under irremediable ER stress," Cell Metabolism, vol. 16, no. 2, pp. 250-264, 2012.
    • (2012) Cell Metabolism , vol.16 , Issue.2 , pp. 250-264
    • Lerner, A.G.1    Upton, J.P.2    Praveen, P.V.K.3
  • 50
    • 33745297834 scopus 로고    scopus 로고
    • Glucose-dependent transcriptional regulation by an evolutionarily conserved glucose-sensing module
    • M. V. Li, B. Chang, M. Imamura, N. Poungvarin, and L. Chan, "Glucose-dependent transcriptional regulation by an evolutionarily conserved glucose-sensing module," Diabetes, vol. 55, no. 5, pp. 1179-1189, 2006.
    • (2006) Diabetes , vol.55 , Issue.5 , pp. 1179-1189
    • Li, M.V.1    Chang, B.2    Imamura, M.3    Poungvarin, N.4    Chan, L.5
  • 51
    • 77954078084 scopus 로고    scopus 로고
    • Tandem ChoRE and CCAAT motifs and associated factors regulate txnip expression in response to glucose or adenosine-containing molecules
    • F.-X Yu and Y Luo, "Tandem ChoRE and CCAAT motifs and associated factors regulate txnip expression in response to glucose or adenosine-containing molecules," PLoS ONE, vol. 4, no. 12, Article ID e8397, 2009.
    • (2009) PLoS ONE , vol.4 , Issue.12
    • Yu, F.-X.1    Luo, Y.2
  • 52
    • 84924608502 scopus 로고    scopus 로고
    • TXNIP, the major player in insulin resistance, is early over-expressed in the brain of the 5XFAD Alzheimer's mice model and is induced by Aβ in vitro: Emerging role of TXNIP and inflammation in Alzheimer's Disease progression
    • T. Gouget, M. Djelloul, J. Boucraut et al., "TXNIP, the major player in insulin resistance, is early over-expressed in the brain of the 5XFAD Alzheimer's mice model and is induced by Aβ in vitro: emerging role of TXNIP and inflammation in Alzheimer's Disease progression," Alzheimer's & Dementia, vol. 7, no. 4, p. S684, 2011.
    • (2011) Alzheimer's & Dementia , vol.7 , Issue.4 , pp. S684
    • Gouget, T.1    Djelloul, M.2    Boucraut, J.3
  • 53
    • 84907434718 scopus 로고    scopus 로고
    • The transcription factor X-box binding protein-1 in neurodegenerative diseases
    • J. Dunys, E. Duplan, and F. Checler, "The transcription factor X-box binding protein-1 in neurodegenerative diseases," Molecular Neurodegeneration, vol. 9, no. 1, article 35, 2014.
    • (2014) Molecular Neurodegeneration , vol.9 , Issue.1
    • Dunys, J.1    Duplan, E.2    Checler, F.3
  • 54
    • 84901022639 scopus 로고    scopus 로고
    • Reduced IRE1 mediates apoptotic cell death by disrupting calcium homeostasis via the InsP3 receptor
    • S. M. Son, J. Byun, S.-E. Roh, S. J. Kim, and I. Mook-Jung, "Reduced IRE1 mediates apoptotic cell death by disrupting calcium homeostasis via the InsP3 receptor," Cell Death and Disease, vol. 5, no. 4, Article ID e1188, 2014.
    • (2014) Cell Death and Disease , vol.5 , Issue.4
    • Son, S.M.1    Byun, J.2    Roh, S.-E.3    Kim, S.J.4    Mook-Jung, I.5
  • 55
    • 0035871641 scopus 로고    scopus 로고
    • Stimulation of beta-amyloid precursor protein trafficking by insulin reduces intra-neuronal beta-amyloid and requires mitogen-activated protein kinase signaling
    • L. Gasparini, G. K. Gouras, R. Wang et al., "Stimulation of beta-amyloid precursor protein trafficking by insulin reduces intra-neuronal beta-amyloid and requires mitogen-activated protein kinase signaling," The journal of Neuroscience, vol. 21, no. 8, pp. 2561-2570, 2001.
    • (2001) The Journal of Neuroscience , vol.21 , Issue.8 , pp. 2561-2570
    • Gasparini, L.1    Gouras, G.K.2    Wang, R.3
  • 56
    • 9144223132 scopus 로고    scopus 로고
    • Mechanisms of soluble beta-amyloid impairment of endothelial function
    • M. T. Gentile, C. Vecchione, A. Maffei et al., "Mechanisms of soluble beta-amyloid impairment of endothelial function," The journal of Biological Chemistry, vol. 279, no. 46, pp. 48135-48142, 2004.
    • (2004) The Journal of Biological Chemistry , vol.279 , Issue.46 , pp. 48135-48142
    • Gentile, M.T.1    Vecchione, C.2    Maffei, A.3
  • 57
    • 84903458925 scopus 로고    scopus 로고
    • The role of endoplasmic reticulum in amyloid precursor protein processing and trafficking: Implications for Alzheimer's disease
    • A. I. Placido, C. M. F. Pereira, A. I. Duarte et al, "The role of endoplasmic reticulum in amyloid precursor protein processing and trafficking: implications for Alzheimer's disease," Biochimica et Biophysica Acta, vol. 1842, no. 9, pp. 1444-1453, 2014.
    • (2014) Biochimica et Biophysica Acta , vol.1842 , Issue.9 , pp. 1444-1453
    • Placido, A.I.1    Pereira, C.M.F.2    Duarte, A.I.3
  • 58
    • 84871797522 scopus 로고    scopus 로고
    • 2+ is a danger signal activating the NLRP3 inflammasome through G protein-coupled calcium sensing receptors
    • 2+ is a danger signal activating the NLRP3 inflammasome through G protein-coupled calcium sensing receptors," Nature Communications, vol. 3, article 2339, 2012.
    • (2012) Nature Communications , vol.3
    • Rossol, M.1    Pierer, M.2    Rauhen, N.3
  • 59
    • 1842738222 scopus 로고    scopus 로고
    • Kinetics of the neuroin-flammation-oxidative stress correlation in rat brain following the injection of fibrillar amyloid-beta onto the hippocampus in vivo
    • S. Rosales-Corral, D. X Tan, R. J. Reiter, M. Valdivia-Velázquez, J. P. Acosta-Martínez, and G G. Ortiz, "Kinetics of the neuroin-flammation-oxidative stress correlation in rat brain following the injection of fibrillar amyloid-beta onto the hippocampus in vivo," journal of Neuroimmunology, vol. 150, no. 1-2, pp. 20-28, 2004.
    • (2004) Journal of Neuroimmunology , vol.150 , Issue.1-2 , pp. 20-28
    • Rosales-Corral, S.1    Tan, D.X.2    Reiter, R.J.3    Valdivia-Velázquez, M.4    Acosta-Martínez, J.P.5    Ortiz, G.G.6
  • 61
    • 84872014417 scopus 로고    scopus 로고
    • Nlrp3 inflammasome activation in type 2 diabetes: Is it clinically relevant?
    • V. D. Dixit, "Nlrp3 inflammasome activation in type 2 diabetes: is it clinically relevant?" Diabetes, vol. 62, no. 1, pp. 22-24, 2013.
    • (2013) Diabetes , vol.62 , Issue.1 , pp. 22-24
    • Dixit, V.D.1
  • 62
    • 79751512463 scopus 로고    scopus 로고
    • The NLRP3 inflammasome instigates obesity-induced inflammation and insulin resistance
    • B. Vandanmagsar, Y.-H. Youm, A. Ravussin et al., "The NLRP3 inflammasome instigates obesity-induced inflammation and insulin resistance," Nature Medicine, vol. 17, no. 2, pp. 179-189, 2011.
    • (2011) Nature Medicine , vol.17 , Issue.2 , pp. 179-189
    • Vandanmagsar, B.1    Youm, Y.-H.2    Ravussin, A.3
  • 64
    • 32944470765 scopus 로고    scopus 로고
    • Cryopyrin activates the inflammasome in response to toxins and ATP
    • S. Mariathasan, D S. Weiss, K. Newton et al., "Cryopyrin activates the inflammasome in response to toxins and ATP," Nature, vol. 440, no. 7081, pp. 228-232, 2006.
    • (2006) Nature , vol.440 , Issue.7081 , pp. 228-232
    • Mariathasan, S.1    Weiss, D.S.2    Newton, K.3
  • 65
    • 47849085872 scopus 로고    scopus 로고
    • The NALP3 inflammasome is involved in the innate immune response to amyloid-beta
    • A. Halle, V. Hornung, G C. Petzold et al., "The NALP3 inflammasome is involved in the innate immune response to amyloid-beta," Nature Immunology, vol. 9, no. 8, pp. 857-865, 2008.
    • (2008) Nature Immunology , vol.9 , Issue.8 , pp. 857-865
    • Halle, A.1    Hornung, V.2    Petzold, G.C.3
  • 67
    • 70350365853 scopus 로고    scopus 로고
    • NADPH oxidase mediates beta-amyloid peptide-induced activation of ERK in hippocampal organotypic cultures
    • E Serrano, A. Chang, C. Hernandez, R. G Pautler, J. D. Sweatt, and E. Klann, "NADPH oxidase mediates beta-amyloid peptide-induced activation of ERK in hippocampal organotypic cultures," Molecular Brain, vol. 2, no. 1, article 31, 2009.
    • (2009) Molecular Brain , vol.2 , Issue.1
    • Serrano, E.1    Chang, A.2    Hernandez, C.3    Pautler, R.G.4    Sweatt, J.D.5    Klann, E.6
  • 68
    • 33845768784 scopus 로고    scopus 로고
    • Microglia-mediated neurotoxicity: Uncovering the molecular mechanisms
    • M. L. Block, L. Zecca, and J.-S. Hong, "Microglia-mediated neurotoxicity: uncovering the molecular mechanisms," Nature Reviews Neuroscience, vol. 8, no. 1, pp. 57-69, 2007
    • (2007) Nature Reviews Neuroscience , vol.8 , Issue.1 , pp. 57-69
    • Block, M.L.1    Zecca, L.2    Hong, J.-S.3
  • 69
    • 33846460101 scopus 로고    scopus 로고
    • Receptor for advanced glycation end products activation injures primary sensory neurons via oxidative stress
    • A. M. Vincent, L. Perrone, K. A. Sullivan et al., "Receptor for advanced glycation end products activation injures primary sensory neurons via oxidative stress," Endocrinology, vol. 148, no. 2, pp. 548-558, 2007
    • (2007) Endocrinology , vol.148 , Issue.2 , pp. 548-558
    • Vincent, A.M.1    Perrone, L.2    Sullivan, K.A.3
  • 70
    • 84896884534 scopus 로고    scopus 로고
    • Increased expression of the receptor for advanced glycation end products in neurons and astrocytes in a triple transgenic mouse model of Alzheimer's disease
    • B. R. Choi, W. H. Cho, J. Kim et al., "Increased expression of the receptor for advanced glycation end products in neurons and astrocytes in a triple transgenic mouse model of Alzheimer's disease," Experimental and Molecular Medicine, vol. 46, article e75, 2014.
    • (2014) Experimental and Molecular Medicine , vol.46
    • Choi, B.R.1    Cho, W.H.2    Kim, J.3
  • 71
    • 0013615899 scopus 로고    scopus 로고
    • RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
    • S. D. Yan, X. Chen, J. Fu et al, "RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease," Nature, vol. 382, no. 6593, pp. 685-691, 1996.
    • (1996) Nature , vol.382 , Issue.6593 , pp. 685-691
    • Yan, S.D.1    Chen, X.2    Fu, J.3
  • 72
    • 0032720953 scopus 로고    scopus 로고
    • The role of oxidative stress and NF-κB activation in late diabetic complications
    • A. K. Mohamed, A. Bierhaus, S. Schiekofer, H. Tritschler, R. Ziegler, and P. P. Nawroth, "The role of oxidative stress and NF-κB activation in late diabetic complications," BioFactors, vol. 10, no. 2-3, pp. 157-167, 1999.
    • (1999) BioFactors , vol.10 , Issue.2-3 , pp. 157-167
    • Mohamed, A.K.1    Bierhaus, A.2    Schiekofer, S.3    Tritschler, H.4    Ziegler, R.5    Nawroth, P.P.6
  • 73
    • 0028068046 scopus 로고
    • Cellular receptors for advanced glycation end products. Implications for induction of oxidant stress and cellular dysfunction in the pathogenesis of vascular lesions
    • A. M. Schmidt, O. Hori, J. Brett, S. D. Yan, J.-L. Wautier, and D. Stern, "Cellular receptors for advanced glycation end products. Implications for induction of oxidant stress and cellular dysfunction in the pathogenesis of vascular lesions," Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 14, no. 10, pp. 1521-1528, 1994.
    • (1994) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.14 , Issue.10 , pp. 1521-1528
    • Schmidt, A.M.1    Hori, O.2    Brett, J.3    Yan, S.D.4    Wautier, J.-L.5    Stern, D.6
  • 74
    • 12744279326 scopus 로고    scopus 로고
    • Redox paradox: Insulin action is facilitated by insulin-stimulated reactive oxygen species with multiple potential signaling targets
    • B. J. Goldstein, M. Kalyankar, and X Wu, "Redox paradox: insulin action is facilitated by insulin-stimulated reactive oxygen species with multiple potential signaling targets," Diabetes, vol. 54, no. 2, pp. 311-321, 2005.
    • (2005) Diabetes , vol.54 , Issue.2 , pp. 311-321
    • Goldstein, B.J.1    Kalyankar, M.2    Wu, X.3
  • 75
    • 0035877633 scopus 로고    scopus 로고
    • Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase lb in vivo and enhances the early insulin action cascade
    • K. Mahadev, A. Zilbering, L. Zhu, and B. J. Goldstein, "Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase lb in vivo and enhances the early insulin action cascade," The journal of Biological Chemistry, vol. 276, no. 24, pp. 21938-21942, 2001.
    • (2001) The Journal of Biological Chemistry , vol.276 , Issue.24 , pp. 21938-21942
    • Mahadev, K.1    Zilbering, A.2    Zhu, L.3    Goldstein, B.J.4
  • 76
    • 33750028310 scopus 로고    scopus 로고
    • Regulation of acetylcholinesterase expression by calcium signaling during calcium ionophore A2
    • H. Zhu, W. Gao, H. Jiang et al., "Regulation of acetylcholinesterase expression by calcium signaling during calcium ionophore A2," The International journal of Biochemistry & Cell Biology, vol. 39, pp. 93-108, 2007
    • (2007) The International Journal of Biochemistry & Cell Biology , vol.39 , pp. 93-108
    • Zhu, H.1    Gao, W.2    Jiang, H.3
  • 77
    • 0027491242 scopus 로고
    • Regulated and constitutive secretion of distinct molecular forms of acetylcholinesterase from PC12 cells
    • E. S. Schweitzer, "Regulated and constitutive secretion of distinct molecular forms of acetylcholinesterase from PC12 cells," journal of Cell Science, vol. 106, no. 3, pp. 731-740, 1993.
    • (1993) Journal of Cell Science , vol.106 , Issue.3 , pp. 731-740
    • Schweitzer, E.S.1
  • 78
    • 1842375103 scopus 로고    scopus 로고
    • The amyloid beta-protein of Alzheimer's disease increases acetylcholinesterase expression by increasing intracellular calcium in embryonal carcinoma P19 cells
    • G. Sberna, J. Sáez-Valero, K. Beyreuther, C. L. Masters, and D. H. Small, "The amyloid beta-protein of Alzheimer's disease increases acetylcholinesterase expression by increasing intracellular calcium in embryonal carcinoma P19 cells," journal of Neurochemistry, vol. 69, no. 3, pp. 1177-1184, 1997
    • (1997) Journal of Neurochemistry , vol.69 , Issue.3 , pp. 1177-1184
    • Sberna, G.1    Sáez-Valero, J.2    Beyreuther, K.3    Masters, C.L.4    Small, D.H.5
  • 79
    • 0026570528 scopus 로고
    • Beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • M. P. Mattson, B. Cheng, D Davis, K. Bryant, I. Lieberburg, and R. E. Rydel, "beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity," The journal of Neuroscience, vol. 12, no. 2, pp. 376-389, 1992.
    • (1992) The Journal of Neuroscience , vol.12 , Issue.2 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 80
    • 0037198403 scopus 로고    scopus 로고
    • A non-cholinergic, trophic action of acetylcholinesterase on hippocampal neurones in vitro: Molecular mechanisms
    • T. Day and S. A. Greenfield, "A non-cholinergic, trophic action of acetylcholinesterase on hippocampal neurones in vitro: molecular mechanisms," Neuroscience, vol. 111, no. 3, pp. 649-656, 2002.
    • (2002) Neuroscience , vol.111 , Issue.3 , pp. 649-656
    • Day, T.1    Greenfield, S.A.2
  • 81
    • 47649127364 scopus 로고    scopus 로고
    • 2+ mobilization and glutamate exocytosis in cerebral synap-tosomes from mice
    • 2+ mobilization and glutamate exocytosis in cerebral synap-tosomes from mice," Diabetes Research and Clinical Practice, vol. 81, no. 2, pp. el4-el7, 2008.
    • (2008) Diabetes Research and Clinical Practice , vol.81 , Issue.2 , pp. el4-el7
    • Satoh, E.1    Takahashi, A.2
  • 83
    • 0034745636 scopus 로고    scopus 로고
    • Neurotoxic Abeta peptides increase oxidative stress in vivo through NMDA-receptor and nitric-oxide-synthase mechanisms, and inhibit complex IV activity and induce a mitochondrial permeability transition in vitro
    • J. K. Parks, T. S. Smith, P. A. Trimmer, J. P. Bennett Jr., and W. J. Davis Parker, "Neurotoxic Abeta peptides increase oxidative stress in vivo through NMDA-receptor and nitric-oxide-synthase mechanisms, and inhibit complex IV activity and induce a mitochondrial permeability transition in vitro," Journal of Neurochemistry, vol. 76, no. 4, pp. 1050-1056, 2001.
    • (2001) Journal of Neurochemistry , vol.76 , Issue.4 , pp. 1050-1056
    • Parks, J.K.1    Smith, T.S.2    Trimmer, P.A.3    Bennett, J.P.4    Davis Parker, W.J.5
  • 85
    • 15444339756 scopus 로고    scopus 로고
    • Brain insulin and insulin receptors in aging and sporadic Alzheimer's disease
    • L. Frölich, D. Blum-Degen, H.-G Bernstein et al., "Brain insulin and insulin receptors in aging and sporadic Alzheimer's disease," Journal of Neural Transmission, vol. 105, no. 4-5, pp. 423-438, 1998.
    • (1998) Journal of Neural Transmission , vol.105 , Issue.4-5 , pp. 423-438
    • Frölich, L.1    Blum-Degen, D.2    Bernstein, H.-G.3
  • 86
    • 70349581633 scopus 로고    scopus 로고
    • Insulin resistance and Alzheimer's disease
    • S. M. de la Monte, "Insulin resistance and Alzheimer's disease," BMB Reports, vol. 42, no. 8, pp. 475-481, 2009.
    • (2009) BMB Reports , vol.42 , Issue.8 , pp. 475-481
    • De La Monte, S.M.1
  • 87
    • 60349128460 scopus 로고    scopus 로고
    • A study of brain insulin receptors, AChE activity and oxidative stress in rat model of ICV STZ induced dementia
    • R. Agrawal, E. Tyagi, R. Shukla, and G Nath, "A study of brain insulin receptors, AChE activity and oxidative stress in rat model of ICV STZ induced dementia," Neuropharmacology, vol. 56, no. 4, pp. 779-787, 2009.
    • (2009) Neuropharmacology , vol.56 , Issue.4 , pp. 779-787
    • Agrawal, R.1    Tyagi, E.2    Shukla, R.3    Nath, G.4
  • 90
    • 0033537830 scopus 로고    scopus 로고
    • Oxidative stress disrupts insulin-induced cellular redistribution of insulin receptor substrate-1 and phosphatidylinositol 3-kinase in 3T3-L1 adipocytes. A putative cellular mechanism for impaired protein kinase B activation and GLUT4 translocation
    • A. Tirosh, R. Potashnik, N. Bashan, and A. Rudich, "Oxidative stress disrupts insulin-induced cellular redistribution of insulin receptor substrate-1 and phosphatidylinositol 3-kinase in 3T3-L1 adipocytes. A putative cellular mechanism for impaired protein kinase B activation and GLUT4 translocation," The Journal of Biological Chemistry, vol. 274, no. 15, pp. 10595-10602, 1999.
    • (1999) The Journal of Biological Chemistry , vol.274 , Issue.15 , pp. 10595-10602
    • Tirosh, A.1    Potashnik, R.2    Bashan, N.3    Rudich, A.4
  • 91
    • 77957229010 scopus 로고    scopus 로고
    • Insulin signaling meets mitochondria in metabolism
    • Z. Cheng, Y. Tseng, and M. E White, "Insulin signaling meets mitochondria in metabolism," Trends in Endocrinology and Metabolism, vol. 21, no. 10, pp. 589-598, 2010.
    • (2010) Trends in Endocrinology and Metabolism , vol.21 , Issue.10 , pp. 589-598
    • Cheng, Z.1    Tseng, Y.2    White, E.M.3
  • 92
    • 0036715628 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase 1B inhibitors for diabetes
    • T. O. Johnson, J. Ermolieff, and M. R. Jirousek, "Protein tyrosine phosphatase 1B inhibitors for diabetes," Nature Reviews Drug Discovery, vol. 1, no. 9, pp. 696-709, 2002.
    • (2002) Nature Reviews Drug Discovery , vol.1 , Issue.9 , pp. 696-709
    • Johnson, T.O.1    Ermolieff, J.2    Jirousek, M.R.3
  • 94
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation
    • J. M. Denu and K. G. Tanner, "Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation," Biochemistry, vol. 37, no. 16, pp. 5633-5642, 1998.
    • (1998) Biochemistry , vol.37 , Issue.16 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 95
    • 0028979464 scopus 로고
    • Crystal structure of the Cys2 activator-binding domain of protein kinase CΔ in complex with phorbol ester
    • G. Zhang, M. G. Kazanietz, P. M. Blumberg, and J. H. Hurley, "Crystal structure of the Cys2 activator-binding domain of protein kinase CΔ in complex with phorbol ester," Cell, vol. 81, no. 6, pp. 917-924, 1995.
    • (1995) Cell , vol.81 , Issue.6 , pp. 917-924
    • Zhang, G.1    Kazanietz, M.G.2    Blumberg, P.M.3    Hurley, J.H.4
  • 96
    • 30344460004 scopus 로고    scopus 로고
    • Redox regulation of cardiac protein kinase C
    • I. Korichneva, "Redox regulation of cardiac protein kinase C," Experimental and Clinical Cardiology, vol. 10, no. 4, pp. 256-261, 2005.
    • (2005) Experimental and Clinical Cardiology , vol.10 , Issue.4 , pp. 256-261
    • Korichneva, I.1
  • 99
    • 0034705402 scopus 로고    scopus 로고
    • Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone
    • S. Barbirz, U. Jakob, and M. O. Glocker, "Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone," The Journal of Biological Chemistry, vol. 275, no. 25, pp. 18759-18766, 2000.
    • (2000) The Journal of Biological Chemistry , vol.275 , Issue.25 , pp. 18759-18766
    • Barbirz, S.1    Jakob, U.2    Glocker, M.O.3
  • 100
    • 0034190297 scopus 로고    scopus 로고
    • Protein kinase C signaling and oxidative stress
    • R. Gopalakrishna and S. Jaken, "Protein kinase C signaling and oxidative stress," Tree Radical Biology and Medicine, vol. 28, no. 9, pp. 1349-1361, 2000.
    • (2000) Tree Radical Biology and Medicine , vol.28 , Issue.9 , pp. 1349-1361
    • Gopalakrishna, R.1    Jaken, S.2
  • 101
    • 0034903753 scopus 로고    scopus 로고
    • Potent inactivation of representative members of each PKC isozyme subfamily and PKD via S-thiolation by the tumor-promotion/progression antagonist glutathione but not by its precursor cysteine
    • F. Chu, N. E. Ward, and G A. O'Brian, "Potent inactivation of representative members of each PKC isozyme subfamily and PKD via S-thiolation by the tumor-promotion/progression antagonist glutathione but not by its precursor cysteine," Carcinogenesis, vol. 22, no. 8, pp. 1221-1229, 2001.
    • (2001) Carcinogenesis , vol.22 , Issue.8 , pp. 1221-1229
    • Chu, F.1    Ward, N.E.2    O'Brian, G.A.3
  • 102
    • 0035941358 scopus 로고    scopus 로고
    • Regulation of vascular endothelial growth factor expression by advanced glycation end products
    • C. Treins, S. Giorgetti-Peraldi, J. Murdaca, and E. Van Obberghen, "Regulation of vascular endothelial growth factor expression by advanced glycation end products," The Journal of Biological Chemistry, vol. 276, no. 47, pp. 43836-43841, 2001.
    • (2001) The Journal of Biological Chemistry , vol.276 , Issue.47 , pp. 43836-43841
    • Treins, C.1    Giorgetti-Peraldi, S.2    Murdaca, J.3    Van Obberghen, E.4
  • 103
    • 17144369501 scopus 로고    scopus 로고
    • Oxidative activation of protein kinase Cgamma through the C1 domain. Effects on gap junctions
    • D. Lin and D. J. Takemoto, "Oxidative activation of protein kinase Cgamma through the C1 domain. Effects on gap junctions," Journal of Biological Chemistry, vol. 280, no. 14, pp. 13682-13693, 2005.
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 13682-13693
    • Lin, D.1    Takemoto, D.J.2
  • 104
    • 14644444082 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications: A unifying mechanism
    • D. LeRoith, S. I. Taylor, and J. M. Olefsky, Eds. Lippincott Williams & Wilkins, Philadelphia, Pa, USA
    • S. Hofmann and M. Brownlee, "Biochemistry and molecular cell biology of diabetic complications: a unifying mechanism," in Diabetes Mellitus: A Tundamental and Clinical Text, D. LeRoith, S. I. Taylor, and J. M. Olefsky, Eds., pp. 1441-14457, Lippincott Williams & Wilkins, Philadelphia, Pa, USA, 2004.
    • (2004) Diabetes Mellitus: A Tundamental and Clinical Text , pp. 1441-14457
    • Hofmann, S.1    Brownlee, M.2
  • 105
    • 0038187674 scopus 로고    scopus 로고
    • GSK-3α regulates production of Alzheimer's disease amyloid-β peptides
    • C. J. Phiel, C. A. Wilson, V. M.-Y Lee, and P. S. Klein, "GSK-3α regulates production of Alzheimer's disease amyloid-β peptides," Nature, vol. 423, no. 6938, pp. 435-439, 2003.
    • (2003) Nature , vol.423 , Issue.6938 , pp. 435-439
    • Phiel, C.J.1    Wilson, C.A.2    Lee, V.M.-Y.3    Klein, P.S.4
  • 108
    • 26844541999 scopus 로고    scopus 로고
    • Melatonin precludes cytoskeletal collapse caused by hydrogen peroxide: Participation of protein kinase C
    • G. Benitez-King, L. Ortiz-López, and G. Jiménez-Rubio, "Melatonin precludes cytoskeletal collapse caused by hydrogen peroxide: participation of protein kinase C," Therapy, vol. 2, no. 5, pp. 767-778, 2005.
    • (2005) Therapy , vol.2 , Issue.5 , pp. 767-778
    • Benitez-King, G.1    Ortiz-López, L.2    Jiménez-Rubio, G.3
  • 109
    • 84875441025 scopus 로고    scopus 로고
    • Sodium phenylbutyrate enhances astrocytic neurotrophin synthesis via protein kinase C (PKC)-mediated activation of cAMP-response element-binding protein (CREB): Implications for alzheimer disease therapy
    • G. T. Corbett, A. Roy, and K. Pahan, "Sodium phenylbutyrate enhances astrocytic neurotrophin synthesis via protein kinase C (PKC)-mediated activation of cAMP-response element-binding protein (CREB): implications for alzheimer disease therapy," The Journal of Biological Chemistry, vol. 288, no. 12, pp. 8299-8312, 2013.
    • (2013) The Journal of Biological Chemistry , vol.288 , Issue.12 , pp. 8299-8312
    • Corbett, G.T.1    Roy, A.2    Pahan, K.3
  • 110
    • 23844459902 scopus 로고    scopus 로고
    • Prolonged Alzheimer-like tau hyperphosphorylation induced by simultaneous inhibition of phosphoinositol-3 kinase and protein kinase C in N2a cells
    • G.-G. Xu, Y.-Q. Deng, S.-J. Liu, H.-L. Li, and J.-Z. Wang, "Prolonged Alzheimer-like tau hyperphosphorylation induced by simultaneous inhibition of phosphoinositol-3 kinase and protein kinase C in N2a cells," Acta Biochimica et Biophysica Sinica, vol. 37, no. 5, pp. 349-354, 2005.
    • (2005) Acta Biochimica et Biophysica Sinica , vol.37 , Issue.5 , pp. 349-354
    • Xu, G.-G.1    Deng, Y.-Q.2    Liu, S.-J.3    Li, H.-L.4    Wang, J.-Z.5
  • 111
    • 0025992927 scopus 로고
    • Action of amyloid beta-protein on protein kinase C activity
    • A. Chauhan, V. P. S. Chauhan, H. Brockerhoff, and H. M. Wisniewski, "Action of amyloid beta-protein on protein kinase C activity," Life Sciences, vol. 49, no. 21, pp. 1555-1562, 1991.
    • (1991) Life Sciences , vol.49 , Issue.21 , pp. 1555-1562
    • Chauhan, A.1    Chauhan, V.P.S.2    Brockerhoff, H.3    Wisniewski, H.M.4
  • 113
    • 84891885282 scopus 로고    scopus 로고
    • Brain atrophy in type 2 diabetes: Regional distribution and influence on cognition
    • C. Moran, T. G. Phan, J. Chen et al., "Brain atrophy in type 2 diabetes: regional distribution and influence on cognition," Diabetes Care, vol. 36, no. 12, pp. 4036-4042, 2013.
    • (2013) Diabetes Care , vol.36 , Issue.12 , pp. 4036-4042
    • Moran, C.1    Phan, T.G.2    Chen, J.3
  • 114
    • 84863940277 scopus 로고    scopus 로고
    • Protein kinase C and tolllike receptor signaling
    • D. J. Loegering and M. R. Lennartz, "Protein kinase C and tolllike receptor signaling," Enzyme Research, vol. 2011, no. 1, Article ID 537821, 2011.
    • (2011) Enzyme Research , vol.2011 , Issue.1
    • Loegering, D.J.1    Lennartz, M.R.2
  • 115
    • 43549087343 scopus 로고    scopus 로고
    • Insulin neuroprotection against oxidative stress is mediated by Akt and GSK-3beta signaling pathways and changes in protein expression
    • A. I. Duarte, P. Santos, C. R. Oliveira, M. S. Santos, and A. C. Rego, "Insulin neuroprotection against oxidative stress is mediated by Akt and GSK-3beta signaling pathways and changes in protein expression," Biochimica et Biophysica Acta-Molecular Cell Research, vol. 1783, no. 6, pp. 994-1002, 2008.
    • (2008) Biochimica et Biophysica Acta-Molecular Cell Research , vol.1783 , Issue.6 , pp. 994-1002
    • Duarte, A.I.1    Santos, P.2    Oliveira, C.R.3    Santos, M.S.4    Rego, A.C.5
  • 116
    • 77749336528 scopus 로고    scopus 로고
    • Amyloid-β neurotoxicity in organotypic culture is attenuated by melatonin: Involvement of GSK-3β, tau and neuroinflammation
    • J. B. Hoppe, R. L. Frozza, A. P. Horn et al., "Amyloid-β neurotoxicity in organotypic culture is attenuated by melatonin: involvement of GSK-3β, tau and neuroinflammation," Journal of Pineal Research, vol. 48, no. 3, pp. 230-238, 2010.
    • (2010) Journal of Pineal Research , vol.48 , Issue.3 , pp. 230-238
    • Hoppe, J.B.1    Frozza, R.L.2    Horn, A.P.3
  • 117
    • 65249113325 scopus 로고    scopus 로고
    • The insulin/Akt signaling pathway is targeted by intracellular beta-amyloid
    • H. K. Lee, P. Kumar, Q. Fu, K. M. Rosen, and H. W. Querfurth, "The insulin/Akt signaling pathway is targeted by intracellular beta-amyloid," Molecular Biology of the Cell, vol. 20, no. 5, pp. 1533-1544, 2009.
    • (2009) Molecular Biology of the Cell , vol.20 , Issue.5 , pp. 1533-1544
    • Lee, H.K.1    Kumar, P.2    Fu, Q.3    Rosen, K.M.4    Querfurth, H.W.5
  • 118
    • 60549084867 scopus 로고    scopus 로고
    • Protection of synapses against Alzheimer's-linked toxins: Insulin signaling prevents the pathogenic binding of Aβ oligomers
    • F. G. de Felice, M. N. N. Vieira, T. R. Bomfim et al., "Protection of synapses against Alzheimer's-linked toxins: insulin signaling prevents the pathogenic binding of Aβ oligomers," Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 6, pp. 1971-1976, 2009.
    • (2009) Proceedings of the National Academy of Sciences of the United States of America , vol.106 , Issue.6 , pp. 1971-1976
    • De Felice, F.G.1    Vieira, M.N.N.2    Bomfim, T.R.3
  • 119
    • 71349085957 scopus 로고    scopus 로고
    • Defects in IGF-1 receptor, insulin receptor and IRS-1/2 in Alzheimer's disease indicate possible resistance to IGF-1 and insulin signalling
    • A. M. Moloney, R. J. Griffin, S. Timmons, R. O'Connor, R. Ravid, and G O'Neill, "Defects in IGF-1 receptor, insulin receptor and IRS-1/2 in Alzheimer's disease indicate possible resistance to IGF-1 and insulin signalling," Neurobiology of Aging, vol. 31, no. 2, pp. 224-243, 2010.
    • (2010) Neurobiology of Aging , vol.31 , Issue.2 , pp. 224-243
    • Moloney, A.M.1    Griffin, R.J.2    Timmons, S.3    O'Connor, R.4    Ravid, R.5    O'Neill, G.6
  • 120
    • 4644286910 scopus 로고    scopus 로고
    • Diet-induced insulin resistance promotes amyloidosis in a transgenic mouse model of Alzheimer's disease
    • L. Ho, W. Qin, P. N. Pompl et al., "Diet-induced insulin resistance promotes amyloidosis in a transgenic mouse model of Alzheimer's disease," The FASEB Journal, vol. 18, no. 7, pp. 902-904, 2004.
    • (2004) The FASEB Journal , vol.18 , Issue.7 , pp. 902-904
    • Ho, L.1    Qin, W.2    Pompl, P.N.3
  • 121
    • 0037390039 scopus 로고    scopus 로고
    • Insulin-degrading enzyme regulates the levels of insulin, amyloid beta-protein, and the beta-amyloid precursor protein intracellular domain in vivo
    • W. Farris, S. Mansourian, Y. Chang et al., "Insulin-degrading enzyme regulates the levels of insulin, amyloid beta-protein, and the beta-amyloid precursor protein intracellular domain in vivo," Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 7, pp. 4162-4167, 2003.
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.7 , pp. 4162-4167
    • Farris, W.1    Mansourian, S.2    Chang, Y.3
  • 122
    • 0028176821 scopus 로고
    • Alzheimer's β-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme
    • I. V. Kurochkin and S. Goto, "Alzheimer's β-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme," FEBS Letters, vol. 345, no. 1, pp. 33-37, 1994.
    • (1994) FEBS Letters , vol.345 , Issue.1 , pp. 33-37
    • Kurochkin, I.V.1    Goto, S.2
  • 124
    • 79952935338 scopus 로고    scopus 로고
    • Redox regulation of insulin degradation by insulin-degrading enzyme
    • C. M. Cordes, R. G. Bennett, G. L. Siford, and F. G. Hamel, "Redox regulation of insulin degradation by insulin-degrading enzyme," PLoS ONE, vol. 6, no. 3, Article ID el8138, 2011.
    • (2011) PLoS ONE , vol.6 , Issue.3
    • Cordes, C.M.1    Bennett, R.G.2    Siford, G.L.3    Hamel, F.G.4
  • 125
    • 27944440133 scopus 로고    scopus 로고
    • Susceptibility of amyloid β peptide degrading enzymes to oxidative damage: A potential Alzheimer's disease spiral
    • H. Shinall, E. S. Song, and L. B. Hersh, "Susceptibility of amyloid β peptide degrading enzymes to oxidative damage: a potential Alzheimer's disease spiral," Biochemistry, vol. 44, no. 46, pp. 15345-15350, 2005.
    • (2005) Biochemistry , vol.44 , Issue.46 , pp. 15345-15350
    • Shinall, H.1    Song, E.S.2    Hersh, L.B.3
  • 126
    • 0018389336 scopus 로고
    • The effect of age on insulin-degrading activity in rat tissue
    • K. Runyan, W. C. Duckworth, A. E. Kitabchi, and G. Huff, "The effect of age on insulin-degrading activity in rat tissue," Diabetes, vol. 28, no. 4, pp. 324-325, 1979.
    • (1979) Diabetes , vol.28 , Issue.4 , pp. 324-325
    • Runyan, K.1    Duckworth, W.C.2    Kitabchi, A.E.3    Huff, G.4
  • 127
    • 0037900150 scopus 로고    scopus 로고
    • In vitro inhibition of insulin-degrading enzyme by long-chain fatty acids and their coenzyme A thioesters
    • F. G. Hamel, J. L. Upward, and R. G. Bennett, "In vitro inhibition of insulin-degrading enzyme by long-chain fatty acids and their coenzyme A thioesters," Endocrinology, vol. 144, no. 6, pp. 2404-2408, 2003.
    • (2003) Endocrinology , vol.144 , Issue.6 , pp. 2404-2408
    • Hamel, F.G.1    Upward, J.L.2    Bennett, R.G.3
  • 128
    • 84921614222 scopus 로고    scopus 로고
    • C allele of the rs2209972 single nucleotide polymorphism of the insulin degrading enzyme gene and Alzheimer's disease in type 2 diabetes, a case control study
    • H. Gutiérrez-Hermosillo, D. de León-Gonzáleze, R. Palacios-Corona et al., "C allele of the rs2209972 single nucleotide polymorphism of the insulin degrading enzyme gene and Alzheimer's disease in type 2 diabetes, a case control study," Medicina Clinica, vol. 144, no. 4, pp. 151-155, 2015.
    • (2015) Medicina Clinica , vol.144 , Issue.4 , pp. 151-155
    • Gutiérrez-Hermosillo, H.1    De León-Gonzáleze, D.2    Palacios-Corona, R.3
  • 129
    • 85047691537 scopus 로고    scopus 로고
    • Inhibition of GAPDH activity by poly(ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells
    • X. Du, T. Matsumura, D. Edelstein et al., "Inhibition of GAPDH activity by poly(ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells," The Journal of Clinical Investigation, vol. 112, no. 7, pp. 1049-1057, 2003.
    • (2003) The Journal of Clinical Investigation , vol.112 , Issue.7 , pp. 1049-1057
    • Du, X.1    Matsumura, T.2    Edelstein, D.3
  • 130
    • 70449712602 scopus 로고    scopus 로고
    • Novel roles for GAPDH in cell death and carcinogenesis
    • A. Colell, D. R. Green, and J.-E. Ricci, "Novel roles for GAPDH in cell death and carcinogenesis," Cell Death and Differentiation, vol. 16, no. 12, pp. 1573-1581, 2009.
    • (2009) Cell Death and Differentiation , vol.16 , Issue.12 , pp. 1573-1581
    • Colell, A.1    Green, D.R.2    Ricci, J.-E.3
  • 131
    • 2442693140 scopus 로고    scopus 로고
    • Nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase: A role in high glucose-induced apoptosis in retinal Müller cells
    • L. L. Kusner, V. P. Sarthy, and S. Mohr, "Nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase: a role in high glucose-induced apoptosis in retinal Müller cells," Investigative Ophthalmology and Visual Science, vol. 45, no. 5, pp. 1553-1561, 2004.
    • (2004) Investigative Ophthalmology and Visual Science , vol.45 , Issue.5 , pp. 1553-1561
    • Kusner, L.L.1    Sarthy, V.P.2    Mohr, S.3
  • 133
    • 77954497959 scopus 로고    scopus 로고
    • Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and alzheimer's disease: Many pathways to neurode-generation
    • D. A. Butterfield, S. S. Hardas, and M. L. B. Lange, "Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and alzheimer's disease: many pathways to neurode-generation," Journal of Alzheimer's Disease, vol. 20, no. 2, pp. 369-393, 2010.
    • (2010) Journal of Alzheimer's Disease , vol.20 , Issue.2 , pp. 369-393
    • Butterfield, D.A.1    Hardas, S.S.2    Lange, M.L.B.3
  • 134
    • 34248223082 scopus 로고    scopus 로고
    • An increase in S-glutathionylated proteins in the Alzheimer's disease inferior parietal lobule, a proteomics approach
    • S. F. Newman, R. Sultana, M. Perluigi et al., "An increase in S-glutathionylated proteins in the Alzheimer's disease inferior parietal lobule, a proteomics approach," Journal of Neuroscience Research, vol. 85, no. 7, pp. 1506-1514, 2007
    • (2007) Journal of Neuroscience Research , vol.85 , Issue.7 , pp. 1506-1514
    • Newman, S.F.1    Sultana, R.2    Perluigi, M.3
  • 135
    • 25844458239 scopus 로고    scopus 로고
    • Current advances on different kinases involved in tau phosphorylation, and implications in Alzheimer's disease and tauopathies
    • I. Ferrer, T. Gomez-Isla, B. Puig et al., "Current advances on different kinases involved in tau phosphorylation, and implications in Alzheimer's disease and tauopathies," Current Alzheimer Research, vol. 2, no. 1, pp. 3-18, 2005.
    • (2005) Current Alzheimer Research , vol.2 , Issue.1 , pp. 3-18
    • Ferrer, I.1    Gomez-Isla, T.2    Puig, B.3
  • 136
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - A visualization system for exploratory research and analysis
    • E. F. Pettersen, T. D. Goddard, C. C. Huang et al., "UCSF Chimera - a visualization system for exploratory research and analysis," Journal of Computational Chemistry, vol. 25, no. 13, pp. 1605-1612, 2004.
    • (2004) Journal of Computational Chemistry , vol.25 , Issue.13 , pp. 1605-1612
    • Pettersen, E.F.1    Goddard, T.D.2    Huang, C.C.3
  • 137
    • 84924625656 scopus 로고    scopus 로고
    • Diabetes, fact sheet no. 312
    • World Health Organization, Ed. World Health Organization
    • World Health Organization, "Diabetes, fact sheet no. 312," in WHO Media Centre, Fact Sheets, World Health Organization, Ed., vol. 2014, World Health Organization, 2014.
    • (2014) WHO Media Centre, Fact Sheets , vol.2014
  • 138
    • 77952771512 scopus 로고    scopus 로고
    • Alzheimer's disease international world Alzheimer report 2014. Dementia and risk reduction
    • Alzheimer's Disease International, Ed. Alzheimer's Disease International, London, UK
    • M. Prince, E. Albanese, M. Guerchet, and M. Prina, "Alzheimer's disease international world Alzheimer report 2014. Dementia and risk reduction," in Alzheimer's Disease International World Alzheimer, Alzheimer's Disease International, Ed., p. 104, Alzheimer's Disease International, London, UK, 2014.
    • (2014) Alzheimer's Disease International World Alzheimer , pp. 104
    • Prince, M.1    Albanese, E.2    Guerchet, M.3    Prina, M.4
  • 139
    • 84899414414 scopus 로고    scopus 로고
    • Diabetes mellitus and the risk of Alzheimer's disease: A nationwide population-based study
    • C. C. Huang, C. M. Chung, H. B. Leu et al., "Diabetes mellitus and the risk of Alzheimer's disease: a nationwide population-based study," PLoS ONE, vol. 9, no. 1, Article ID e87095, 2014.
    • (2014) PLoS ONE , vol.9 , Issue.1
    • Huang, C.C.1    Chung, C.M.2    Leu, H.B.3
  • 140
    • 15244351255 scopus 로고    scopus 로고
    • Impaired insulin and insulin-like growth factor expression and signaling mechanisms in Alzheimer's disease-is this type 3 diabetes?
    • E. Steen, B. M. Terry, E. J. Rivera et al., "Impaired insulin and insulin-like growth factor expression and signaling mechanisms in Alzheimer's disease-is this type 3 diabetes?" Journal of Alzheimer's Disease, vol. 7, no. 1, pp. 63-80, 2005.
    • (2005) Journal of Alzheimer's Disease , vol.7 , Issue.1 , pp. 63-80
    • Steen, E.1    Terry, B.M.2    Rivera, E.J.3
  • 143
    • 2442421194 scopus 로고    scopus 로고
    • Is oxidative stress the pathogenic mechanism underlying insulin resistance, diabetes, and cardiovascular disease? The common soil hypothesis revisited
    • A. Ceriello and E. Motz, "Is oxidative stress the pathogenic mechanism underlying insulin resistance, diabetes, and cardiovascular disease? The common soil hypothesis revisited," Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 24, no. 5, pp. 816-823, 2004.
    • (2004) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.24 , Issue.5 , pp. 816-823
    • Ceriello, A.1    Motz, E.2
  • 144
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • M. Brownlee, "Biochemistry and molecular cell biology of diabetic complications," Nature, vol. 414, no. 6865, pp. 813-820, 2001.
    • (2001) Nature , vol.414 , Issue.6865 , pp. 813-820
    • Brownlee, M.1
  • 146
    • 0023913225 scopus 로고
    • The involvement of aldose reductase in diabetic complications
    • J. H. Kinoshita and C. Nishimura, "The involvement of aldose reductase in diabetic complications," Diabetes/Metabolism Reviews, vol. 4, no. 4, pp. 323-337, 1988.
    • (1988) Diabetes/Metabolism Reviews , vol.4 , Issue.4 , pp. 323-337
    • Kinoshita, J.H.1    Nishimura, C.2
  • 147
    • 56649112649 scopus 로고    scopus 로고
    • Hyperglycemia not hypoglycemia alters neuronal dendrites and impairs spatial memory
    • J. I. Malone, S. Hanna, S. Saporta et al., "Hyperglycemia not hypoglycemia alters neuronal dendrites and impairs spatial memory," Pediatric Diabetes, vol. 9, no. 6, pp. 531-539, 2008.
    • (2008) Pediatric Diabetes , vol.9 , Issue.6 , pp. 531-539
    • Malone, J.I.1    Hanna, S.2    Saporta, S.3
  • 150
    • 0037305028 scopus 로고    scopus 로고
    • Alzheimer's disease and total plasma aminothiols
    • A. McCaddon, P. Hudson, D. Hill et al., "Alzheimer's disease and total plasma aminothiols," Biological Psychiatry, vol. 53, no. 3, pp. 254-260, 2003.
    • (2003) Biological Psychiatry , vol.53 , Issue.3 , pp. 254-260
    • McCaddon, A.1    Hudson, P.2    Hill, D.3
  • 151
    • 84901911564 scopus 로고    scopus 로고
    • The emerging role of glutathione in Alzheimer's disease
    • S. Saharan and P. K. Mandai, "The emerging role of glutathione in Alzheimer's disease," Journal of Alzheimer's Disease, vol. 40, pp. 519-529, 2014.
    • (2014) Journal of Alzheimer's Disease , vol.40 , pp. 519-529
    • Saharan, S.1    Mandai, P.K.2
  • 152
    • 48249094537 scopus 로고    scopus 로고
    • Reducing oxidative stress in patients with type 2 diabetes mellitus: A primary care call to action
    • J. Unger, "Reducing oxidative stress in patients with type 2 diabetes mellitus: a primary care call to action," Insulin, vol. 3, no. 3, pp. 176-184, 2008.
    • (2008) Insulin , vol.3 , Issue.3 , pp. 176-184
    • Unger, J.1
  • 154
    • 79951696287 scopus 로고    scopus 로고
    • Glutathione synthesis is diminished in patients with uncontrolled diabetes and restored by dietary supplementation with cysteine and glycine
    • R. V. Sekhar, S. V. Mckay, S. G Patel et al, "Glutathione synthesis is diminished in patients with uncontrolled diabetes and restored by dietary supplementation with cysteine and glycine," Diabetes Care, vol. 34, no. 1, pp. 162-167, 2011.
    • (2011) Diabetes Care , vol.34 , Issue.1 , pp. 162-167
    • Sekhar, R.V.1    Mckay, S.V.2    Patel, S.G.3
  • 156
    • 35148870841 scopus 로고    scopus 로고
    • Paradoxical upregulation of glutamatergic presynaptic boutons during mild cognitive impairment
    • K. F. S. Bell, D. A. Bennett, and A. C. Cuello, "Paradoxical upregulation of glutamatergic presynaptic boutons during mild cognitive impairment," The Journal of Neuroscience, vol. 27, no. 40, pp. 10810-10817, 2007
    • (2007) The Journal of Neuroscience , vol.27 , Issue.40 , pp. 10810-10817
    • Bell, K.F.S.1    Bennett, D.A.2    Cuello, A.C.3
  • 157
    • 84856718797 scopus 로고    scopus 로고
    • Alzheimer's disease: Pathological mechanisms and the beneficial role of melatonin
    • S. A. Rosales-Corral, D. Acuna-Castroviejo, A. Coto-Montes et al., "Alzheimer's disease: pathological mechanisms and the beneficial role of melatonin," Journal of Pineal Research, vol. 52, no. 2, pp. 167-202, 2012.
    • (2012) Journal of Pineal Research , vol.52 , Issue.2 , pp. 167-202
    • Rosales-Corral, S.A.1    Acuna-Castroviejo, D.2    Coto-Montes, A.3
  • 158
    • 34248174912 scopus 로고    scopus 로고
    • System xc- and glutamate transporter inhibition mediates microglial toxicity to oligodendrocytes
    • M. Domercq, M. V. Sanchez-Gomez, C. Sherwin, E. Etxebarria, R. Fern, and C. Matute, "System xc- and glutamate transporter inhibition mediates microglial toxicity to oligodendrocytes," The Journal of Immunology, vol. 178, no. 10, pp. 6549-6556, 2007.
    • (2007) The Journal of Immunology , vol.178 , Issue.10 , pp. 6549-6556
    • Domercq, M.1    Sanchez-Gomez, M.V.2    Sherwin, C.3    Etxebarria, E.4    Fern, R.5    Matute, C.6
  • 159
    • 79959596092 scopus 로고    scopus 로고
    • Fisetin lowers methylglyoxal dependent protein glycation and limits the complications of diabetes
    • P. Maher, R. Dargusch, J. L. Ehren, S. Okada, K. Sharma, and D. Schubert, "Fisetin lowers methylglyoxal dependent protein glycation and limits the complications of diabetes," PLoS ONE, vol. 6, no. 6, Article ID e21226, 2011.
    • (2011) PLoS ONE , vol.6 , Issue.6
    • Maher, P.1    Dargusch, R.2    Ehren, J.L.3    Okada, S.4    Sharma, K.5    Schubert, D.6
  • 160
    • 84867308972 scopus 로고    scopus 로고
    • Participation of antioxidant and cholinergic system in protective effect of naringenin against type-2 diabetes-induced memory dysfunction in rats
    • A. Rahigude, P. Bhutada, S. Kaulaskar, M. Aswar, and K. Otari, "Participation of antioxidant and cholinergic system in protective effect of naringenin against type-2 diabetes-induced memory dysfunction in rats," Neuroscience, vol. 226, pp. 62-72, 2012.
    • (2012) Neuroscience , vol.226 , pp. 62-72
    • Rahigude, A.1    Bhutada, P.2    Kaulaskar, S.3    Aswar, M.4    Otari, K.5
  • 161
    • 84858152480 scopus 로고    scopus 로고
    • Oxidative stress, glutathione status, sirtuin and cellular stress response in type 2 diabetes
    • V. Calabrese, C. Cornelius, V. Leso et al., "Oxidative stress, glutathione status, sirtuin and cellular stress response in type 2 diabetes," Biochimica et Biophysica Acta: Molecular Basis of Disease, vol. 1822, no. 5, pp. 729-736, 2012.
    • (2012) Biochimica et Biophysica Acta: Molecular Basis of Disease , vol.1822 , Issue.5 , pp. 729-736
    • Calabrese, V.1    Cornelius, C.2    Leso, V.3
  • 163
    • 26844519964 scopus 로고    scopus 로고
    • Diabetes causes inhibition of glucose-6-phosphate dehydrogenase via activation of PKA, which contributes to oxidative stress in rat kidney cortex
    • Y. Xu, B. W. Osborne, and R. C. Stanton, "Diabetes causes inhibition of glucose-6-phosphate dehydrogenase via activation of PKA, which contributes to oxidative stress in rat kidney cortex," The American Journal of Physiology-Renal Physiology, vol. 289, no. 5, pp. F1040-F1047, 2005.
    • (2005) The American Journal of Physiology-Renal Physiology , vol.289 , Issue.5 , pp. F1040-F1047
    • Xu, Y.1    Osborne, B.W.2    Stanton, R.C.3
  • 164
    • 0033198043 scopus 로고    scopus 로고
    • CAMP-dependent protein kinase phosphorylations on Tau in Alzheimer's disease
    • G. A. Jicha, C. Weaver, E. Lane et al., "cAMP-dependent protein kinase phosphorylations on Tau in Alzheimer's disease," The Journal of Neuroscience, vol. 19, no. 17, pp. 7486-7494, 1999.
    • (1999) The Journal of Neuroscience , vol.19 , Issue.17 , pp. 7486-7494
    • Jicha, G.A.1    Weaver, C.2    Lane, E.3
  • 165
    • 67849099654 scopus 로고    scopus 로고
    • Biphasic effects of forskolin on tau phosphorylation and spatial memory in rats
    • Q. Tian, J. X. Zhang, Y. Zhang et al., "Biphasic effects of forskolin on tau phosphorylation and spatial memory in rats," Journal of Alzheimer's Disease, vol. 17, no. 3, pp. 631-642, 2009.
    • (2009) Journal of Alzheimer's Disease , vol.17 , Issue.3 , pp. 631-642
    • Tian, Q.1    Zhang, J.X.2    Zhang, Y.3
  • 167
    • 84908376973 scopus 로고    scopus 로고
    • Homocysteine and cytosolic GSH depletion induce apoptosis and oxidative toxicity through cytosolic calcium overload in the hippocampus of aged mice: Involvement of TRPM2 and TRPV1 channels
    • I. S. Ovey and M. Naziroglu, "Homocysteine and cytosolic GSH depletion induce apoptosis and oxidative toxicity through cytosolic calcium overload in the hippocampus of aged mice: involvement of TRPM2 and TRPV1 channels," Neuroscience, vol. 284, pp. 225-233, 2015.
    • (2015) Neuroscience , vol.284 , pp. 225-233
    • Ovey, I.S.1    Naziroglu, M.2
  • 168
    • 44649198605 scopus 로고    scopus 로고
    • Insulin receptor signaling regulates synapse number, dendritic plasticity, and circuit function in vivo
    • S. L. Chiu, C. M. Chen, and H. T. Cline, "Insulin receptor signaling regulates synapse number, dendritic plasticity, and circuit function in vivo," Neuron, vol. 58, no. 5, pp. 708-719, 2008.
    • (2008) Neuron , vol.58 , Issue.5 , pp. 708-719
    • Chiu, S.L.1    Chen, C.M.2    Cline, H.T.3
  • 169
    • 7444232547 scopus 로고    scopus 로고
    • Glycation-induced inactivation of NADP(+)-dependent isocitrate dehydrogenase: Implications for diabetes and aging
    • I. S. Kil, J. H. Lee, A. H. Shin, and J. W. Park, "Glycation-induced inactivation of NADP(+)-dependent isocitrate dehydrogenase: Implications for diabetes and aging," Free Radical Biology and Medicine, vol. 37, no. 11, pp. 1765-1778, 2004.
    • (2004) Free Radical Biology and Medicine , vol.37 , Issue.11 , pp. 1765-1778
    • Kil, I.S.1    Lee, J.H.2    Shin, A.H.3    Park, J.W.4
  • 171
    • 1642377274 scopus 로고    scopus 로고
    • Impaired mitochondrial activity in the insulin-resistant offspring of patients with type 2 diabetes
    • K. E Petersen, S. Dufour, D. Befroy, R. Garcia, and G. I. Shulman, "Impaired mitochondrial activity in the insulin-resistant offspring of patients with type 2 diabetes," The New England Journal of Medicine, vol. 350, no. 7, pp. 664-671, 2004.
    • (2004) The New England Journal of Medicine , vol.350 , Issue.7 , pp. 664-671
    • Petersen, K.E.1    Dufour, S.2    Befroy, D.3    Garcia, R.4    Shulman, G.I.5
  • 172
    • 0030009314 scopus 로고    scopus 로고
    • BCL-2 expression or antioxidants prevent hyperglycemia-induced formation of intracellular advanced glycation endproducts in bovine endothelial cells
    • I. Giardino, D. Edelstein, and M. Brownlee, "BCL-2 expression or antioxidants prevent hyperglycemia-induced formation of intracellular advanced glycation endproducts in bovine endothelial cells," The Journal of Clinical Investigation, vol. 97, no. 6, pp. 1422-1428, 1996.
    • (1996) The Journal of Clinical Investigation , vol.97 , Issue.6 , pp. 1422-1428
    • Giardino, I.1    Edelstein, D.2    Brownlee, M.3
  • 173
    • 0034643340 scopus 로고    scopus 로고
    • Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage
    • T. Nishikawa, D. Edelstein, X L. Du et al., "Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage," Nature, vol. 404, no. 6779, pp. 787-790, 2000.
    • (2000) Nature , vol.404 , Issue.6779 , pp. 787-790
    • Nishikawa, T.1    Edelstein, D.2    Du, X.L.3
  • 174
    • 84863847452 scopus 로고    scopus 로고
    • Aldose reductase, oxidative stress, and diabetic mellitus
    • W. H. Tang, K. A. Martin, and J. Hwa, "Aldose reductase, oxidative stress, and diabetic mellitus," Frontiers in Pharmacology, vol. 3, article 87, 2012.
    • (2012) Frontiers in Pharmacology , vol.3
    • Tang, W.H.1    Martin, K.A.2    Hwa, J.3
  • 175
    • 0010435350 scopus 로고    scopus 로고
    • Postnatal development of malic enzyme isoforms in rat brain
    • A. Teelken and J. Korf, Eds. Springer, Boston, MA, USA
    • R. Vogel, H. Wiesinger, and B. Hamprecht, "Postnatal development of malic enzyme isoforms in rat brain," in Neurochemistry, A. Teelken and J. Korf, Eds., pp. 765-769, Springer, Boston, MA, USA, 1997
    • (1997) Neurochemistry , pp. 765-769
    • Vogel, R.1    Wiesinger, H.2    Hamprecht, B.3
  • 176
    • 0018829349 scopus 로고
    • Mitochondrial malic enzymes. An association between NAD(P)+-dependent malic enzyme and cell renewal in Sprague-Dawley rat tissues
    • W. O. Nagel, R. T. Dauchy, and L. A. Sauer, "Mitochondrial malic enzymes. An association between NAD(P)+-dependent malic enzyme and cell renewal in Sprague-Dawley rat tissues," The Journal of Biological Chemistry, vol. 255, no. 9, pp. 3849-3854, 1980.
    • (1980) The Journal of Biological Chemistry , vol.255 , Issue.9 , pp. 3849-3854
    • Nagel, W.O.1    Dauchy, R.T.2    Sauer, L.A.3
  • 177
    • 0027465673 scopus 로고
    • Purification of cytosolic malic enzyme from bovine brain, generation of monoclonal antibodies, and immunocytochemical localization of the enzyme in glial cells of neural primary cultures
    • G. M. Kurz, H. Wiesinger, and B. Hamprecht, "Purification of cytosolic malic enzyme from bovine brain, generation of monoclonal antibodies, and immunocytochemical localization of the enzyme in glial cells of neural primary cultures," Journal of Neurochemistry, vol. 60, no. 4, pp. 1467-1474, 1993.
    • (1993) Journal of Neurochemistry , vol.60 , Issue.4 , pp. 1467-1474
    • Kurz, G.M.1    Wiesinger, H.2    Hamprecht, B.3
  • 178
    • 0032524879 scopus 로고    scopus 로고
    • Malic enzyme isoforms in astrocytes: Comparative study on activities in rat brain tissue and astroglia-rich primary cultures
    • R. Vogel, B. Hamprecht, and H. Wiesinger, "Malic enzyme isoforms in astrocytes: comparative study on activities in rat brain tissue and astroglia-rich primary cultures," Neuroscience Letters, vol. 247, no. 2-3, pp. 123-126, 1998.
    • (1998) Neuroscience Letters , vol.247 , Issue.2-3 , pp. 123-126
    • Vogel, R.1    Hamprecht, B.2    Wiesinger, H.3
  • 179
    • 0016818582 scopus 로고
    • Enzymes of glucose metabolism and of the citrate cleavage pathway in adipose tissue of normal and diabetic subjects
    • F. Belfiore, A. M. Rabuazzo, E. Napoli, V. Borzi, and L. Lo Vecchio, "Enzymes of glucose metabolism and of the citrate cleavage pathway in adipose tissue of normal and diabetic subjects," Diabetes, vol. 24, no. 10, pp. 865-873, 1975.
    • (1975) Diabetes , vol.24 , Issue.10 , pp. 865-873
    • Belfiore, F.1    Rabuazzo, A.M.2    Napoli, E.3    Borzi, V.4    Lo Vecchio, L.5
  • 180
    • 0028860813 scopus 로고
    • Localization of thioredoxin in the rat brain and functional implications
    • A. Lippoldt, C. A. Padilla, H. Gerst et al., "Localization of thioredoxin in the rat brain and functional implications," The Journal of Neuroscience, vol. 15, no. 10, pp. 6747-6756, 1995.
    • (1995) The Journal of Neuroscience , vol.15 , Issue.10 , pp. 6747-6756
    • Lippoldt, A.1    Padilla, C.A.2    Gerst, H.3
  • 181
    • 84878786543 scopus 로고    scopus 로고
    • Oxidative modification of lipoic acid by HNE in alzheimer disease brain
    • S. S. Hardas, R. Sultana, A. M. Clark et al., "Oxidative modification of lipoic acid by HNE in alzheimer disease brain," Redox Biology, vol. 1, no. 1, pp. 80-85, 2013.
    • (2013) Redox Biology , vol.1 , Issue.1 , pp. 80-85
    • Hardas, S.S.1    Sultana, R.2    Clark, A.M.3
  • 182
    • 17744367054 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein is stimulated by glucose through a carbohydrate response element and induces beta-cell apoptosis
    • A. H. Minn, C. Hafele, and A. Shalev, "Thioredoxin-interacting protein is stimulated by glucose through a carbohydrate response element and induces beta-cell apoptosis," Endocrinology, vol. 146, no. 5, pp. 2397-2405, 2005.
    • (2005) Endocrinology , vol.146 , Issue.5 , pp. 2397-2405
    • Minn, A.H.1    Hafele, C.2    Shalev, A.3
  • 183
    • 42449110310 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein. A critical link between glucose toxicity and β-cell apoptosis
    • J. Chen, G Saxena, I. N. Mungrue, A. J. Lusis, and A. Shalev, "Thioredoxin-interacting protein. A critical link between glucose toxicity and β-cell apoptosis," Diabetes, vol. 57, no. 4, pp. 938-944, 2008.
    • (2008) Diabetes , vol.57 , Issue.4 , pp. 938-944
    • Chen, J.1    Saxena, G.2    Mungrue, I.N.3    Lusis, A.J.4    Shalev, A.5
  • 184
    • 84859504173 scopus 로고    scopus 로고
    • Induction of thioredoxin-interacting protein is mediated by oxidative stress, calcium, and glucose after brain injury in mice
    • G. S. Kim, J. E. Jung, P. Narasimhan, H. Sakata, and P. H. Chan, "Induction of thioredoxin-interacting protein is mediated by oxidative stress, calcium, and glucose after brain injury in mice," Neurobiology of Disease, vol. 46, no. 2, pp. 440-449, 2012.
    • (2012) Neurobiology of Disease , vol.46 , Issue.2 , pp. 440-449
    • Kim, G.S.1    Jung, J.E.2    Narasimhan, P.3    Sakata, H.4    Chan, P.H.5
  • 185
    • 84864682160 scopus 로고    scopus 로고
    • IREla induces thioredoxin-interacting protein to activate the NLRP3 inflammasome and promote programmed cell death under irremediable ER stress
    • A. G Lerner, J. P. Upton, P. V. K. Praveen et al., "IREla induces thioredoxin-interacting protein to activate the NLRP3 inflammasome and promote programmed cell death under irremediable ER stress," Cell Metabolism, vol. 16, no. 2, pp. 250-264, 2012.
    • (2012) Cell Metabolism , vol.16 , Issue.2 , pp. 250-264
    • Lerner, A.G.1    Upton, J.P.2    Praveen, P.V.K.3
  • 186
    • 33745297834 scopus 로고    scopus 로고
    • Glucose-dependent transcriptional regulation by an evolutionarily conserved glucose-sensing module
    • M. V. Li, B. Chang, M. Imamura, N. Poungvarin, and L. Chan, "Glucose-dependent transcriptional regulation by an evolutionarily conserved glucose-sensing module," Diabetes, vol. 55, no. 5, pp. 1179-1189, 2006.
    • (2006) Diabetes , vol.55 , Issue.5 , pp. 1179-1189
    • Li, M.V.1    Chang, B.2    Imamura, M.3    Poungvarin, N.4    Chan, L.5
  • 187
    • 77954078084 scopus 로고    scopus 로고
    • Tandem ChoRE and CCAAT motifs and associated factors regulate txnip expression in response to glucose or adenosine-containing molecules
    • F.-X Yu and Y Luo, "Tandem ChoRE and CCAAT motifs and associated factors regulate txnip expression in response to glucose or adenosine-containing molecules," PLoS ONE, vol. 4, no. 12, Article ID e8397, 2009.
    • (2009) PLoS ONE , vol.4 , Issue.12
    • Yu, F.-X.1    Luo, Y.2
  • 188
    • 84924608502 scopus 로고    scopus 로고
    • TXNIP, the major player in insulin resistance, is early over-expressed in the brain of the 5XFAD Alzheimer's mice model and is induced by Aβ in vitro: Emerging role of TXNIP and inflammation in Alzheimer's Disease progression
    • T. Gouget, M. Djelloul, J. Boucraut et al., "TXNIP, the major player in insulin resistance, is early over-expressed in the brain of the 5XFAD Alzheimer's mice model and is induced by Aβ in vitro: emerging role of TXNIP and inflammation in Alzheimer's Disease progression," Alzheimer's & Dementia, vol. 7, no. 4, p. S684, 2011.
    • (2011) Alzheimer's & Dementia , vol.7 , Issue.4 , pp. S684
    • Gouget, T.1    Djelloul, M.2    Boucraut, J.3
  • 189
    • 84907434718 scopus 로고    scopus 로고
    • The transcription factor X-box binding protein-1 in neurodegenerative diseases
    • J. Dunys, E. Duplan, and F. Checler, "The transcription factor X-box binding protein-1 in neurodegenerative diseases," Molecular Neurodegeneration, vol. 9, no. 1, article 35, 2014.
    • (2014) Molecular Neurodegeneration , vol.9 , Issue.1
    • Dunys, J.1    Duplan, E.2    Checler, F.3
  • 190
    • 84901022639 scopus 로고    scopus 로고
    • Reduced IRE1 mediates apoptotic cell death by disrupting calcium homeostasis via the InsP3 receptor
    • S. M. Son, J. Byun, S.-E. Roh, S. J. Kim, and I. Mook-Jung, "Reduced IRE1 mediates apoptotic cell death by disrupting calcium homeostasis via the InsP3 receptor," Cell Death and Disease, vol. 5, no. 4, Article ID e1188, 2014.
    • (2014) Cell Death and Disease , vol.5 , Issue.4
    • Son, S.M.1    Byun, J.2    Roh, S.-E.3    Kim, S.J.4    Mook-Jung, I.5
  • 191
    • 0035871641 scopus 로고    scopus 로고
    • Stimulation of beta-amyloid precursor protein trafficking by insulin reduces intra-neuronal beta-amyloid and requires mitogen-activated protein kinase signaling
    • L. Gasparini, G. K. Gouras, R. Wang et al., "Stimulation of beta-amyloid precursor protein trafficking by insulin reduces intra-neuronal beta-amyloid and requires mitogen-activated protein kinase signaling," The journal of Neuroscience, vol. 21, no. 8, pp. 2561-2570, 2001.
    • (2001) The Journal of Neuroscience , vol.21 , Issue.8 , pp. 2561-2570
    • Gasparini, L.1    Gouras, G.K.2    Wang, R.3
  • 192
    • 9144223132 scopus 로고    scopus 로고
    • Mechanisms of soluble beta-amyloid impairment of endothelial function
    • M. T. Gentile, C. Vecchione, A. Maffei et al., "Mechanisms of soluble beta-amyloid impairment of endothelial function," The journal of Biological Chemistry, vol. 279, no. 46, pp. 48135-48142, 2004.
    • (2004) The Journal of Biological Chemistry , vol.279 , Issue.46 , pp. 48135-48142
    • Gentile, M.T.1    Vecchione, C.2    Maffei, A.3
  • 193
    • 84903458925 scopus 로고    scopus 로고
    • The role of endoplasmic reticulum in amyloid precursor protein processing and trafficking: Implications for Alzheimer's disease
    • A. I. Placido, C. M. F. Pereira, A. I. Duarte et al, "The role of endoplasmic reticulum in amyloid precursor protein processing and trafficking: implications for Alzheimer's disease," Biochimica et Biophysica Acta, vol. 1842, no. 9, pp. 1444-1453, 2014.
    • (2014) Biochimica et Biophysica Acta , vol.1842 , Issue.9 , pp. 1444-1453
    • Placido, A.I.1    Pereira, C.M.F.2    Duarte, A.I.3
  • 194
    • 84871797522 scopus 로고    scopus 로고
    • 2+ is a danger signal activating the NLRP3 inflammasome through G protein-coupled calcium sensing receptors
    • 2+ is a danger signal activating the NLRP3 inflammasome through G protein-coupled calcium sensing receptors," Nature Communications, vol. 3, article 2339, 2012.
    • (2012) Nature Communications , vol.3
    • Rossol, M.1    Pierer, M.2    Rauhen, N.3
  • 195
    • 1842738222 scopus 로고    scopus 로고
    • Kinetics of the neuroin-flammation-oxidative stress correlation in rat brain following the injection of fibrillar amyloid-beta onto the hippocampus in vivo
    • S. Rosales-Corral, D. X Tan, R. J. Reiter, M. Valdivia-Velázquez, J. P. Acosta-Martínez, and G G. Ortiz, "Kinetics of the neuroin-flammation-oxidative stress correlation in rat brain following the injection of fibrillar amyloid-beta onto the hippocampus in vivo," journal of Neuroimmunology, vol. 150, no. 1-2, pp. 20-28, 2004.
    • (2004) Journal of Neuroimmunology , vol.150 , Issue.1-2 , pp. 20-28
    • Rosales-Corral, S.1    Tan, D.X.2    Reiter, R.J.3    Valdivia-Velázquez, M.4    Acosta-Martínez, J.P.5    Ortiz, G.G.6
  • 197
    • 84872014417 scopus 로고    scopus 로고
    • Nlrp3 inflammasome activation in type 2 diabetes: Is it clinically relevant?
    • V. D. Dixit, "Nlrp3 inflammasome activation in type 2 diabetes: is it clinically relevant?" Diabetes, vol. 62, no. 1, pp. 22-24, 2013.
    • (2013) Diabetes , vol.62 , Issue.1 , pp. 22-24
    • Dixit, V.D.1
  • 198
    • 79751512463 scopus 로고    scopus 로고
    • The NLRP3 inflammasome instigates obesity-induced inflammation and insulin resistance
    • B. Vandanmagsar, Y.-H. Youm, A. Ravussin et al., "The NLRP3 inflammasome instigates obesity-induced inflammation and insulin resistance," Nature Medicine, vol. 17, no. 2, pp. 179-189, 2011.
    • (2011) Nature Medicine , vol.17 , Issue.2 , pp. 179-189
    • Vandanmagsar, B.1    Youm, Y.-H.2    Ravussin, A.3
  • 200
    • 32944470765 scopus 로고    scopus 로고
    • Cryopyrin activates the inflammasome in response to toxins and ATP
    • S. Mariathasan, D S. Weiss, K. Newton et al., "Cryopyrin activates the inflammasome in response to toxins and ATP," Nature, vol. 440, no. 7081, pp. 228-232, 2006.
    • (2006) Nature , vol.440 , Issue.7081 , pp. 228-232
    • Mariathasan, S.1    Weiss, D.S.2    Newton, K.3
  • 201
    • 47849085872 scopus 로고    scopus 로고
    • The NALP3 inflammasome is involved in the innate immune response to amyloid-beta
    • A. Halle, V. Hornung, G C. Petzold et al., "The NALP3 inflammasome is involved in the innate immune response to amyloid-beta," Nature Immunology, vol. 9, no. 8, pp. 857-865, 2008.
    • (2008) Nature Immunology , vol.9 , Issue.8 , pp. 857-865
    • Halle, A.1    Hornung, V.2    Petzold, G.C.3
  • 203
    • 70350365853 scopus 로고    scopus 로고
    • NADPH oxidase mediates beta-amyloid peptide-induced activation of ERK in hippocampal organotypic cultures
    • E Serrano, A. Chang, C. Hernandez, R. G Pautler, J. D. Sweatt, and E. Klann, "NADPH oxidase mediates beta-amyloid peptide-induced activation of ERK in hippocampal organotypic cultures," Molecular Brain, vol. 2, no. 1, article 31, 2009.
    • (2009) Molecular Brain , vol.2 , Issue.1
    • Serrano, E.1    Chang, A.2    Hernandez, C.3    Pautler, R.G.4    Sweatt, J.D.5    Klann, E.6
  • 204
    • 33845768784 scopus 로고    scopus 로고
    • Microglia-mediated neurotoxicity: Uncovering the molecular mechanisms
    • M. L. Block, L. Zecca, and J.-S. Hong, "Microglia-mediated neurotoxicity: uncovering the molecular mechanisms," Nature Reviews Neuroscience, vol. 8, no. 1, pp. 57-69, 2007
    • (2007) Nature Reviews Neuroscience , vol.8 , Issue.1 , pp. 57-69
    • Block, M.L.1    Zecca, L.2    Hong, J.-S.3
  • 205
    • 33846460101 scopus 로고    scopus 로고
    • Receptor for advanced glycation end products activation injures primary sensory neurons via oxidative stress
    • A. M. Vincent, L. Perrone, K. A. Sullivan et al., "Receptor for advanced glycation end products activation injures primary sensory neurons via oxidative stress," Endocrinology, vol. 148, no. 2, pp. 548-558, 2007
    • (2007) Endocrinology , vol.148 , Issue.2 , pp. 548-558
    • Vincent, A.M.1    Perrone, L.2    Sullivan, K.A.3
  • 206
    • 84896884534 scopus 로고    scopus 로고
    • Increased expression of the receptor for advanced glycation end products in neurons and astrocytes in a triple transgenic mouse model of Alzheimer's disease
    • B. R. Choi, W. H. Cho, J. Kim et al., "Increased expression of the receptor for advanced glycation end products in neurons and astrocytes in a triple transgenic mouse model of Alzheimer's disease," Experimental and Molecular Medicine, vol. 46, article e75, 2014.
    • (2014) Experimental and Molecular Medicine , vol.46
    • Choi, B.R.1    Cho, W.H.2    Kim, J.3
  • 207
    • 0013615899 scopus 로고    scopus 로고
    • RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
    • S. D. Yan, X. Chen, J. Fu et al, "RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease," Nature, vol. 382, no. 6593, pp. 685-691, 1996.
    • (1996) Nature , vol.382 , Issue.6593 , pp. 685-691
    • Yan, S.D.1    Chen, X.2    Fu, J.3
  • 208
    • 0032720953 scopus 로고    scopus 로고
    • The role of oxidative stress and NF-κB activation in late diabetic complications
    • A. K. Mohamed, A. Bierhaus, S. Schiekofer, H. Tritschler, R. Ziegler, and P. P. Nawroth, "The role of oxidative stress and NF-κB activation in late diabetic complications," BioFactors, vol. 10, no. 2-3, pp. 157-167, 1999.
    • (1999) BioFactors , vol.10 , Issue.2-3 , pp. 157-167
    • Mohamed, A.K.1    Bierhaus, A.2    Schiekofer, S.3    Tritschler, H.4    Ziegler, R.5    Nawroth, P.P.6
  • 209
    • 0028068046 scopus 로고
    • Cellular receptors for advanced glycation end products. Implications for induction of oxidant stress and cellular dysfunction in the pathogenesis of vascular lesions
    • A. M. Schmidt, O. Hori, J. Brett, S. D. Yan, J.-L. Wautier, and D. Stern, "Cellular receptors for advanced glycation end products. Implications for induction of oxidant stress and cellular dysfunction in the pathogenesis of vascular lesions," Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 14, no. 10, pp. 1521-1528, 1994.
    • (1994) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.14 , Issue.10 , pp. 1521-1528
    • Schmidt, A.M.1    Hori, O.2    Brett, J.3    Yan, S.D.4    Wautier, J.-L.5    Stern, D.6
  • 210
    • 12744279326 scopus 로고    scopus 로고
    • Redox paradox: Insulin action is facilitated by insulin-stimulated reactive oxygen species with multiple potential signaling targets
    • B. J. Goldstein, M. Kalyankar, and X Wu, "Redox paradox: insulin action is facilitated by insulin-stimulated reactive oxygen species with multiple potential signaling targets," Diabetes, vol. 54, no. 2, pp. 311-321, 2005.
    • (2005) Diabetes , vol.54 , Issue.2 , pp. 311-321
    • Goldstein, B.J.1    Kalyankar, M.2    Wu, X.3
  • 211
    • 0035877633 scopus 로고    scopus 로고
    • Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase lb in vivo and enhances the early insulin action cascade
    • K. Mahadev, A. Zilbering, L. Zhu, and B. J. Goldstein, "Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase lb in vivo and enhances the early insulin action cascade," The journal of Biological Chemistry, vol. 276, no. 24, pp. 21938-21942, 2001.
    • (2001) The Journal of Biological Chemistry , vol.276 , Issue.24 , pp. 21938-21942
    • Mahadev, K.1    Zilbering, A.2    Zhu, L.3    Goldstein, B.J.4
  • 212
    • 33750028310 scopus 로고    scopus 로고
    • Regulation of acetylcholinesterase expression by calcium signaling during calcium ionophore A2
    • H. Zhu, W. Gao, H. Jiang et al., "Regulation of acetylcholinesterase expression by calcium signaling during calcium ionophore A2," The International journal of Biochemistry & Cell Biology, vol. 39, pp. 93-108, 2007
    • (2007) The International Journal of Biochemistry & Cell Biology , vol.39 , pp. 93-108
    • Zhu, H.1    Gao, W.2    Jiang, H.3
  • 213
    • 0027491242 scopus 로고
    • Regulated and constitutive secretion of distinct molecular forms of acetylcholinesterase from PC12 cells
    • E. S. Schweitzer, "Regulated and constitutive secretion of distinct molecular forms of acetylcholinesterase from PC12 cells," journal of Cell Science, vol. 106, no. 3, pp. 731-740, 1993.
    • (1993) Journal of Cell Science , vol.106 , Issue.3 , pp. 731-740
    • Schweitzer, E.S.1
  • 214
    • 1842375103 scopus 로고    scopus 로고
    • The amyloid beta-protein of Alzheimer's disease increases acetylcholinesterase expression by increasing intracellular calcium in embryonal carcinoma P19 cells
    • G. Sberna, J. Sáez-Valero, K. Beyreuther, C. L. Masters, and D. H. Small, "The amyloid beta-protein of Alzheimer's disease increases acetylcholinesterase expression by increasing intracellular calcium in embryonal carcinoma P19 cells," journal of Neurochemistry, vol. 69, no. 3, pp. 1177-1184, 1997
    • (1997) Journal of Neurochemistry , vol.69 , Issue.3 , pp. 1177-1184
    • Sberna, G.1    Sáez-Valero, J.2    Beyreuther, K.3    Masters, C.L.4    Small, D.H.5
  • 215
    • 0026570528 scopus 로고
    • Beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • M. P. Mattson, B. Cheng, D Davis, K. Bryant, I. Lieberburg, and R. E. Rydel, "beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity," The journal of Neuroscience, vol. 12, no. 2, pp. 376-389, 1992.
    • (1992) The Journal of Neuroscience , vol.12 , Issue.2 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 216
    • 0037198403 scopus 로고    scopus 로고
    • A non-cholinergic, trophic action of acetylcholinesterase on hippocampal neurones in vitro: Molecular mechanisms
    • T. Day and S. A. Greenfield, "A non-cholinergic, trophic action of acetylcholinesterase on hippocampal neurones in vitro: molecular mechanisms," Neuroscience, vol. 111, no. 3, pp. 649-656, 2002.
    • (2002) Neuroscience , vol.111 , Issue.3 , pp. 649-656
    • Day, T.1    Greenfield, S.A.2
  • 217
    • 47649127364 scopus 로고    scopus 로고
    • 2+ mobilization and glutamate exocytosis in cerebral synap-tosomes from mice
    • 2+ mobilization and glutamate exocytosis in cerebral synap-tosomes from mice," Diabetes Research and Clinical Practice, vol. 81, no. 2, pp. el4-el7, 2008.
    • (2008) Diabetes Research and Clinical Practice , vol.81 , Issue.2 , pp. el4-el7
    • Satoh, E.1    Takahashi, A.2
  • 219
    • 0034745636 scopus 로고    scopus 로고
    • Neurotoxic Abeta peptides increase oxidative stress in vivo through NMDA-receptor and nitric-oxide-synthase mechanisms, and inhibit complex IV activity and induce a mitochondrial permeability transition in vitro
    • J. K. Parks, T. S. Smith, P. A. Trimmer, J. P. Bennett Jr., and W. J. Davis Parker, "Neurotoxic Abeta peptides increase oxidative stress in vivo through NMDA-receptor and nitric-oxide-synthase mechanisms, and inhibit complex IV activity and induce a mitochondrial permeability transition in vitro," Journal of Neurochemistry, vol. 76, no. 4, pp. 1050-1056, 2001.
    • (2001) Journal of Neurochemistry , vol.76 , Issue.4 , pp. 1050-1056
    • Parks, J.K.1    Smith, T.S.2    Trimmer, P.A.3    Bennett, J.P.4    Davis Parker, W.J.5
  • 221
    • 15444339756 scopus 로고    scopus 로고
    • Brain insulin and insulin receptors in aging and sporadic Alzheimer's disease
    • L. Frölich, D. Blum-Degen, H.-G Bernstein et al., "Brain insulin and insulin receptors in aging and sporadic Alzheimer's disease," Journal of Neural Transmission, vol. 105, no. 4-5, pp. 423-438, 1998.
    • (1998) Journal of Neural Transmission , vol.105 , Issue.4-5 , pp. 423-438
    • Frölich, L.1    Blum-Degen, D.2    Bernstein, H.-G.3
  • 222
    • 70349581633 scopus 로고    scopus 로고
    • Insulin resistance and Alzheimer's disease
    • S. M. de la Monte, "Insulin resistance and Alzheimer's disease," BMB Reports, vol. 42, no. 8, pp. 475-481, 2009.
    • (2009) BMB Reports , vol.42 , Issue.8 , pp. 475-481
    • De La Monte, S.M.1
  • 223
    • 60349128460 scopus 로고    scopus 로고
    • A study of brain insulin receptors, AChE activity and oxidative stress in rat model of ICV STZ induced dementia
    • R. Agrawal, E. Tyagi, R. Shukla, and G Nath, "A study of brain insulin receptors, AChE activity and oxidative stress in rat model of ICV STZ induced dementia," Neuropharmacology, vol. 56, no. 4, pp. 779-787, 2009.
    • (2009) Neuropharmacology , vol.56 , Issue.4 , pp. 779-787
    • Agrawal, R.1    Tyagi, E.2    Shukla, R.3    Nath, G.4
  • 226
    • 0033537830 scopus 로고    scopus 로고
    • Oxidative stress disrupts insulin-induced cellular redistribution of insulin receptor substrate-1 and phosphatidylinositol 3-kinase in 3T3-L1 adipocytes. A putative cellular mechanism for impaired protein kinase B activation and GLUT4 translocation
    • A. Tirosh, R. Potashnik, N. Bashan, and A. Rudich, "Oxidative stress disrupts insulin-induced cellular redistribution of insulin receptor substrate-1 and phosphatidylinositol 3-kinase in 3T3-L1 adipocytes. A putative cellular mechanism for impaired protein kinase B activation and GLUT4 translocation," The Journal of Biological Chemistry, vol. 274, no. 15, pp. 10595-10602, 1999.
    • (1999) The Journal of Biological Chemistry , vol.274 , Issue.15 , pp. 10595-10602
    • Tirosh, A.1    Potashnik, R.2    Bashan, N.3    Rudich, A.4
  • 227
    • 77957229010 scopus 로고    scopus 로고
    • Insulin signaling meets mitochondria in metabolism
    • Z. Cheng, Y. Tseng, and M. E White, "Insulin signaling meets mitochondria in metabolism," Trends in Endocrinology and Metabolism, vol. 21, no. 10, pp. 589-598, 2010.
    • (2010) Trends in Endocrinology and Metabolism , vol.21 , Issue.10 , pp. 589-598
    • Cheng, Z.1    Tseng, Y.2    White, E.M.3
  • 228
    • 0036715628 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase 1B inhibitors for diabetes
    • T. O. Johnson, J. Ermolieff, and M. R. Jirousek, "Protein tyrosine phosphatase 1B inhibitors for diabetes," Nature Reviews Drug Discovery, vol. 1, no. 9, pp. 696-709, 2002.
    • (2002) Nature Reviews Drug Discovery , vol.1 , Issue.9 , pp. 696-709
    • Johnson, T.O.1    Ermolieff, J.2    Jirousek, M.R.3
  • 230
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation
    • J. M. Denu and K. G. Tanner, "Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation," Biochemistry, vol. 37, no. 16, pp. 5633-5642, 1998.
    • (1998) Biochemistry , vol.37 , Issue.16 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 231
    • 0028979464 scopus 로고
    • Crystal structure of the Cys2 activator-binding domain of protein kinase CΔ in complex with phorbol ester
    • G. Zhang, M. G. Kazanietz, P. M. Blumberg, and J. H. Hurley, "Crystal structure of the Cys2 activator-binding domain of protein kinase CΔ in complex with phorbol ester," Cell, vol. 81, no. 6, pp. 917-924, 1995.
    • (1995) Cell , vol.81 , Issue.6 , pp. 917-924
    • Zhang, G.1    Kazanietz, M.G.2    Blumberg, P.M.3    Hurley, J.H.4
  • 232
    • 30344460004 scopus 로고    scopus 로고
    • Redox regulation of cardiac protein kinase C
    • I. Korichneva, "Redox regulation of cardiac protein kinase C," Experimental and Clinical Cardiology, vol. 10, no. 4, pp. 256-261, 2005.
    • (2005) Experimental and Clinical Cardiology , vol.10 , Issue.4 , pp. 256-261
    • Korichneva, I.1
  • 235
    • 0034705402 scopus 로고    scopus 로고
    • Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone
    • S. Barbirz, U. Jakob, and M. O. Glocker, "Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone," The Journal of Biological Chemistry, vol. 275, no. 25, pp. 18759-18766, 2000.
    • (2000) The Journal of Biological Chemistry , vol.275 , Issue.25 , pp. 18759-18766
    • Barbirz, S.1    Jakob, U.2    Glocker, M.O.3
  • 236
    • 0034190297 scopus 로고    scopus 로고
    • Protein kinase C signaling and oxidative stress
    • R. Gopalakrishna and S. Jaken, "Protein kinase C signaling and oxidative stress," Tree Radical Biology and Medicine, vol. 28, no. 9, pp. 1349-1361, 2000.
    • (2000) Tree Radical Biology and Medicine , vol.28 , Issue.9 , pp. 1349-1361
    • Gopalakrishna, R.1    Jaken, S.2
  • 237
    • 0034903753 scopus 로고    scopus 로고
    • Potent inactivation of representative members of each PKC isozyme subfamily and PKD via S-thiolation by the tumor-promotion/progression antagonist glutathione but not by its precursor cysteine
    • F. Chu, N. E. Ward, and G A. O'Brian, "Potent inactivation of representative members of each PKC isozyme subfamily and PKD via S-thiolation by the tumor-promotion/progression antagonist glutathione but not by its precursor cysteine," Carcinogenesis, vol. 22, no. 8, pp. 1221-1229, 2001.
    • (2001) Carcinogenesis , vol.22 , Issue.8 , pp. 1221-1229
    • Chu, F.1    Ward, N.E.2    O'Brian, G.A.3
  • 238
    • 0035941358 scopus 로고    scopus 로고
    • Regulation of vascular endothelial growth factor expression by advanced glycation end products
    • C. Treins, S. Giorgetti-Peraldi, J. Murdaca, and E. Van Obberghen, "Regulation of vascular endothelial growth factor expression by advanced glycation end products," The Journal of Biological Chemistry, vol. 276, no. 47, pp. 43836-43841, 2001.
    • (2001) The Journal of Biological Chemistry , vol.276 , Issue.47 , pp. 43836-43841
    • Treins, C.1    Giorgetti-Peraldi, S.2    Murdaca, J.3    Van Obberghen, E.4
  • 239
    • 17144369501 scopus 로고    scopus 로고
    • Oxidative activation of protein kinase Cgamma through the C1 domain. Effects on gap junctions
    • D. Lin and D. J. Takemoto, "Oxidative activation of protein kinase Cgamma through the C1 domain. Effects on gap junctions," Journal of Biological Chemistry, vol. 280, no. 14, pp. 13682-13693, 2005.
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 13682-13693
    • Lin, D.1    Takemoto, D.J.2
  • 240
    • 14644444082 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications: A unifying mechanism
    • D. LeRoith, S. I. Taylor, and J. M. Olefsky, Eds. Lippincott Williams & Wilkins, Philadelphia, Pa, USA
    • S. Hofmann and M. Brownlee, "Biochemistry and molecular cell biology of diabetic complications: a unifying mechanism," in Diabetes Mellitus: A Tundamental and Clinical Text, D. LeRoith, S. I. Taylor, and J. M. Olefsky, Eds., pp. 1441-14457, Lippincott Williams & Wilkins, Philadelphia, Pa, USA, 2004.
    • (2004) Diabetes Mellitus: A Tundamental and Clinical Text , pp. 1441-14457
    • Hofmann, S.1    Brownlee, M.2
  • 241
    • 0038187674 scopus 로고    scopus 로고
    • GSK-3α regulates production of Alzheimer's disease amyloid-β peptides
    • C. J. Phiel, C. A. Wilson, V. M.-Y Lee, and P. S. Klein, "GSK-3α regulates production of Alzheimer's disease amyloid-β peptides," Nature, vol. 423, no. 6938, pp. 435-439, 2003.
    • (2003) Nature , vol.423 , Issue.6938 , pp. 435-439
    • Phiel, C.J.1    Wilson, C.A.2    Lee, V.M.-Y.3    Klein, P.S.4
  • 244
    • 26844541999 scopus 로고    scopus 로고
    • Melatonin precludes cytoskeletal collapse caused by hydrogen peroxide: Participation of protein kinase C
    • G. Benitez-King, L. Ortiz-López, and G. Jiménez-Rubio, "Melatonin precludes cytoskeletal collapse caused by hydrogen peroxide: participation of protein kinase C," Therapy, vol. 2, no. 5, pp. 767-778, 2005.
    • (2005) Therapy , vol.2 , Issue.5 , pp. 767-778
    • Benitez-King, G.1    Ortiz-López, L.2    Jiménez-Rubio, G.3
  • 245
    • 84875441025 scopus 로고    scopus 로고
    • Sodium phenylbutyrate enhances astrocytic neurotrophin synthesis via protein kinase C (PKC)-mediated activation of cAMP-response element-binding protein (CREB): Implications for alzheimer disease therapy
    • G. T. Corbett, A. Roy, and K. Pahan, "Sodium phenylbutyrate enhances astrocytic neurotrophin synthesis via protein kinase C (PKC)-mediated activation of cAMP-response element-binding protein (CREB): implications for alzheimer disease therapy," The Journal of Biological Chemistry, vol. 288, no. 12, pp. 8299-8312, 2013.
    • (2013) The Journal of Biological Chemistry , vol.288 , Issue.12 , pp. 8299-8312
    • Corbett, G.T.1    Roy, A.2    Pahan, K.3
  • 246
    • 23844459902 scopus 로고    scopus 로고
    • Prolonged Alzheimer-like tau hyperphosphorylation induced by simultaneous inhibition of phosphoinositol-3 kinase and protein kinase C in N2a cells
    • G.-G. Xu, Y.-Q. Deng, S.-J. Liu, H.-L. Li, and J.-Z. Wang, "Prolonged Alzheimer-like tau hyperphosphorylation induced by simultaneous inhibition of phosphoinositol-3 kinase and protein kinase C in N2a cells," Acta Biochimica et Biophysica Sinica, vol. 37, no. 5, pp. 349-354, 2005.
    • (2005) Acta Biochimica et Biophysica Sinica , vol.37 , Issue.5 , pp. 349-354
    • Xu, G.-G.1    Deng, Y.-Q.2    Liu, S.-J.3    Li, H.-L.4    Wang, J.-Z.5
  • 247
    • 0025992927 scopus 로고
    • Action of amyloid beta-protein on protein kinase C activity
    • A. Chauhan, V. P. S. Chauhan, H. Brockerhoff, and H. M. Wisniewski, "Action of amyloid beta-protein on protein kinase C activity," Life Sciences, vol. 49, no. 21, pp. 1555-1562, 1991.
    • (1991) Life Sciences , vol.49 , Issue.21 , pp. 1555-1562
    • Chauhan, A.1    Chauhan, V.P.S.2    Brockerhoff, H.3    Wisniewski, H.M.4
  • 249
    • 84891885282 scopus 로고    scopus 로고
    • Brain atrophy in type 2 diabetes: Regional distribution and influence on cognition
    • C. Moran, T. G. Phan, J. Chen et al., "Brain atrophy in type 2 diabetes: regional distribution and influence on cognition," Diabetes Care, vol. 36, no. 12, pp. 4036-4042, 2013.
    • (2013) Diabetes Care , vol.36 , Issue.12 , pp. 4036-4042
    • Moran, C.1    Phan, T.G.2    Chen, J.3
  • 250
    • 84863940277 scopus 로고    scopus 로고
    • Protein kinase C and tolllike receptor signaling
    • D. J. Loegering and M. R. Lennartz, "Protein kinase C and tolllike receptor signaling," Enzyme Research, vol. 2011, no. 1, Article ID 537821, 2011.
    • (2011) Enzyme Research , vol.2011 , Issue.1
    • Loegering, D.J.1    Lennartz, M.R.2
  • 251
    • 43549087343 scopus 로고    scopus 로고
    • Insulin neuroprotection against oxidative stress is mediated by Akt and GSK-3beta signaling pathways and changes in protein expression
    • A. I. Duarte, P. Santos, C. R. Oliveira, M. S. Santos, and A. C. Rego, "Insulin neuroprotection against oxidative stress is mediated by Akt and GSK-3beta signaling pathways and changes in protein expression," Biochimica et Biophysica Acta-Molecular Cell Research, vol. 1783, no. 6, pp. 994-1002, 2008.
    • (2008) Biochimica et Biophysica Acta-Molecular Cell Research , vol.1783 , Issue.6 , pp. 994-1002
    • Duarte, A.I.1    Santos, P.2    Oliveira, C.R.3    Santos, M.S.4    Rego, A.C.5
  • 252
    • 77749336528 scopus 로고    scopus 로고
    • Amyloid-β neurotoxicity in organotypic culture is attenuated by melatonin: Involvement of GSK-3β, tau and neuroinflammation
    • J. B. Hoppe, R. L. Frozza, A. P. Horn et al., "Amyloid-β neurotoxicity in organotypic culture is attenuated by melatonin: involvement of GSK-3β, tau and neuroinflammation," Journal of Pineal Research, vol. 48, no. 3, pp. 230-238, 2010.
    • (2010) Journal of Pineal Research , vol.48 , Issue.3 , pp. 230-238
    • Hoppe, J.B.1    Frozza, R.L.2    Horn, A.P.3
  • 253
    • 65249113325 scopus 로고    scopus 로고
    • The insulin/Akt signaling pathway is targeted by intracellular beta-amyloid
    • H. K. Lee, P. Kumar, Q. Fu, K. M. Rosen, and H. W. Querfurth, "The insulin/Akt signaling pathway is targeted by intracellular beta-amyloid," Molecular Biology of the Cell, vol. 20, no. 5, pp. 1533-1544, 2009.
    • (2009) Molecular Biology of the Cell , vol.20 , Issue.5 , pp. 1533-1544
    • Lee, H.K.1    Kumar, P.2    Fu, Q.3    Rosen, K.M.4    Querfurth, H.W.5
  • 254
    • 60549084867 scopus 로고    scopus 로고
    • Protection of synapses against Alzheimer's-linked toxins: Insulin signaling prevents the pathogenic binding of Aβ oligomers
    • F. G. de Felice, M. N. N. Vieira, T. R. Bomfim et al., "Protection of synapses against Alzheimer's-linked toxins: insulin signaling prevents the pathogenic binding of Aβ oligomers," Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 6, pp. 1971-1976, 2009.
    • (2009) Proceedings of the National Academy of Sciences of the United States of America , vol.106 , Issue.6 , pp. 1971-1976
    • De Felice, F.G.1    Vieira, M.N.N.2    Bomfim, T.R.3
  • 255
    • 71349085957 scopus 로고    scopus 로고
    • Defects in IGF-1 receptor, insulin receptor and IRS-1/2 in Alzheimer's disease indicate possible resistance to IGF-1 and insulin signalling
    • A. M. Moloney, R. J. Griffin, S. Timmons, R. O'Connor, R. Ravid, and G O'Neill, "Defects in IGF-1 receptor, insulin receptor and IRS-1/2 in Alzheimer's disease indicate possible resistance to IGF-1 and insulin signalling," Neurobiology of Aging, vol. 31, no. 2, pp. 224-243, 2010.
    • (2010) Neurobiology of Aging , vol.31 , Issue.2 , pp. 224-243
    • Moloney, A.M.1    Griffin, R.J.2    Timmons, S.3    O'Connor, R.4    Ravid, R.5    O'Neill, G.6
  • 256
    • 4644286910 scopus 로고    scopus 로고
    • Diet-induced insulin resistance promotes amyloidosis in a transgenic mouse model of Alzheimer's disease
    • L. Ho, W. Qin, P. N. Pompl et al., "Diet-induced insulin resistance promotes amyloidosis in a transgenic mouse model of Alzheimer's disease," The FASEB Journal, vol. 18, no. 7, pp. 902-904, 2004.
    • (2004) The FASEB Journal , vol.18 , Issue.7 , pp. 902-904
    • Ho, L.1    Qin, W.2    Pompl, P.N.3
  • 257
    • 0037390039 scopus 로고    scopus 로고
    • Insulin-degrading enzyme regulates the levels of insulin, amyloid beta-protein, and the beta-amyloid precursor protein intracellular domain in vivo
    • W. Farris, S. Mansourian, Y. Chang et al., "Insulin-degrading enzyme regulates the levels of insulin, amyloid beta-protein, and the beta-amyloid precursor protein intracellular domain in vivo," Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 7, pp. 4162-4167, 2003.
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.7 , pp. 4162-4167
    • Farris, W.1    Mansourian, S.2    Chang, Y.3
  • 258
    • 0028176821 scopus 로고
    • Alzheimer's β-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme
    • I. V. Kurochkin and S. Goto, "Alzheimer's β-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme," FEBS Letters, vol. 345, no. 1, pp. 33-37, 1994.
    • (1994) FEBS Letters , vol.345 , Issue.1 , pp. 33-37
    • Kurochkin, I.V.1    Goto, S.2
  • 260
    • 79952935338 scopus 로고    scopus 로고
    • Redox regulation of insulin degradation by insulin-degrading enzyme
    • C. M. Cordes, R. G. Bennett, G. L. Siford, and F. G. Hamel, "Redox regulation of insulin degradation by insulin-degrading enzyme," PLoS ONE, vol. 6, no. 3, Article ID el8138, 2011.
    • (2011) PLoS ONE , vol.6 , Issue.3
    • Cordes, C.M.1    Bennett, R.G.2    Siford, G.L.3    Hamel, F.G.4
  • 261
    • 27944440133 scopus 로고    scopus 로고
    • Susceptibility of amyloid β peptide degrading enzymes to oxidative damage: A potential Alzheimer's disease spiral
    • H. Shinall, E. S. Song, and L. B. Hersh, "Susceptibility of amyloid β peptide degrading enzymes to oxidative damage: a potential Alzheimer's disease spiral," Biochemistry, vol. 44, no. 46, pp. 15345-15350, 2005.
    • (2005) Biochemistry , vol.44 , Issue.46 , pp. 15345-15350
    • Shinall, H.1    Song, E.S.2    Hersh, L.B.3
  • 262
    • 0018389336 scopus 로고
    • The effect of age on insulin-degrading activity in rat tissue
    • K. Runyan, W. C. Duckworth, A. E. Kitabchi, and G. Huff, "The effect of age on insulin-degrading activity in rat tissue," Diabetes, vol. 28, no. 4, pp. 324-325, 1979.
    • (1979) Diabetes , vol.28 , Issue.4 , pp. 324-325
    • Runyan, K.1    Duckworth, W.C.2    Kitabchi, A.E.3    Huff, G.4
  • 263
    • 0037900150 scopus 로고    scopus 로고
    • In vitro inhibition of insulin-degrading enzyme by long-chain fatty acids and their coenzyme A thioesters
    • F. G. Hamel, J. L. Upward, and R. G. Bennett, "In vitro inhibition of insulin-degrading enzyme by long-chain fatty acids and their coenzyme A thioesters," Endocrinology, vol. 144, no. 6, pp. 2404-2408, 2003.
    • (2003) Endocrinology , vol.144 , Issue.6 , pp. 2404-2408
    • Hamel, F.G.1    Upward, J.L.2    Bennett, R.G.3
  • 264
    • 84921614222 scopus 로고    scopus 로고
    • C allele of the rs2209972 single nucleotide polymorphism of the insulin degrading enzyme gene and Alzheimer's disease in type 2 diabetes, a case control study
    • H. Gutiérrez-Hermosillo, D. de León-Gonzáleze, R. Palacios-Corona et al., "C allele of the rs2209972 single nucleotide polymorphism of the insulin degrading enzyme gene and Alzheimer's disease in type 2 diabetes, a case control study," Medicina Clinica, vol. 144, no. 4, pp. 151-155, 2015.
    • (2015) Medicina Clinica , vol.144 , Issue.4 , pp. 151-155
    • Gutiérrez-Hermosillo, H.1    De León-Gonzáleze, D.2    Palacios-Corona, R.3
  • 265
    • 85047691537 scopus 로고    scopus 로고
    • Inhibition of GAPDH activity by poly(ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells
    • X. Du, T. Matsumura, D. Edelstein et al., "Inhibition of GAPDH activity by poly(ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells," The Journal of Clinical Investigation, vol. 112, no. 7, pp. 1049-1057, 2003.
    • (2003) The Journal of Clinical Investigation , vol.112 , Issue.7 , pp. 1049-1057
    • Du, X.1    Matsumura, T.2    Edelstein, D.3
  • 266
    • 70449712602 scopus 로고    scopus 로고
    • Novel roles for GAPDH in cell death and carcinogenesis
    • A. Colell, D. R. Green, and J.-E. Ricci, "Novel roles for GAPDH in cell death and carcinogenesis," Cell Death and Differentiation, vol. 16, no. 12, pp. 1573-1581, 2009.
    • (2009) Cell Death and Differentiation , vol.16 , Issue.12 , pp. 1573-1581
    • Colell, A.1    Green, D.R.2    Ricci, J.-E.3
  • 267
    • 2442693140 scopus 로고    scopus 로고
    • Nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase: A role in high glucose-induced apoptosis in retinal Müller cells
    • L. L. Kusner, V. P. Sarthy, and S. Mohr, "Nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase: a role in high glucose-induced apoptosis in retinal Müller cells," Investigative Ophthalmology and Visual Science, vol. 45, no. 5, pp. 1553-1561, 2004.
    • (2004) Investigative Ophthalmology and Visual Science , vol.45 , Issue.5 , pp. 1553-1561
    • Kusner, L.L.1    Sarthy, V.P.2    Mohr, S.3
  • 269
    • 77954497959 scopus 로고    scopus 로고
    • Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and alzheimer's disease: Many pathways to neurode-generation
    • D. A. Butterfield, S. S. Hardas, and M. L. B. Lange, "Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and alzheimer's disease: many pathways to neurode-generation," Journal of Alzheimer's Disease, vol. 20, no. 2, pp. 369-393, 2010.
    • (2010) Journal of Alzheimer's Disease , vol.20 , Issue.2 , pp. 369-393
    • Butterfield, D.A.1    Hardas, S.S.2    Lange, M.L.B.3
  • 270
    • 34248223082 scopus 로고    scopus 로고
    • An increase in S-glutathionylated proteins in the Alzheimer's disease inferior parietal lobule, a proteomics approach
    • S. F. Newman, R. Sultana, M. Perluigi et al., "An increase in S-glutathionylated proteins in the Alzheimer's disease inferior parietal lobule, a proteomics approach," Journal of Neuroscience Research, vol. 85, no. 7, pp. 1506-1514, 2007
    • (2007) Journal of Neuroscience Research , vol.85 , Issue.7 , pp. 1506-1514
    • Newman, S.F.1    Sultana, R.2    Perluigi, M.3
  • 271
    • 25844458239 scopus 로고    scopus 로고
    • Current advances on different kinases involved in tau phosphorylation, and implications in Alzheimer's disease and tauopathies
    • I. Ferrer, T. Gomez-Isla, B. Puig et al., "Current advances on different kinases involved in tau phosphorylation, and implications in Alzheimer's disease and tauopathies," Current Alzheimer Research, vol. 2, no. 1, pp. 3-18, 2005.
    • (2005) Current Alzheimer Research , vol.2 , Issue.1 , pp. 3-18
    • Ferrer, I.1    Gomez-Isla, T.2    Puig, B.3
  • 272
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - A visualization system for exploratory research and analysis
    • E. F. Pettersen, T. D. Goddard, C. C. Huang et al., "UCSF Chimera - a visualization system for exploratory research and analysis," Journal of Computational Chemistry, vol. 25, no. 13, pp. 1605-1612, 2004.
    • (2004) Journal of Computational Chemistry , vol.25 , Issue.13 , pp. 1605-1612
    • Pettersen, E.F.1    Goddard, T.D.2    Huang, C.C.3


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