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Volumn 9, Issue JUL, 2015, Pages

Cortical iron regulation and inflammatory response in Alzheimer's disease and APPSWE/PS1ΔE9 mice: A histological perspective

Author keywords

Alzheimer's disease; Amyloid beta plaques; APP PS1; Astrocyte; Ferritin; Histology; Iron; Microglia

Indexed keywords

AMYLOID BETA PROTEIN ANTIBODY; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; FERRITIN; IRON; PRESENILIN 1; THIOFLAVINE;

EID: 84938500229     PISSN: 16624548     EISSN: 1662453X     Source Type: Journal    
DOI: 10.3389/fnins.2015.00255     Document Type: Article
Times cited : (40)

References (82)
  • 1
    • 0032613038 scopus 로고    scopus 로고
    • Role of free radicals and metal ions in the pathogenesis of Alzheimer's disease
    • Atwood, C. S., Huang, X., Moir, R. D., Tanzi, R. E., and Bush, A. I. (1999). Role of free radicals and metal ions in the pathogenesis of Alzheimer's disease. Met. Ions Biol. Syst. 36, 309-364.
    • (1999) Met. Ions Biol. Syst , vol.36 , pp. 309-364
    • Atwood, C.S.1    Huang, X.2    Moir, R.D.3    Tanzi, R.E.4    Bush, A.I.5
  • 2
    • 57449119060 scopus 로고    scopus 로고
    • Physiological and pathological aspects of Abeta in iron homeostasis via 5'UTR in the APP mRNA and the therapeutic use of iron-chelators
    • Avramovich-Tirosh, Y., Amit, T., Bar-Am, O., Weinreb, O., and Youdim, M. B. (2008). Physiological and pathological aspects of Abeta in iron homeostasis via 5'UTR in the APP mRNA and the therapeutic use of iron-chelators. BMC Neurosci. 9(Suppl. 2):S2. doi: 10.1186/1471-2202-9-S2-S2.
    • (2008) BMC Neurosci , vol.9 , pp. S2
    • Avramovich-Tirosh, Y.1    Amit, T.2    Bar-Am, O.3    Weinreb, O.4    Youdim, M.B.5
  • 3
    • 84884852756 scopus 로고    scopus 로고
    • Metallostasis in Alzheimer's disease
    • Ayton, S., Lei, P., and Bush, A. I. (2013). Metallostasis in Alzheimer's disease. Free Radic. Biol. Med. 62, 76-89. doi: 10.1016/j.freeradbiomed.2012.10.558.
    • (2013) Free Radic. Biol. Med , vol.62 , pp. 76-89
    • Ayton, S.1    Lei, P.2    Bush, A.I.3
  • 4
    • 84896844669 scopus 로고    scopus 로고
    • Ceruloplasmin and beta-amyloid precursor protein confer neuroprotection in traumatic brain injury and lower neuronal iron
    • Ayton, S., Zhang, M., Roberts, B. R., Lam, L. Q., Lind, M., McLean, C., et al. (2014). Ceruloplasmin and beta-amyloid precursor protein confer neuroprotection in traumatic brain injury and lower neuronal iron. Free Radic. Biol. Med. 69, 331-337. doi: 10.1016/j.freeradbiomed.2014.01.041.
    • (2014) Free Radic. Biol. Med , vol.69 , pp. 331-337
    • Ayton, S.1    Zhang, M.2    Roberts, B.R.3    Lam, L.Q.4    Lind, M.5    McLean, C.6
  • 5
    • 0034802570 scopus 로고    scopus 로고
    • Immunological aspects of microglia: relevance to Alzheimer's disease
    • Benveniste, E. N., Nguyen, V. T., and O'Keefe, G. M. (2001). Immunological aspects of microglia: relevance to Alzheimer's disease. Neurochem. Int. 39, 381-391. doi: 10.1016/S0197-0186(01)00045-6.
    • (2001) Neurochem. Int , vol.39 , pp. 381-391
    • Benveniste, E.N.1    Nguyen, V.T.2    O'Keefe, G.M.3
  • 6
    • 0028873173 scopus 로고
    • Iron levels modulate alpha-secretase cleavage of amyloid precursor protein
    • Bodovitz, S., Falduto, M. T., Frail, D. E., and Klein, W. L. (1995). Iron levels modulate alpha-secretase cleavage of amyloid precursor protein. J. Neurochem. 64, 307-315. doi: 10.1046/j.1471-4159.1995.64010307.x.
    • (1995) J. Neurochem , vol.64 , pp. 307-315
    • Bodovitz, S.1    Falduto, M.T.2    Frail, D.E.3    Klein, W.L.4
  • 7
    • 0030499678 scopus 로고    scopus 로고
    • A vector for expressing foreign genes in the brains and hearts of transgenic mice
    • Borchelt, D. R., Davis, J., Fischer, M., Lee, M. K., Slunt, H. H., Ratovitsky, T., et al. (1996). A vector for expressing foreign genes in the brains and hearts of transgenic mice. Genet. Anal. 13, 159-163. doi: 10.1016/S1050-3862(96)00167-2.
    • (1996) Genet. Anal , vol.13 , pp. 159-163
    • Borchelt, D.R.1    Davis, J.2    Fischer, M.3    Lee, M.K.4    Slunt, H.H.5    Ratovitsky, T.6
  • 8
    • 0030833055 scopus 로고    scopus 로고
    • Accelerated amyloid deposition in the brains of transgenic mice coexpressing mutant presenilin 1 and amyloid precursor proteins
    • Borchelt, D. R., Ratovitski, T., van Lare, J., Lee, M. K., Gonzales, V., Jenkins, N. A., et al. (1997). Accelerated amyloid deposition in the brains of transgenic mice coexpressing mutant presenilin 1 and amyloid precursor proteins. Neuron 19, 939-945. doi: 10.1016/S0896-6273(00)80974-5.
    • (1997) Neuron , vol.19 , pp. 939-945
    • Borchelt, D.R.1    Ratovitski, T.2    van Lare, J.3    Lee, M.K.4    Gonzales, V.5    Jenkins, N.A.6
  • 9
    • 85013603520 scopus 로고    scopus 로고
    • Elevated copper in the amyloid plaques and iron in the cortex are observed in mouse models of Alzheimer's disease that exhibit neurodegeneration
    • Bourassa, M. W., Leskovjan, A. C., Tappero, R. V., Farquhar, E. R., Colton, C. A., Van Nostrand, W. E., et al. (2013). Elevated copper in the amyloid plaques and iron in the cortex are observed in mouse models of Alzheimer's disease that exhibit neurodegeneration. Biomed. Spectrosc. Imaging 2, 129-139. doi: 10.3233/BSI-130041.
    • (2013) Biomed. Spectrosc. Imaging , vol.2 , pp. 129-139
    • Bourassa, M.W.1    Leskovjan, A.C.2    Tappero, R.V.3    Farquhar, E.R.4    Colton, C.A.5    Van Nostrand, W.E.6
  • 10
    • 33749150163 scopus 로고    scopus 로고
    • Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry
    • Braak, H., Alafuzoff, I., Arzberger, T., Kretzschmar, H., and Del Tredici, K. (2006). Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry. Acta Neuropathol. 112, 389-404. doi: 10.1007/s00401-006-0127-z.
    • (2006) Acta Neuropathol , vol.112 , pp. 389-404
    • Braak, H.1    Alafuzoff, I.2    Arzberger, T.3    Kretzschmar, H.4    Del Tredici, K.5
  • 11
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak, H., and Braak, E. (1991). Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol. 82, 239-259. doi: 10.1007/BF00308809.
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 12
    • 0036860349 scopus 로고    scopus 로고
    • Metal complexing agents as therapies for Alzheimer's disease
    • Bush, A. I. (2002). Metal complexing agents as therapies for Alzheimer's disease. Neurobiol. Aging 23, 1031-1038. doi: 10.1016/S0197-4580(02)00120-3.
    • (2002) Neurobiol. Aging , vol.23 , pp. 1031-1038
    • Bush, A.I.1
  • 13
    • 53149091603 scopus 로고    scopus 로고
    • Iron deficiency alters expression of genes implicated in Alzheimer disease pathogenesis
    • Carlson, E. S., Magid, R., Petryk, A., and Georgieff, M. K. (2008). Iron deficiency alters expression of genes implicated in Alzheimer disease pathogenesis. Brain Res. 1237, 75-83. doi: 10.1016/j.brainres.2008.07.109.
    • (2008) Brain Res , vol.1237 , pp. 75-83
    • Carlson, E.S.1    Magid, R.2    Petryk, A.3    Georgieff, M.K.4
  • 14
    • 4644276796 scopus 로고    scopus 로고
    • Massive CA1/2 neuronal loss with intraneuronal and N-terminal truncated Abeta42 accumulation in a novel Alzheimer transgenic model
    • Casas, C., Sergeant, N., Itier, J. M., Blanchard, V., Wirths, O., van der Kolk, N., et al. (2004). Massive CA1/2 neuronal loss with intraneuronal and N-terminal truncated Abeta42 accumulation in a novel Alzheimer transgenic model. Am. J. Pathol. 165, 1289-1300. doi: 10.1016/S0002-9440(10)63388-3.
    • (2004) Am. J. Pathol , vol.165 , pp. 1289-1300
    • Casas, C.1    Sergeant, N.2    Itier, J.M.3    Blanchard, V.4    Wirths, O.5    van der Kolk, N.6
  • 15
    • 79955654586 scopus 로고    scopus 로고
    • Magnetic resonance imaging of amyloid plaques in transgenic mouse models of Alzheimer's disease
    • Chamberlain, R., Wengenack, T. M., Poduslo, J. F., Garwood, M., and Jack, C. R. Jr. (2011). Magnetic resonance imaging of amyloid plaques in transgenic mouse models of Alzheimer's disease. Curr. Med. Imaging Rev. 7, 3-7. doi: 10.2174/157340511794653522.
    • (2011) Curr. Med. Imaging Rev , vol.7 , pp. 3-7
    • Chamberlain, R.1    Wengenack, T.M.2    Poduslo, J.F.3    Garwood, M.4    Jack, C.R.5
  • 16
    • 47849086918 scopus 로고    scopus 로고
    • Three-dimensional tomographic imaging and characterization of iron compounds within Alzheimer's plaque core material
    • Collingwood, J. F., Chong, R. K., Kasama, T., Cervera-Gontard, L., Dunin-Borkowski, R. E., Perry, G., et al. (2008). Three-dimensional tomographic imaging and characterization of iron compounds within Alzheimer's plaque core material. J. Alzheimers. Dis. 14, 235-245.
    • (2008) J. Alzheimers. Dis , vol.14 , pp. 235-245
    • Collingwood, J.F.1    Chong, R.K.2    Kasama, T.3    Cervera-Gontard, L.4    Dunin-Borkowski, R.E.5    Perry, G.6
  • 17
    • 0028350924 scopus 로고
    • Isoforms of ferritin have a specific cellular distribution in the brain
    • Connor, J. R., Boeshore, K. L., Benkovic, S. A., and Menzies, S. L. (1994). Isoforms of ferritin have a specific cellular distribution in the brain. J. Neurosci. Res. 37, 461-465. doi: 10.1002/jnr.490370405.
    • (1994) J. Neurosci. Res , vol.37 , pp. 461-465
    • Connor, J.R.1    Boeshore, K.L.2    Benkovic, S.A.3    Menzies, S.L.4
  • 18
    • 0022508973 scopus 로고
    • The distribution of transferrin immunoreactivity in the rat central nervous system
    • Connor, J. R., and Fine, R. E. (1986). The distribution of transferrin immunoreactivity in the rat central nervous system. Brain Res. 368, 319-328. doi: 10.1016/0006-8993(86)90576-7.
    • (1986) Brain Res , vol.368 , pp. 319-328
    • Connor, J.R.1    Fine, R.E.2
  • 19
    • 0023140776 scopus 로고
    • Development of transferrin-positive oligodendrocytes in the rat central nervous system
    • Connor, J. R., and Fine, R. E. (1987). Development of transferrin-positive oligodendrocytes in the rat central nervous system. J. Neurosci. Res. 17, 51-59. doi: 10.1002/jnr.490170108.
    • (1987) J. Neurosci. Res , vol.17 , pp. 51-59
    • Connor, J.R.1    Fine, R.E.2
  • 20
    • 0025648166 scopus 로고
    • Cellular distribution of transferrin, ferritin, and iron in normal and aged human brains
    • Connor, J. R., Menzies, S. L., St Martin, S. M., and Mufson, E. J. (1990). Cellular distribution of transferrin, ferritin, and iron in normal and aged human brains. J. Neurosci. Res. 27, 595-611. doi: 10.1002/jnr.490270421.
    • (1990) J. Neurosci. Res , vol.27 , pp. 595-611
    • Connor, J.R.1    Menzies, S.L.2    St Martin, S.M.3    Mufson, E.J.4
  • 21
    • 0026513756 scopus 로고
    • A histochemical study of iron, transferrin, and ferritin in Alzheimer's diseased brains
    • Connor, J. R., Menzies, S. L., St Martin, S. M., and Mufson, E. J. (1992b). A histochemical study of iron, transferrin, and ferritin in Alzheimer's diseased brains. J. Neurosci. Res. 31, 75-83. doi: 10.1002/jnr.490310111.
    • (1992) J. Neurosci. Res , vol.31 , pp. 75-83
    • Connor, J.R.1    Menzies, S.L.2    St Martin, S.M.3    Mufson, E.J.4
  • 22
    • 0026590705 scopus 로고
    • Regional distribution of iron and iron-regulatory proteins in the brain in aging and Alzheimer's disease
    • Connor, J. R., Snyder, B. S., Beard, J. L., Fine, R. E., and Mufson, E. J. (1992a). Regional distribution of iron and iron-regulatory proteins in the brain in aging and Alzheimer's disease. J. Neurosci. Res. 31, 327-335. doi: 10.1002/jnr.490310214.
    • (1992) J. Neurosci. Res , vol.31 , pp. 327-335
    • Connor, J.R.1    Snyder, B.S.2    Beard, J.L.3    Fine, R.E.4    Mufson, E.J.5
  • 23
    • 0036582717 scopus 로고    scopus 로고
    • Neuronal deficiency of presenilin 1 inhibits amyloid plaque formation and corrects hippocampal long-term potentiation but not a cognitive defect of amyloid precursor protein [V717I] transgenic mice
    • Dewachter, I., Reverse, D., Caluwaerts, N., Ris, L., Kuiperi, C., Van den Haute, C., et al. (2002). Neuronal deficiency of presenilin 1 inhibits amyloid plaque formation and corrects hippocampal long-term potentiation but not a cognitive defect of amyloid precursor protein [V717I] transgenic mice. J. Neurosci. 22, 3445-3453.
    • (2002) J. Neurosci , vol.22 , pp. 3445-3453
    • Dewachter, I.1    Reverse, D.2    Caluwaerts, N.3    Ris, L.4    Kuiperi, C.5    Van den Haute, C.6
  • 24
    • 77956647381 scopus 로고    scopus 로고
    • Iron-export ferroxidase activity of beta-amyloid precursor protein is inhibited by zinc in Alzheimer's disease
    • Duce, J. A., Tsatsanis, A., Cater, M. A., James, S. A., Robb, E., Wikhe, K., et al. (2010). Iron-export ferroxidase activity of beta-amyloid precursor protein is inhibited by zinc in Alzheimer's disease. Cell 142, 857-867. doi: 10.1016/j.cell.2010.08.014.
    • (2010) Cell , vol.142 , pp. 857-867
    • Duce, J.A.1    Tsatsanis, A.2    Cater, M.A.3    James, S.A.4    Robb, E.5    Wikhe, K.6
  • 25
    • 33645053770 scopus 로고    scopus 로고
    • Age-related evolution of amyloid burden, iron load, and MR relaxation times in a transgenic mouse model of Alzheimer's disease
    • El Tannir El Tayara, N., Delatour, B., Le Cudennec, C., Guegan, M., Volk, A., and Dhenain, M. (2006). Age-related evolution of amyloid burden, iron load, and MR relaxation times in a transgenic mouse model of Alzheimer's disease. Neurobiol. Dis. 22, 199-208. doi: 10.1016/j.nbd.2005.10.013.
    • (2006) Neurobiol. Dis , vol.22 , pp. 199-208
    • El Tannir El Tayara, N.1    Delatour, B.2    Le Cudennec, C.3    Guegan, M.4    Volk, A.5    Dhenain, M.6
  • 26
    • 84855801337 scopus 로고    scopus 로고
    • Modest amyloid deposition is associated with iron dysregulation, microglial activation, and oxidative stress
    • Gallagher, J. J., Finnegan, M. E., Grehan, B., Dobson, J., Collingwood, J. F., and Lynch, M. A. (2012). Modest amyloid deposition is associated with iron dysregulation, microglial activation, and oxidative stress. J. Alzheimers Dis. 28, 147-161. doi: 10.3233/JAD-2011-110614.
    • (2012) J. Alzheimers Dis , vol.28 , pp. 147-161
    • Gallagher, J.J.1    Finnegan, M.E.2    Grehan, B.3    Dobson, J.4    Collingwood, J.F.5    Lynch, M.A.6
  • 27
    • 0028000825 scopus 로고
    • Altered brain metabolism of iron as a cause of neurodegenerative diseases?
    • Gerlach, M., Ben-Shachar, D., Riederer, P., and Youdim, M. B. (1994). Altered brain metabolism of iron as a cause of neurodegenerative diseases? J. Neurochem. 63, 793-807. doi: 10.1046/j.1471-4159.1994.63030793.x.
    • (1994) J. Neurochem , vol.63 , pp. 793-807
    • Gerlach, M.1    Ben-Shachar, D.2    Riederer, P.3    Youdim, M.B.4
  • 28
    • 33749161414 scopus 로고    scopus 로고
    • Deposition of iron and beta-amyloid plaques is associated with cortical cellular damage in rabbits fed with long-term cholesterol-enriched diets
    • Ghribi, O., Golovko, M. Y., Larsen, B., Schrag, M., and Murphy, E. J. (2006). Deposition of iron and beta-amyloid plaques is associated with cortical cellular damage in rabbits fed with long-term cholesterol-enriched diets. J. Neurochem. 99, 438-449. doi: 10.1111/j.1471-4159.2006.04079.x.
    • (2006) J. Neurochem , vol.99 , pp. 438-449
    • Ghribi, O.1    Golovko, M.Y.2    Larsen, B.3    Schrag, M.4    Murphy, E.J.5
  • 29
    • 0036175608 scopus 로고    scopus 로고
    • Time course of the development of Alzheimer-like pathology in the doubly transgenic PS1+APP mouse
    • Gordon, M. N., Holcomb, L. A., Jantzen, P. T., DiCarlo, G., Wilcock, D., Boyett, K. W., et al. (2002). Time course of the development of Alzheimer-like pathology in the doubly transgenic PS1+APP mouse. Exp. Neurol. 173, 183-195. doi: 10.1006/exnr.2001.7754.
    • (2002) Exp. Neurol , vol.173 , pp. 183-195
    • Gordon, M.N.1    Holcomb, L.A.2    Jantzen, P.T.3    DiCarlo, G.4    Wilcock, D.5    Boyett, K.W.6
  • 30
    • 0025648873 scopus 로고
    • Ferritin is a component of the neuritic (senile) plaque in Alzheimer dementia
    • Grundke-Iqbal, I., Fleming, J., Tung, Y. C., Lassmann, H., Iqbal, K., and Joshi, J. G. (1990). Ferritin is a component of the neuritic (senile) plaque in Alzheimer dementia. Acta Neuropathol. 81, 105-110. doi: 10.1007/BF00334497.
    • (1990) Acta Neuropathol , vol.81 , pp. 105-110
    • Grundke-Iqbal, I.1    Fleming, J.2    Tung, Y.C.3    Lassmann, H.4    Iqbal, K.5    Joshi, J.G.6
  • 31
    • 84871958441 scopus 로고    scopus 로고
    • Deferoxamine inhibits iron induced hippocampal tau phosphorylation in the Alzheimer transgenic mouse brain
    • Guo, C., Wang, P., Zhong, M. L., Wang, T., Huang, X. S., Li, J. Y., et al. (2013b). Deferoxamine inhibits iron induced hippocampal tau phosphorylation in the Alzheimer transgenic mouse brain. Neurochem. Int. 62, 165-172. doi: 10.1016/j.neuint.2012.12.005.
    • (2013) Neurochem. Int , vol.62 , pp. 165-172
    • Guo, C.1    Wang, P.2    Zhong, M.L.3    Wang, T.4    Huang, X.S.5    Li, J.Y.6
  • 32
    • 84869080922 scopus 로고    scopus 로고
    • Intranasal deferoxamine reverses iron-induced memory deficits and inhibits amyloidogenic APP processing in a transgenic mouse model of Alzheimer's disease
    • Guo, C., Wang, T., Zheng, W., Shan, Z. Y., Teng, W. P., and Wang, Z. Y. (2013a). Intranasal deferoxamine reverses iron-induced memory deficits and inhibits amyloidogenic APP processing in a transgenic mouse model of Alzheimer's disease. Neurobiol. Aging 34, 562-575. doi: 10.1016/j.neurobiolaging.2012.05.009.
    • (2013) Neurobiol. Aging , vol.34 , pp. 562-575
    • Guo, C.1    Wang, T.2    Zheng, W.3    Shan, Z.Y.4    Teng, W.P.5    Wang, Z.Y.6
  • 33
    • 84881593997 scopus 로고    scopus 로고
    • Effects of the gamma-secretase inhibitor semagacestat on hippocampal neuronal network oscillation
    • Hajos, M., Morozova, E., Siok, C., Atchison, K., Nolan, C. E., Riddell, D., et al. (2013). Effects of the gamma-secretase inhibitor semagacestat on hippocampal neuronal network oscillation. Front. Pharmacol. 4:72. doi: 10.3389/fphar.2013.00072.
    • (2013) Front. Pharmacol , vol.4 , pp. 72
    • Hajos, M.1    Morozova, E.2    Siok, C.3    Atchison, K.4    Nolan, C.E.5    Riddell, D.6
  • 34
    • 0036714614 scopus 로고    scopus 로고
    • H and L ferritin subunit mRNA expression differs in brains of control and iron-deficient rats
    • Han, J., Day, J. R., Connor, J. R., and Beard, J. L. (2002). H and L ferritin subunit mRNA expression differs in brains of control and iron-deficient rats. J. Nutr. 132, 2769-2774.
    • (2002) J. Nutr , vol.132 , pp. 2769-2774
    • Han, J.1    Day, J.R.2    Connor, J.R.3    Beard, J.L.4
  • 35
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer's disease
    • Hardy, J., and Allsop, D. (1991). Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol. Sci. 12, 383-388. doi: 10.1016/0165-6147(91)90609-V.
    • (1991) Trends Pharmacol. Sci , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 36
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy, J., and Selkoe, D. J. (2002). The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356. doi: 10.1126/science.1072994.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 37
    • 33744454404 scopus 로고    scopus 로고
    • Alzheimer's disease pathogenesis: role of aging
    • Harman, D. (2006). Alzheimer's disease pathogenesis: role of aging. Ann. N.Y. Acad. Sci. 1067, 454-460. doi: 10.1196/annals.1354.065.
    • (2006) Ann. N.Y. Acad. Sci , vol.1067 , pp. 454-460
    • Harman, D.1
  • 38
    • 18344414746 scopus 로고    scopus 로고
    • The A beta peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction
    • Huang, X., Atwood, C. S., Hartshorn, M. A., Multhaup, G., Goldstein, L. E., Scarpa, R. C., et al. (1999). The A beta peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction. Biochemistry 38, 7609-7616. doi: 10.1021/bi990438f.
    • (1999) Biochemistry , vol.38 , pp. 7609-7616
    • Huang, X.1    Atwood, C.S.2    Hartshorn, M.A.3    Multhaup, G.4    Goldstein, L.E.5    Scarpa, R.C.6
  • 39
    • 10044278300 scopus 로고    scopus 로고
    • In vivo visualization of Alzheimer's amyloid plaques by magnetic resonance imaging in transgenic mice without a contrast agent
    • Jack, C. R. Jr., Garwood, M., Wengenack, T. M., Borowski, B., Curran, G. L., Lin, J., et al. (2004). In vivo visualization of Alzheimer's amyloid plaques by magnetic resonance imaging in transgenic mice without a contrast agent. Magn. Reson. Med. 52, 1263-1271. doi: 10.1002/mrm.20266.
    • (2004) Magn. Reson. Med , vol.52 , pp. 1263-1271
    • Jack, C.R.1    Garwood, M.2    Wengenack, T.M.3    Borowski, B.4    Curran, G.L.5    Lin, J.6
  • 40
    • 0035049961 scopus 로고    scopus 로고
    • Co-expression of multiple transgenes in mouse CNS: a comparison of strategies
    • Jankowsky, J. L., Slunt, H. H., Ratovitski, T., Jenkins, N. A., Copeland, N. G., and Borchelt, D. R. (2001). Co-expression of multiple transgenes in mouse CNS: a comparison of strategies. Biomol. Eng. 17, 157-165. doi: 10.1016/S1389-0344(01)00067-3.
    • (2001) Biomol. Eng , vol.17 , pp. 157-165
    • Jankowsky, J.L.1    Slunt, H.H.2    Ratovitski, T.3    Jenkins, N.A.4    Copeland, N.G.5    Borchelt, D.R.6
  • 42
    • 69049113059 scopus 로고    scopus 로고
    • Ternary complexes of iron, amyloid-beta, and nitrilotriacetic acid: binding affinities, redox properties, and relevance to iron-induced oxidative stress in Alzheimer's disease
    • Jiang, D., Li, X., Williams, R., Patel, S., Men, L., Wang, Y., et al. (2009). Ternary complexes of iron, amyloid-beta, and nitrilotriacetic acid: binding affinities, redox properties, and relevance to iron-induced oxidative stress in Alzheimer's disease. Biochemistry 48, 7939-7947. doi: 10.1021/bi900907a.
    • (2009) Biochemistry , vol.48 , pp. 7939-7947
    • Jiang, D.1    Li, X.2    Williams, R.3    Patel, S.4    Men, L.5    Wang, Y.6
  • 43
    • 0024853737 scopus 로고
    • Ferritin immunohistochemistry as a marker for microglia
    • Kaneko, Y., Kitamoto, T., Tateishi, J., and Yamaguchi, K. (1989). Ferritin immunohistochemistry as a marker for microglia. Acta Neuropathol. 79, 129-136. doi: 10.1007/BF00294369.
    • (1989) Acta Neuropathol , vol.79 , pp. 129-136
    • Kaneko, Y.1    Kitamoto, T.2    Tateishi, J.3    Yamaguchi, K.4
  • 44
    • 31644435643 scopus 로고    scopus 로고
    • Redox cycling of iron by Abeta42
    • Khan, A., Dobson, J. P., and Exley, C. (2006). Redox cycling of iron by Abeta42. Free Radic. Biol. Med. 40, 557-569. doi: 10.1016/j.freeradbiomed.2005.09.013.
    • (2006) Free Radic. Biol. Med , vol.40 , pp. 557-569
    • Khan, A.1    Dobson, J.P.2    Exley, C.3
  • 45
    • 0037013327 scopus 로고    scopus 로고
    • Intracellular amyloid-beta 1-42, but not extracellular soluble amyloid-beta peptides, induces neuronal apoptosis
    • Kienlen-Campard, P., Miolet, S., Tasiaux, B., and Octave, J. N. (2002). Intracellular amyloid-beta 1-42, but not extracellular soluble amyloid-beta peptides, induces neuronal apoptosis. J. Biol. Chem. 277, 15666-15670. doi: 10.1074/jbc.M200887200.
    • (2002) J. Biol. Chem , vol.277 , pp. 15666-15670
    • Kienlen-Campard, P.1    Miolet, S.2    Tasiaux, B.3    Octave, J.N.4
  • 46
    • 7744235869 scopus 로고    scopus 로고
    • Microglial phagocytosis of fibrillar beta-amyloid through a beta1 integrin-dependent mechanism
    • Koenigsknecht, J., and Landreth, G. (2004). Microglial phagocytosis of fibrillar beta-amyloid through a beta1 integrin-dependent mechanism. J. Neurosci. 24, 9838-9846. doi: 10.1523/JNEUROSCI.2557-04.2004.
    • (2004) J. Neurosci , vol.24 , pp. 9838-9846
    • Koenigsknecht, J.1    Landreth, G.2
  • 47
    • 0026095312 scopus 로고
    • Oligodendrocytes and myelin sheaths in normal, quaking and shiverer brains are enriched in iron
    • LeVine, S. M. (1991). Oligodendrocytes and myelin sheaths in normal, quaking and shiverer brains are enriched in iron. J. Neurosci. Res. 29, 413-419. doi: 10.1002/jnr.490290317.
    • (1991) J. Neurosci. Res , vol.29 , pp. 413-419
    • LeVine, S.M.1
  • 48
    • 0030788672 scopus 로고    scopus 로고
    • Iron deposits in multiple sclerosis and Alzheimer's disease brains
    • LeVine, S. M. (1997). Iron deposits in multiple sclerosis and Alzheimer's disease brains. Brain Res. 760, 298-303. doi: 10.1016/S0006-8993(97)00470-8.
    • (1997) Brain Res , vol.760 , pp. 298-303
    • LeVine, S.M.1
  • 49
    • 51349095669 scopus 로고    scopus 로고
    • Microglial dystrophy in the aged and Alzheimer's disease brain is associated with ferritin immunoreactivity
    • Lopes, K. O., Sparks, D. L., and Streit, W. J. (2008). Microglial dystrophy in the aged and Alzheimer's disease brain is associated with ferritin immunoreactivity. Glia 56, 1048-1060. doi: 10.1002/glia.20678.
    • (2008) Glia , vol.56 , pp. 1048-1060
    • Lopes, K.O.1    Sparks, D.L.2    Streit, W.J.3
  • 50
    • 34648859471 scopus 로고    scopus 로고
    • Oxidative damage in mild cognitive impairment and early Alzheimer's disease
    • Lovell, M. A., and Markesbery, W. R. (2007). Oxidative damage in mild cognitive impairment and early Alzheimer's disease. J. Neurosci. Res. 85, 3036-3040. doi: 10.1002/jnr.21346.
    • (2007) J. Neurosci. Res , vol.85 , pp. 3036-3040
    • Lovell, M.A.1    Markesbery, W.R.2
  • 52
    • 84871246344 scopus 로고    scopus 로고
    • Animal models of Alzheimer's Disease: utilization of transgenic Alzheimer's disease models in studies of amyloid beta clearance
    • Malm, T., Magga, J., and Koistinaho, J. (2012). Animal models of Alzheimer's Disease: utilization of transgenic Alzheimer's disease models in studies of amyloid beta clearance. Curr. Transl. Geriatr. Exp. Gerontol. Rep. 1, 11-20. doi: 10.1007/s13670-011-0004-z.
    • (2012) Curr. Transl. Geriatr. Exp. Gerontol. Rep , vol.1 , pp. 11-20
    • Malm, T.1    Magga, J.2    Koistinaho, J.3
  • 53
    • 20444440369 scopus 로고    scopus 로고
    • Metals and amyloid-beta in Alzheimer's disease
    • Maynard, C. J., Bush, A. I., Masters, C. L., Cappai, R., and Li, Q. X. (2005). Metals and amyloid-beta in Alzheimer's disease. Int. J. Exp. Pathol. 86, 147-159. doi: 10.1111/j.0959-9673.2005.00434.x.
    • (2005) Int. J. Exp. Pathol , vol.86 , pp. 147-159
    • Maynard, C.J.1    Bush, A.I.2    Masters, C.L.3    Cappai, R.4    Li, Q.X.5
  • 54
    • 66149090377 scopus 로고    scopus 로고
    • MRI and histological analysis of beta-amyloid plaques in both human Alzheimer's disease and APP/PS1 transgenic mice
    • Meadowcroft, M. D., Connor, J. R., Smith, M. B., and Yang, Q. X. (2009). MRI and histological analysis of beta-amyloid plaques in both human Alzheimer's disease and APP/PS1 transgenic mice. J. Magn. Reson. Imaging 29, 997-1007. doi: 10.1002/jmri.21731.
    • (2009) J. Magn. Reson. Imaging , vol.29 , pp. 997-1007
    • Meadowcroft, M.D.1    Connor, J.R.2    Smith, M.B.3    Yang, Q.X.4
  • 55
    • 33746935592 scopus 로고    scopus 로고
    • Ferritin levels in microglia depend upon activation: modulation by reactive oxygen species
    • Mehlhase, J., Gieche, J., Widmer, R., and Grune, T. (2006). Ferritin levels in microglia depend upon activation: modulation by reactive oxygen species. Biochim. Biophys. Acta 1763, 854-859. doi: 10.1016/j.bbamcr.2006.04.012.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 854-859
    • Mehlhase, J.1    Gieche, J.2    Widmer, R.3    Grune, T.4
  • 56
    • 84881340502 scopus 로고    scopus 로고
    • Naturally occurring autoantibodies interfere with beta-amyloid metabolism and improve cognition in a transgenic mouse model of Alzheimer's disease 24 h after single treatment
    • Mengel, D., Roskam, S., Neff, F., Balakrishnan, K., Deuster, O., Gold, M., et al. (2013). Naturally occurring autoantibodies interfere with beta-amyloid metabolism and improve cognition in a transgenic mouse model of Alzheimer's disease 24 h after single treatment. Transl. Psychiatry 3, e236. doi: 10.1038/tp.2012.151.
    • (2013) Transl. Psychiatry , vol.3
    • Mengel, D.1    Roskam, S.2    Neff, F.3    Balakrishnan, K.4    Deuster, O.5    Gold, M.6
  • 57
    • 20344398223 scopus 로고    scopus 로고
    • Astrocyte activation and reactive gliosis
    • Pekny, M., and Nilsson, M. (2005). Astrocyte activation and reactive gliosis. Glia 50, 427-434. doi: 10.1002/glia.20207.
    • (2005) Glia , vol.50 , pp. 427-434
    • Pekny, M.1    Nilsson, M.2
  • 58
    • 18744374615 scopus 로고    scopus 로고
    • Is oxidative damage the fundamental pathogenic mechanism of Alzheimer's and other neurodegenerative diseases?
    • Perry, G., Nunomura, A., Hirai, K., Zhu, X., Perez, M., Avila, J., et al. (2002). Is oxidative damage the fundamental pathogenic mechanism of Alzheimer's and other neurodegenerative diseases? Free Radic. Biol. Med. 33, 1475-1479. doi: 10.1016/S0891-5849(02)01113-9.
    • (2002) Free Radic. Biol. Med , vol.33 , pp. 1475-1479
    • Perry, G.1    Nunomura, A.2    Hirai, K.3    Zhu, X.4    Perez, M.5    Avila, J.6
  • 59
    • 60349125886 scopus 로고    scopus 로고
    • Reassessing the amyloid cascade hypothesis of Alzheimer's disease
    • Pimplikar, S. W. (2009). Reassessing the amyloid cascade hypothesis of Alzheimer's disease. Int. J. Biochem. Cell Biol. 41, 1261-1268. doi: 10.1016/j.biocel.2008.12.015.
    • (2009) Int. J. Biochem. Cell Biol , vol.41 , pp. 1261-1268
    • Pimplikar, S.W.1
  • 60
    • 0141707862 scopus 로고    scopus 로고
    • PS2APP transgenic mice, coexpressing hPS2mut and hAPPswe, show age-related cognitive deficits associated with discrete brain amyloid deposition and inflammation
    • Richards, J. G., Higgins, G. A., Ouagazzal, A. M., Ozmen, L., Kew, J. N., Bohrmann, B., et al. (2003). PS2APP transgenic mice, coexpressing hPS2mut and hAPPswe, show age-related cognitive deficits associated with discrete brain amyloid deposition and inflammation. J. Neurosci. 23, 8989-9003.
    • (2003) J. Neurosci , vol.23 , pp. 8989-9003
    • Richards, J.G.1    Higgins, G.A.2    Ouagazzal, A.M.3    Ozmen, L.4    Kew, J.N.5    Bohrmann, B.6
  • 61
    • 59149101704 scopus 로고    scopus 로고
    • Iron and the translation of the amyloid precursor protein (APP) and ferritin mRNAs: riboregulation against neural oxidative damage in Alzheimer's disease
    • Rogers, J. T., Bush, A. I., Cho, H. H., Smith, D. H., Thomson, A. M., Friedlich, A. L., et al. (2008). Iron and the translation of the amyloid precursor protein (APP) and ferritin mRNAs: riboregulation against neural oxidative damage in Alzheimer's disease. Biochem. Soc. Trans. 36(Pt 6), 1282-1287. doi: 10.1042/BST0361282.
    • (2008) Biochem. Soc. Trans , vol.36 , pp. 1282-1287
    • Rogers, J.T.1    Bush, A.I.2    Cho, H.H.3    Smith, D.H.4    Thomson, A.M.5    Friedlich, A.L.6
  • 63
    • 43249119241 scopus 로고    scopus 로고
    • Influence of multiple metal ions on beta-amyloid aggregation and dissociation on a solid surface
    • Ryu, J., Girigoswami, K., Ha, C., Ku, S. H., and Park, C. B. (2008). Influence of multiple metal ions on beta-amyloid aggregation and dissociation on a solid surface. Biochemistry 47, 5328-5335. doi: 10.1021/bi800012e.
    • (2008) Biochemistry , vol.47 , pp. 5328-5335
    • Ryu, J.1    Girigoswami, K.2    Ha, C.3    Ku, S.H.4    Park, C.B.5
  • 64
    • 0033964859 scopus 로고    scopus 로고
    • In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: a central role for bound transition metals
    • Sayre, L. M., Perry, G., Harris, P. L., Liu, Y., Schubert, K. A., and Smith, M. A. (2000). In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: a central role for bound transition metals. J. Neurochem. 74, 270-279. doi: 10.1046/j.1471-4159.2000.0740270.x.
    • (2000) J. Neurochem , vol.74 , pp. 270-279
    • Sayre, L.M.1    Perry, G.2    Harris, P.L.3    Liu, Y.4    Schubert, K.A.5    Smith, M.A.6
  • 65
    • 0030983405 scopus 로고    scopus 로고
    • Mechanisms of neurotoxicity associated with amyloid beta deposition and the role of free radicals in the pathogenesis of Alzheimer's disease: a critical appraisal
    • Sayre, L. M., Zagorski, M. G., Surewicz, W. K., Krafft, G. A., and Perry, G. (1997). Mechanisms of neurotoxicity associated with amyloid beta deposition and the role of free radicals in the pathogenesis of Alzheimer's disease: a critical appraisal. Chem. Res. Toxicol. 10, 518-526. doi: 10.1021/tx970009n.
    • (1997) Chem. Res. Toxicol , vol.10 , pp. 518-526
    • Sayre, L.M.1    Zagorski, M.G.2    Surewicz, W.K.3    Krafft, G.A.4    Perry, G.5
  • 66
    • 13844253258 scopus 로고    scopus 로고
    • Fluoro-Jade C results in ultra high resolution and contrast labeling of degenerating neurons
    • Schmued, L. C., Stowers, C. C., Scallet, A. C., and Xu, L. (2005). Fluoro-Jade C results in ultra high resolution and contrast labeling of degenerating neurons. Brain Res. 1035, 24-31. doi: 10.1016/j.brainres.2004.11.054.
    • (2005) Brain Res , vol.1035 , pp. 24-31
    • Schmued, L.C.1    Stowers, C.C.2    Scallet, A.C.3    Xu, L.4
  • 67
    • 64049105735 scopus 로고    scopus 로고
    • The induction of HIF-1 reduces astrocyte activation by amyloid beta peptide
    • Schubert, D., Soucek, T., and Blouw, B. (2009). The induction of HIF-1 reduces astrocyte activation by amyloid beta peptide. Eur. J. Neurosci. 29, 1323-1334. doi: 10.1111/j.1460-9568.2009.06712.x.
    • (2009) Eur. J. Neurosci , vol.29 , pp. 1323-1334
    • Schubert, D.1    Soucek, T.2    Blouw, B.3
  • 68
    • 2942611429 scopus 로고    scopus 로고
    • Transgenic mice overexpressing amyloid beta protein are an incomplete model of Alzheimer disease
    • Schwab, C., Hosokawa, M., and McGeer, P. L. (2004). Transgenic mice overexpressing amyloid beta protein are an incomplete model of Alzheimer disease. Exp. Neurol. 188, 52-64. doi: 10.1016/j.expneurol.2004.03.016.
    • (2004) Exp. Neurol , vol.188 , pp. 52-64
    • Schwab, C.1    Hosokawa, M.2    McGeer, P.L.3
  • 69
    • 0034551780 scopus 로고    scopus 로고
    • Presenilin-1 P264L knock-in mutation: differential effects on abeta production, amyloid deposition, and neuronal vulnerability
    • Siman, R., Reaume, A. G., Savage, M. J., Trusko, S., Lin, Y. G., Scott, R. W., et al. (2000). Presenilin-1 P264L knock-in mutation: differential effects on abeta production, amyloid deposition, and neuronal vulnerability. J. Neurosci. 20, 8717-8726. doi: 10.1016/s0197-4580(00)82329-5.
    • (2000) J. Neurosci , vol.20 , pp. 8717-8726
    • Siman, R.1    Reaume, A.G.2    Savage, M.J.3    Trusko, S.4    Lin, Y.G.5    Scott, R.W.6
  • 70
    • 0030885482 scopus 로고    scopus 로고
    • Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
    • Smith, M. A., Harris, P. L., Sayre, L. M., and Perry, G. (1997). Iron accumulation in Alzheimer disease is a source of redox-generated free radicals. Proc. Natl. Acad. Sci. U.S.A. 94, 9866-9868. doi: 10.1073/pnas.94.18.9866.
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 9866-9868
    • Smith, M.A.1    Harris, P.L.2    Sayre, L.M.3    Perry, G.4
  • 71
    • 0033751421 scopus 로고    scopus 로고
    • Metabolic, metallic, and mitotic sources of oxidative stress in Alzheimer disease
    • Smith, M. A., Nunomura, A., Zhu, X., Takeda, A., and Perry, G. (2000). Metabolic, metallic, and mitotic sources of oxidative stress in Alzheimer disease. Antioxid. Redox Signal. 2, 413-420. doi: 10.1089/15230860050192198.
    • (2000) Antioxid. Redox Signal , vol.2 , pp. 413-420
    • Smith, M.A.1    Nunomura, A.2    Zhu, X.3    Takeda, A.4    Perry, G.5
  • 72
    • 0001912805 scopus 로고    scopus 로고
    • Is Alzheimer's a disease of oxidative stress?
    • Smith, M. A., Sayre, L. M., and Perry, G. (1996). Is Alzheimer's a disease of oxidative stress? Alzheimers Dis. Rev. 1, 63-67.
    • (1996) Alzheimers Dis. Rev , vol.1 , pp. 63-67
    • Smith, M.A.1    Sayre, L.M.2    Perry, G.3
  • 73
    • 0035997492 scopus 로고    scopus 로고
    • Expression of ferritin, transferrin receptor, and non-specific resistance associated macrophage proteins 1 and 2 (Nramp1 and Nramp2) in the human rheumatoid synovium
    • Telfer, J. F., and Brock, J. H. (2002). Expression of ferritin, transferrin receptor, and non-specific resistance associated macrophage proteins 1 and 2 (Nramp1 and Nramp2) in the human rheumatoid synovium. Ann. Rheum. Dis. 61, 741-744. doi: 10.1136/ard.61.8.741.
    • (2002) Ann. Rheum. Dis , vol.61 , pp. 741-744
    • Telfer, J.F.1    Brock, J.H.2
  • 74
    • 0037216723 scopus 로고    scopus 로고
    • Mouse brains deficient in H-ferritin have normal iron concentration but a protein profile of iron deficiency and increased evidence of oxidative stress
    • Thompson, K., Menzies, S., Muckenthaler, M., Torti, F. M., Wood, T., Torti, S. V., et al. (2003). Mouse brains deficient in H-ferritin have normal iron concentration but a protein profile of iron deficiency and increased evidence of oxidative stress. J. Neurosci. Res. 71, 46-63. doi: 10.1002/jnr.10463.
    • (2003) J. Neurosci. Res , vol.71 , pp. 46-63
    • Thompson, K.1    Menzies, S.2    Muckenthaler, M.3    Torti, F.M.4    Wood, T.5    Torti, S.V.6
  • 75
    • 0034795366 scopus 로고    scopus 로고
    • Microglia-astrocyte interaction in Alzheimer's disease: friends or foes for the nervous system?
    • von Bernhardi, R., and Ramirez, G. (2001). Microglia-astrocyte interaction in Alzheimer's disease: friends or foes for the nervous system? Biol. Res. 34, 123-128. doi: 10.4067/S0716-97602001000200017.
    • (2001) Biol. Res , vol.34 , pp. 123-128
    • von Bernhardi, R.1    Ramirez, G.2
  • 76
    • 84864575680 scopus 로고    scopus 로고
    • In vivo magnetic resonance imaging of amyloid-beta plaques in mice
    • Wadghiri, Y. Z., Hoang, D. M., Wisniewski, T., and Sigurdsson, E. M. (2012). In vivo magnetic resonance imaging of amyloid-beta plaques in mice. Methods Mol. Biol. 849, 435-451. doi: 10.1007/978-1-61779-551-0_30.
    • (2012) Methods Mol. Biol , vol.849 , pp. 435-451
    • Wadghiri, Y.Z.1    Hoang, D.M.2    Wisniewski, T.3    Sigurdsson, E.M.4
  • 77
    • 0038790267 scopus 로고    scopus 로고
    • Origin and turnover of microglial cells in fibrillar plaques of APPsw transgenic mice
    • Wegiel, J., Imaki, H., Wang, K. C., Wronska, A., Osuchowski, M., and Rubenstein, R. (2003). Origin and turnover of microglial cells in fibrillar plaques of APPsw transgenic mice. Acta Neuropathol. 105, 393-402. doi: 10.1007/s00401-002-0660-3.
    • (2003) Acta Neuropathol , vol.105 , pp. 393-402
    • Wegiel, J.1    Imaki, H.2    Wang, K.C.3    Wronska, A.4    Osuchowski, M.5    Rubenstein, R.6
  • 78
    • 0035054886 scopus 로고    scopus 로고
    • The role of microglial cells and astrocytes in fibrillar plaque evolution in transgenic APP(SW) mice
    • Wegiel, J., Wang, K. C., Imaki, H., Rubenstein, R., Wronska, A., Osuchowski, M., et al. (2001). The role of microglial cells and astrocytes in fibrillar plaque evolution in transgenic APP(SW) mice. Neurobiol. Aging 22, 49-61. doi: 10.1016/S0197-4580(00)00181-0.
    • (2001) Neurobiol. Aging , vol.22 , pp. 49-61
    • Wegiel, J.1    Wang, K.C.2    Imaki, H.3    Rubenstein, R.4    Wronska, A.5    Osuchowski, M.6
  • 79
    • 0034295217 scopus 로고    scopus 로고
    • Microglia cells are the driving force in fibrillar plaque formation, whereas astrocytes are a leading factor in plague degradation
    • Wegiel, J., Wang, K. C., Tarnawski, M., and Lach, B. (2000). Microglia cells are the driving force in fibrillar plaque formation, whereas astrocytes are a leading factor in plague degradation. Acta Neuropathol. 100, 356-364. doi: 10.1007/s004010000199.
    • (2000) Acta Neuropathol , vol.100 , pp. 356-364
    • Wegiel, J.1    Wang, K.C.2    Tarnawski, M.3    Lach, B.4
  • 80
    • 77957939522 scopus 로고    scopus 로고
    • Regional differences in MRI detection of amyloid plaques in AD transgenic mouse brain
    • Wengenack, T. M., Reyes, D. A., Curran, G. L., Borowski, B. J., Lin, J., Preboske, G. M., et al. (2011). Regional differences in MRI detection of amyloid plaques in AD transgenic mouse brain. Neuroimage 54, 113-122. doi: 10.1016/j.neuroimage.2010.08.033.
    • (2011) Neuroimage , vol.54 , pp. 113-122
    • Wengenack, T.M.1    Reyes, D.A.2    Curran, G.L.3    Borowski, B.J.4    Lin, J.5    Preboske, G.M.6
  • 81
    • 84914693430 scopus 로고    scopus 로고
    • beta-Amyloid precursor protein does not possess ferroxidase activity but does stabilize the cell surface ferrous iron exporter ferroportin
    • Wong, B. X., Tsatsanis, A., Lim, L. Q., Adlard, P. A., Bush, A. I., and Duce, J. A. (2014). beta-Amyloid precursor protein does not possess ferroxidase activity but does stabilize the cell surface ferrous iron exporter ferroportin. PLoS ONE 9:e114174. doi: 10.1371/journal.pone.0114174.
    • (2014) PLoS ONE , vol.9
    • Wong, B.X.1    Tsatsanis, A.2    Lim, L.Q.3    Adlard, P.A.4    Bush, A.I.5    Duce, J.A.6
  • 82
    • 65249085666 scopus 로고    scopus 로고
    • Dystrophic neurites in TgCRND8 and Tg2576 mice mimic human pathological brain aging
    • Woodhouse, A., Vickers, J. C., Adlard, P. A., and Dickson, T. C. (2009). Dystrophic neurites in TgCRND8 and Tg2576 mice mimic human pathological brain aging. Neurobiol. Aging 30, 864-874. doi: 10.1016/j.neurobiolaging.2007.09.003.
    • (2009) Neurobiol. Aging , vol.30 , pp. 864-874
    • Woodhouse, A.1    Vickers, J.C.2    Adlard, P.A.3    Dickson, T.C.4


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