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Volumn 5 APR, Issue , 2014, Pages

The iron regulatory capability of the major protein participants in prevalent neurodegenerative disorders

Author keywords

A synuclein; Alzheimer's disease; Amyloid precursor protein; Huntington's disease; Parkinson's disease; Prion disease; Prion protein; Tau

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; CD71 ANTIGEN; CERULOPLASMIN; HUNTINGTIN; IRON REGULATORY FACTOR; MESSENGER RNA; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 2; PRION PROTEIN; TAU PROTEIN;

EID: 84901058201     PISSN: None     EISSN: 16639812     Source Type: Journal    
DOI: 10.3389/fphar.2014.00081     Document Type: Review
Times cited : (39)

References (160)
  • 1
    • 84862889276 scopus 로고    scopus 로고
    • Prion propagation, toxicity and degradation
    • doi: 10.1038/nn.3120
    • Aguzzi, A., and Falsig, J. (2012). Prion propagation, toxicity and degradation. Nat. Neurosci. 15, 936-939. doi: 10.1038/nn.3120
    • (2012) Nat. Neurosci. , vol.15 , pp. 936-939
    • Aguzzi, A.1    Falsig, J.2
  • 2
    • 67649739079 scopus 로고    scopus 로고
    • Iron toxicity in diseases of aging: Alzheimer's disease, Parkinson's disease and atherosclerosis
    • doi: 10.3233/JAD-2009-1010
    • Altamura, S., and Muckenthaler, M. U. (2009). Iron toxicity in diseases of aging: Alzheimer's disease, Parkinson's disease and atherosclerosis. J. Alzheimers Dis. 16, 879-895. doi: 10.3233/JAD-2009-1010
    • (2009) J. Alzheimers Dis. , vol.16 , pp. 879-895
    • Altamura, S.1    Muckenthaler, M.U.2
  • 3
    • 43249100611 scopus 로고    scopus 로고
    • Targeting multiple Alzheimer's disease etiologies with multimodal neuroprotective and neurorestorative iron chelators
    • doi: 10.1096/fj.07-8627rev
    • Amit, T., Avramovich-Tirosh, Y., Youdim, M. B., and Mandel, S. (2008). Targeting multiple Alzheimer's disease etiologies with multimodal neuroprotective and neurorestorative iron chelators. FASEB J. 22, 1296-1305. doi: 10.1096/fj.07-8627rev
    • (2008) FASEB J. , vol.22 , pp. 1296-1305
    • Amit, T.1    Avramovich-Tirosh, Y.2    Youdim, M.B.3    Mandel, S.4
  • 4
    • 83055194393 scopus 로고    scopus 로고
    • High field magnetic resonance microscopy of the human hippocampus in Alzheimer's disease: quantitative imaging and correlation with iron
    • doi: 10.1016/j.neuroimage.2011.08.019
    • Antharam, V., Collingwood, J. F., Bullivant, J. P., Davidson, M. R., Chandra, S., Mikhaylova, A., et al. (2012). High field magnetic resonance microscopy of the human hippocampus in Alzheimer's disease: quantitative imaging and correlation with iron. Neuroimage 59, 1249-1260. doi: 10.1016/j.neuroimage.2011.08.019
    • (2012) Neuroimage , vol.59 , pp. 1249-1260
    • Antharam, V.1    Collingwood, J.F.2    Bullivant, J.P.3    Davidson, M.R.4    Chandra, S.5    Mikhaylova, A.6
  • 5
    • 67650091951 scopus 로고    scopus 로고
    • Age-related iron deposition in the basal ganglia: quantitative analysis in healthy subjects
    • doi: 10.1148/radiol.2522081399
    • Aquino, D., Bizzi, A., Grisoli, M., Garavaglia, B., Bruzzone, M. G., Nardocci, N., et al. (2009). Age-related iron deposition in the basal ganglia: quantitative analysis in healthy subjects. Radiology 252, 165-172. doi: 10.1148/radiol.2522081399
    • (2009) Radiology , vol.252 , pp. 165-172
    • Aquino, D.1    Bizzi, A.2    Grisoli, M.3    Garavaglia, B.4    Bruzzone, M.G.5    Nardocci, N.6
  • 6
    • 33644778691 scopus 로고    scopus 로고
    • Amyloid-beta peptide binds with heme to form a peroxidase: relationship to the cytopathologies of Alzheimer's disease
    • doi: 10.1073/pnas.0600134103
    • Atamna, H., and Boyle, K. (2006). Amyloid-beta peptide binds with heme to form a peroxidase: relationship to the cytopathologies of Alzheimer's disease. Proc. Natl. Acad. Sci. U.S.A. 103, 3381-3386. doi: 10.1073/pnas.0600134103
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 3381-3386
    • Atamna, H.1    Boyle, K.2
  • 7
    • 3342880690 scopus 로고    scopus 로고
    • A role for heme in Alzheimer's disease: heme binds amyloid beta and has altered metabolism
    • doi: 10.1073/pnas.0404349101
    • Atamna, H., and Frey, W. H. II. (2004). A role for heme in Alzheimer's disease: heme binds amyloid beta and has altered metabolism. Proc. Natl. Acad. Sci. U.S.A. 101, 11153-11158. doi: 10.1073/pnas.0404349101
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 11153-11158
    • Atamna, H.1    Frey II, W.H.2
  • 8
    • 67349131967 scopus 로고    scopus 로고
    • Human and rodent amyloid-beta peptides differentially bind heme: relevance to the human susceptibility to Alzheimer's disease
    • doi: 10.1016/j.abb.2009.05.003
    • Atamna, H., Frey, W. H. II, and Ko, N. (2009). Human and rodent amyloid-beta peptides differentially bind heme: relevance to the human susceptibility to Alzheimer's disease. Arch. Biochem. Biophys. 487, 59-65. doi: 10.1016/j.abb.2009.05.003
    • (2009) Arch. Biochem. Biophys. , vol.487 , pp. 59-65
    • Atamna, H.1    Frey II, W.H.2    Ko, N.3
  • 9
    • 84878398613 scopus 로고    scopus 로고
    • Ceruloplasmin dysfunction and therapeutic potential for Parkinson disease
    • doi: 10.1002/ana.23817
    • Ayton, S., Lei, P., Duce, J. A., Wong, B. X., Sedjahtera, A., Adlard, P. A., et al. (2012). Ceruloplasmin dysfunction and therapeutic potential for Parkinson disease. Ann. Neurol. 73, 554-559. doi: 10.1002/ana.23817
    • (2012) Ann. Neurol. , vol.73 , pp. 554-559
    • Ayton, S.1    Lei, P.2    Duce, J.A.3    Wong, B.X.4    Sedjahtera, A.5    Adlard, P.A.6
  • 10
    • 79952763943 scopus 로고    scopus 로고
    • Reorganizing metals: the use of chelating compounds as potential therapies for metal-related neurodegenerative disease
    • doi: 10.2174/156802611794785181
    • Badrick, A. C., and Jones, C. E. (2011). Reorganizing metals: the use of chelating compounds as potential therapies for metal-related neurodegenerative disease. Curr. Top. Med. Chem. 11, 543-552. doi: 10.2174/156802611794785181
    • (2011) Curr. Top. Med. Chem. , vol.11 , pp. 543-552
    • Badrick, A.C.1    Jones, C.E.2
  • 11
    • 0027430183 scopus 로고
    • Ferritin, transferrin, and iron in selected regions of the adult and aged rat brain
    • doi: 10.1002/cne.903380108
    • Benkovic, S. A., and Connor, J. R. (1993). Ferritin, transferrin, and iron in selected regions of the adult and aged rat brain. J. Comp. Neurol. 338, 97-113. doi: 10.1002/cne.903380108
    • (1993) J. Comp. Neurol. , vol.338 , pp. 97-113
    • Benkovic, S.A.1    Connor, J.R.2
  • 12
    • 33845892752 scopus 로고    scopus 로고
    • Systematic meta-analyses of Alzheimer disease genetic association studies: the AlzGene database
    • doi: 10.1038/ng1934
    • Bertram, L., McQueen, M. B., Mullin, K., Blacker, D., and Tanzi, R. E. (2007). Systematic meta-analyses of Alzheimer disease genetic association studies: the AlzGene database. Nat. Genet. 39, 17-23. doi: 10.1038/ng1934
    • (2007) Nat. Genet. , vol.39 , pp. 17-23
    • Bertram, L.1    McQueen, M.B.2    Mullin, K.3    Blacker, D.4    Tanzi, R.E.5
  • 13
    • 34548021006 scopus 로고    scopus 로고
    • Copper- and iron-induced differential fibril formation in alpha-synuclein: TEM study
    • doi: 10.1016/j.neulet.2007.06.052
    • Bharathi, Indi, S. S., and Rao, K. S. (2007). Copper- and iron-induced differential fibril formation in alpha-synuclein: TEM study. Neurosci. Lett. 424, 78-82. doi: 10.1016/j.neulet.2007.06.052
    • (2007) Neurosci. Lett. , vol.424 , pp. 78-82
    • Bharathi Indi, S.S.1    Rao, K.S.2
  • 14
    • 84855461629 scopus 로고    scopus 로고
    • MRI estimates of brain iron concentration in normal aging using quantitative susceptibility mapping
    • doi: 10.1016/j.neuroimage.2011.08.077
    • Bilgic, B., Pfefferbaum, A., Rohlfing, T., Sullivan, E. V., and Adalsteinsson, E. (2012). MRI estimates of brain iron concentration in normal aging using quantitative susceptibility mapping. Neuroimage 59, 2625-2635. doi: 10.1016/j.neuroimage.2011.08.077
    • (2012) Neuroimage , vol.59 , pp. 2625-2635
    • Bilgic, B.1    Pfefferbaum, A.2    Rohlfing, T.3    Sullivan, E.V.4    Adalsteinsson, E.5
  • 15
    • 33746633380 scopus 로고    scopus 로고
    • Interaction of alpha-synuclein with divalent metal ions reveals key differences: a link between structure, binding specificity and fibrillation enhancement
    • doi: 10.1021/ja0618649
    • Binolfi, A., Rasia, R. M., Bertoncini, C. W., Ceolin, M., Zweckstetter, M., Griesinger, C., et al. (2006). Interaction of alpha-synuclein with divalent metal ions reveals key differences: a link between structure, binding specificity and fibrillation enhancement. J. Am. Chem. Soc. 128, 9893-9901. doi: 10.1021/ja0618649
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 9893-9901
    • Binolfi, A.1    Rasia, R.M.2    Bertoncini, C.W.3    Ceolin, M.4    Zweckstetter, M.5    Griesinger, C.6
  • 16
    • 35148867570 scopus 로고    scopus 로고
    • Genes related to iron metabolism and susceptibility to Alzheimer's disease in Basque population
    • doi: 10.1016/j.neurobiolaging.2006.08.009
    • Blazquez, L., De Juan, D., Ruiz-Martinez, J., Emparanza, J. I., Saenz, A., Otaegui, D., et al. (2007). Genes related to iron metabolism and susceptibility to Alzheimer's disease in Basque population. Neurobiol. Aging 28, 1941-1943. doi: 10.1016/j.neurobiolaging.2006.08.009
    • (2007) Neurobiol. Aging , vol.28 , pp. 1941-1943
    • Blazquez, L.1    De Juan, D.2    Ruiz-Martinez, J.3    Emparanza, J.I.4    Saenz, A.5    Otaegui, D.6
  • 17
    • 34347370842 scopus 로고    scopus 로고
    • Selective iron chelation in Friedreich ataxia: biologic and clinical implications
    • doi: 10.1182/blood-2006-12-065433
    • Boddaert, N., Le Quan Sang, K. H., Rotig, A., Leroy-Willig, A., Gallet, S., Brunelle, F., et al. (2007). Selective iron chelation in Friedreich ataxia: biologic and clinical implications. Blood 110, 401-408. doi: 10.1182/blood-2006-12-065433
    • (2007) Blood , vol.110 , pp. 401-408
    • Boddaert, N.1    Le Quan Sang, K.H.2    Rotig, A.3    Leroy-Willig, A.4    Gallet, S.5    Brunelle, F.6
  • 18
    • 0030832287 scopus 로고    scopus 로고
    • A laser microprobe mass analysis of brain aluminum and iron in dementia pugilistica: comparison with Alzheimer's disease
    • doi: 10.1159/000112903
    • Bouras, C., Giannakopoulos, P., Good, P. F., Hsu, A., Hof, P. R., and Perl, D. P. (1997). A laser microprobe mass analysis of brain aluminum and iron in dementia pugilistica: comparison with Alzheimer's disease. Eur. Neurol. 38, 53-58. doi: 10.1159/000112903
    • (1997) Eur. Neurol. , vol.38 , pp. 53-58
    • Bouras, C.1    Giannakopoulos, P.2    Good, P.F.3    Hsu, A.4    Hof, P.R.5    Perl, D.P.6
  • 19
    • 80052758497 scopus 로고    scopus 로고
    • Iron(II) binding to amyloid-beta, the Alzheimer's peptide
    • doi: 10.1021/ic201233b
    • Bousejra-ElGarah, F., Bijani, C., Coppel, Y., Faller, P., and Hureau, C. (2011). Iron(II) binding to amyloid-beta, the Alzheimer's peptide. Inorg. Chem. 50, 9024-9030. doi: 10.1021/ic201233b
    • (2011) Inorg. Chem. , vol.50 , pp. 9024-9030
    • Bousejra-ElGarah, F.1    Bijani, C.2    Coppel, Y.3    Faller, P.4    Hureau, C.5
  • 20
    • 0027939105 scopus 로고
    • Oxidative damage and mitochondrial dysfunction in neurodegenerative diseases
    • Browne, S. E., and Beal, M. F. (1994). Oxidative damage and mitochondrial dysfunction in neurodegenerative diseases. Biochem. Soc. Trans. 22, 1002-1006.
    • (1994) Biochem. Soc. Trans. , vol.22 , pp. 1002-1006
    • Browne, S.E.1    Beal, M.F.2
  • 21
    • 23444455247 scopus 로고    scopus 로고
    • Dopamine promotes alpha-synuclein aggregation into SDS-resistant soluble oligomers via a distinct folding pathway
    • doi: 10.1096/fj.04-3437fje
    • Cappai, R., Leck, S. L., Tew, D. J., Williamson, N. A., Smith, D. P., Galatis, D., et al. (2005). Dopamine promotes alpha-synuclein aggregation into SDS-resistant soluble oligomers via a distinct folding pathway. FASEB J. 19, 1377-1379. doi: 10.1096/fj.04-3437fje
    • (2005) FASEB J. , vol.19 , pp. 1377-1379
    • Cappai, R.1    Leck, S.L.2    Tew, D.J.3    Williamson, N.A.4    Smith, D.P.5    Galatis, D.6
  • 22
    • 34548744723 scopus 로고    scopus 로고
    • Iron: the Redox-active center of oxidative stress in Alzheimer disease
    • doi: 10.1007/s11064-007-9360-7
    • Castellani, R. J., Moreira, P. I., Liu, G., Dobson, J., Perry, G., Smith, M. A., et al. (2007). Iron: the Redox-active center of oxidative stress in Alzheimer disease. Neurochem. Res. 32, 1640-1645. doi: 10.1007/s11064-007-9360-7
    • (2007) Neurochem. Res. , vol.32 , pp. 1640-1645
    • Castellani, R.J.1    Moreira, P.I.2    Liu, G.3    Dobson, J.4    Perry, G.5    Smith, M.A.6
  • 23
    • 0033947467 scopus 로고    scopus 로고
    • Sequestration of iron by Lewy bodies in Parkinson's disease
    • doi: 10.1007/s004010050001
    • Castellani, R. J., Siedlak, S. L., Perry, G., and Smith, M. A. (2000). Sequestration of iron by Lewy bodies in Parkinson's disease. Acta Neuropathol. 100, 111-114. doi: 10.1007/s004010050001
    • (2000) Acta Neuropathol. , vol.100 , pp. 111-114
    • Castellani, R.J.1    Siedlak, S.L.2    Perry, G.3    Smith, M.A.4
  • 24
    • 33750310849 scopus 로고    scopus 로고
    • Prions and their partners in crime
    • doi: 10.1038/nature05294
    • Caughey, B., and Baron, G. S. (2006). Prions and their partners in crime. Nature 443, 803-810. doi: 10.1038/nature05294
    • (2006) Nature , vol.443 , pp. 803-810
    • Caughey, B.1    Baron, G.S.2
  • 25
    • 33747429095 scopus 로고    scopus 로고
    • Dietary and genetically-induced oxidative stress alter tau phosphorylation: influence of folate and apolipoprotein E deficiency
    • Chan, A., and Shea, T. B. (2006). Dietary and genetically-induced oxidative stress alter tau phosphorylation: influence of folate and apolipoprotein E deficiency. J. Alzheimers Dis. 9, 399-405.
    • (2006) J. Alzheimers Dis. , vol.9 , pp. 399-405
    • Chan, A.1    Shea, T.B.2
  • 26
    • 4644290985 scopus 로고    scopus 로고
    • Alpha-synuclein locus duplication as a cause of familial Parkinson's disease
    • doi: 10.1016/S0140-6736(04)17103-1
    • Chartier-Harlin, M. C., Kachergus, J., Roumier, C., Mouroux, V., Douay, X., Lincoln, S., et al. (2004). Alpha-synuclein locus duplication as a cause of familial Parkinson's disease. Lancet 364, 1167-1169. doi: 10.1016/S0140-6736(04)17103-1
    • (2004) Lancet , vol.364 , pp. 1167-1169
    • Chartier-Harlin, M.C.1    Kachergus, J.2    Roumier, C.3    Mouroux, V.4    Douay, X.5    Lincoln, S.6
  • 27
    • 84885404060 scopus 로고    scopus 로고
    • Iron accumulates in Huntington's disease neurons: protection by deferoxamine
    • doi: 10.1371/journal.pone.0077023
    • Chen, J., Marks, E., Lai, B., Zhang, Z., Duce, J. A., Lam, L. Q., et al. (2013). Iron accumulates in Huntington's disease neurons: protection by deferoxamine. PLoS ONE 8:e77023. doi: 10.1371/journal.pone.0077023
    • (2013) PLoS ONE , vol.8
    • Chen, J.1    Marks, E.2    Lai, B.3    Zhang, Z.4    Duce, J.A.5    Lam, L.Q.6
  • 28
    • 33751104718 scopus 로고    scopus 로고
    • HFE mutations and Alzheimer's disease
    • Connor, J. R., and Lee, S. Y. (2006). HFE mutations and Alzheimer's disease. J. Alzheimers Dis. 10, 267-276.
    • (2006) J. Alzheimers Dis. , vol.10 , pp. 267-276
    • Connor, J.R.1    Lee, S.Y.2
  • 29
    • 0025648166 scopus 로고
    • Cellular distribution of transferrin, ferritin, and iron in normal and aged human brains
    • doi: 10.1002/jnr.490270421
    • 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
  • 30
    • 0029092802 scopus 로고
    • A quantitative analysis of isoferritins in select regions of aged, parkinsonian, and Alzheimer's diseased brains
    • doi: 10.1046/j.1471-4159.1995.65020717.x
    • Connor, J. R., Snyder, B. S., Arosio, P., Loeffler, D. A., and Lewitt, P. (1995). A quantitative analysis of isoferritins in select regions of aged, parkinsonian, and Alzheimer's diseased brains. J. Neurochem. 65, 717-724. doi: 10.1046/j.1471-4159.1995.65020717.x
    • (1995) J. Neurochem. , vol.65 , pp. 717-724
    • Connor, J.R.1    Snyder, B.S.2    Arosio, P.3    Loeffler, D.A.4    Lewitt, P.5
  • 31
    • 0026590705 scopus 로고
    • Regional distribution of iron and iron-regulatory proteins in the brain in aging and Alzheimer's disease
    • doi: 10.1002/jnr.490310214
    • Connor, J. R., Snyder, B. S., Beard, J. L., Fine, R. E., and Mufson, E. J. (1992). 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
  • 32
    • 0027327899 scopus 로고
    • Ceruloplasmin levels in the human superior temporal gyrus in aging and Alzheimer's disease
    • doi: 10.1016/0304-3940(93)90805-U
    • Connor, J. R., Tucker, P., Johnson, M., and Snyder, B. (1993). Ceruloplasmin levels in the human superior temporal gyrus in aging and Alzheimer's disease. Neurosci. Lett. 159, 88-90. doi: 10.1016/0304-3940(93)90805-U
    • (1993) Neurosci. Lett. , vol.159 , pp. 88-90
    • Connor, J.R.1    Tucker, P.2    Johnson, M.3    Snyder, B.4
  • 35
    • 33749042331 scopus 로고    scopus 로고
    • Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration
    • doi: 10.1016/j.cell.2006.09.015
    • Cui, L., Jeong, H., Borovecki, F., Parkhurst, C. N., Tanese, N., and Krainc, D. (2006). Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration. Cell 127, 59-69. doi: 10.1016/j.cell.2006.09.015
    • (2006) Cell , vol.127 , pp. 59-69
    • Cui, L.1    Jeong, H.2    Borovecki, F.3    Parkhurst, C.N.4    Tanese, N.5    Krainc, D.6
  • 36
    • 79251572323 scopus 로고    scopus 로고
    • Alpha-synuclein is a cellular ferrireductase
    • doi: 10.1371/journal.pone.0015814
    • Davies, P., Moualla, D., and Brown, D. R. (2011). Alpha-synuclein is a cellular ferrireductase. PLoS ONE 6:e15814. doi: 10.1371/journal.pone.0015814
    • (2011) PLoS ONE , vol.6
    • Davies, P.1    Moualla, D.2    Brown, D.R.3
  • 37
    • 84897930725 scopus 로고    scopus 로고
    • Targeting chelatable iron as a therapeutic modality in Parkinson's disease
    • doi: 10.1089/ars.2013.5593 [Epub ahead of print].
    • Devos, D., Moreau, C., Devedjian, J. C., Kluza, J., Petrault, M., Laloux, C., et al. (2014). Targeting chelatable iron as a therapeutic modality in Parkinson's disease. Antioxid. Redox Signal. doi: 10.1089/ars.2013.5593 [Epub ahead of print].
    • (2014) Antioxid. Redox Signal.
    • Devos, D.1    Moreau, C.2    Devedjian, J.C.3    Kluza, J.4    Petrault, M.5    Laloux, C.6
  • 38
    • 0025821265 scopus 로고
    • Alterations in the levels of iron, ferritin and other trace metals in Parkinson's disease and other neurodegenerative diseases affecting the basal ganglia
    • doi: 10.1093/brain/114.4.1953
    • Dexter, D. T., Carayon, A., Javoy-Agid, F., Agid, Y., Wells, F. R., Daniel, S. E., et al. (1991). Alterations in the levels of iron, ferritin and other trace metals in Parkinson's disease and other neurodegenerative diseases affecting the basal ganglia. Brain 114(Pt 4), 1953-1975. doi: 10.1093/brain/114.4.1953
    • (1991) Brain , vol.114 , Issue.PART 4 , pp. 1953-1975
    • Dexter, D.T.1    Carayon, A.2    Javoy-Agid, F.3    Agid, Y.4    Wells, F.R.5    Daniel, S.E.6
  • 39
    • 65249141710 scopus 로고    scopus 로고
    • Correlation of iron in the hippocampus with MMSE in patients with Alzheimer's disease
    • doi: 10.1002/jmri.21730
    • Ding, B., Chen, K. M., Ling, H. W., Sun, F., Li, X., Wan, T., et al. (2009). Correlation of iron in the hippocampus with MMSE in patients with Alzheimer's disease. J. Magn. Reson. Imaging 29, 793-798. doi: 10.1002/jmri.21730
    • (2009) J. Magn. Reson. Imaging , vol.29 , pp. 793-798
    • Ding, B.1    Chen, K.M.2    Ling, H.W.3    Sun, F.4    Li, X.5    Wan, T.6
  • 40
    • 78449268317 scopus 로고    scopus 로고
    • Prevalence of iron deficiency in children with Down syndrome
    • doi: 10.1016/j.jpeds.2010.06.011
    • Dixon, N. E., Crissman, B. G., Smith, P. B., Zimmerman, S. A., Worley, G., and Kishnani, P. S. (2010). Prevalence of iron deficiency in children with Down syndrome. J. Pediatr. 157, 967-971 e1. doi: 10.1016/j.jpeds.2010.06.011
    • (2010) J. Pediatr. , vol.157
    • Dixon, N.E.1    Crissman, B.G.2    Smith, P.B.3    Zimmerman, S.A.4    Worley, G.5    Kishnani, P.S.6
  • 41
    • 77953940704 scopus 로고    scopus 로고
    • Biological metals and Alzheimer's disease: implications for therapeutics and diagnostics
    • doi: 10.1016/j.pneurobio.2010.04.003
    • Duce, J. A., and Bush, A. I. (2010). Biological metals and Alzheimer's disease: implications for therapeutics and diagnostics. Prog. Neurobiol. 92, 1-18. doi: 10.1016/j.pneurobio.2010.04.003
    • (2010) Prog. Neurobiol. , vol.92 , pp. 1-18
    • Duce, J.A.1    Bush, A.I.2
  • 42
    • 77956647381 scopus 로고    scopus 로고
    • Iron-export ferroxidase activity of beta-amyloid precursor protein is inhibited by zinc in Alzheimer's disease
    • doi: 10.1016/j.cell.2010.08.014
    • 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
  • 43
    • 0037150687 scopus 로고    scopus 로고
    • Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease
    • doi: 10.1126/science.1072613
    • Dunah, A. W., Jeong, H., Griffin, A., Kim, Y. M., Standaert, D. G., Hersch, S. M., et al. (2002). Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease. Science 296, 2238-2243. doi: 10.1126/science.1072613
    • (2002) Science , vol.296 , pp. 2238-2243
    • Dunah, A.W.1    Jeong, H.2    Griffin, A.3    Kim, Y.M.4    Standaert, D.G.5    Hersch, S.M.6
  • 44
    • 84865051177 scopus 로고    scopus 로고
    • A synthetic peptide with the putative iron binding motif of amyloid precursor protein (APP) does not catalytically oxidize iron
    • doi: 10.1371/journal.pone.0040287
    • Ebrahimi, K. H., Hagedoorn, P. L., and Hagen, W. R. (2012). A synthetic peptide with the putative iron binding motif of amyloid precursor protein (APP) does not catalytically oxidize iron. PLoS ONE 7:e40287. doi: 10.1371/journal.pone.0040287
    • (2012) PLoS ONE , vol.7
    • Ebrahimi, K.H.1    Hagedoorn, P.L.2    Hagen, W.R.3
  • 45
    • 17644397044 scopus 로고    scopus 로고
    • Histological co-localization of iron in Abeta plaques of PS/APP transgenic mice
    • doi: 10.1007/s11064-004-2442-x
    • Falangola, M. F., Lee, S. P., Nixon, R. A., Duff, K., and Helpern, J. A. (2005). Histological co-localization of iron in Abeta plaques of PS/APP transgenic mice. Neurochem. Res. 30, 201-205. doi: 10.1007/s11064-004-2442-x
    • (2005) Neurochem. Res. , vol.30 , pp. 201-205
    • Falangola, M.F.1    Lee, S.P.2    Nixon, R.A.3    Duff, K.4    Helpern, J.A.5
  • 46
    • 0042433192 scopus 로고    scopus 로고
    • Neuromelanin associated redox-active iron is increased in the substantia nigra of patients with Parkinson's disease
    • doi: 10.1046/j.1471-4159.2003.01923.x
    • Faucheux, B. A., Martin, M. E., Beaumont, C., Hauw, J. J., Agid, Y., and Hirsch, E. C. (2003). Neuromelanin associated redox-active iron is increased in the substantia nigra of patients with Parkinson's disease. J. Neurochem. 86, 1142-1148. doi: 10.1046/j.1471-4159.2003.01923.x
    • (2003) J. Neurochem. , vol.86 , pp. 1142-1148
    • Faucheux, B.A.1    Martin, M.E.2    Beaumont, C.3    Hauw, J.J.4    Agid, Y.5    Hirsch, E.C.6
  • 47
    • 84861453955 scopus 로고    scopus 로고
    • a-Synuclein expression is modulated at the translational level by iron
    • doi: 10.1097/WNR.0b013e328354a1f0
    • Febbraro, F., Giorgi, M., Caldarola, S., Loreni, F., and Romero-Ramos, M. (2012). a-Synuclein expression is modulated at the translational level by iron. Neuroreport 23, 576-580. doi: 10.1097/WNR.0b013e328354a1f0
    • (2012) Neuroreport , vol.23 , pp. 576-580
    • Febbraro, F.1    Giorgi, M.2    Caldarola, S.3    Loreni, F.4    Romero-Ramos, M.5
  • 48
    • 18544384019 scopus 로고
    • Oxidation of tartaric acid in presence of iron
    • doi: 10.1039/ct8946500899
    • Fenton, H. J. H. (1894). Oxidation of tartaric acid in presence of iron. J. Chem. Soc. Trans. 65, 899-911. doi: 10.1039/ct8946500899
    • (1894) J. Chem. Soc. Trans. , vol.65 , pp. 899-911
    • Fenton, H.J.H.1
  • 49
    • 33751080354 scopus 로고    scopus 로고
    • Huntingtin inclusion bodies are iron-dependent centers of oxidative events
    • doi: 10.1111/j.1742-4658.2006.05537.x
    • Firdaus, W. J., Wyttenbach, A., Giuliano, P., Kretz-Remy, C., Currie, R. W., and Arrigo, A. P. (2006). Huntingtin inclusion bodies are iron-dependent centers of oxidative events. FEBS J. 273, 5428-5441. doi: 10.1111/j.1742-4658.2006.05537.x
    • (2006) FEBS J. , vol.273 , pp. 5428-5441
    • Firdaus, W.J.1    Wyttenbach, A.2    Giuliano, P.3    Kretz-Remy, C.4    Currie, R.W.5    Arrigo, A.P.6
  • 50
    • 55349106939 scopus 로고    scopus 로고
    • Mechanisms of copper ion mediated Huntington's disease progression
    • doi: 10.1371/journal.pone.0000334
    • Fox, J. H., Kama, J. A., Lieberman, G., Chopra, R., Dorsey, K., Chopra, V., et al. (2007). Mechanisms of copper ion mediated Huntington's disease progression. PLoS ONE 2:e334. doi: 10.1371/journal.pone.0000334
    • (2007) PLoS ONE , vol.2
    • Fox, J.H.1    Kama, J.A.2    Lieberman, G.3    Chopra, R.4    Dorsey, K.5    Chopra, V.6
  • 51
    • 33847320669 scopus 로고    scopus 로고
    • The 5'-untranslated region of Parkinson's disease alpha-synuclein messengerRNA contains a predicted iron responsive element
    • doi: 10.1038/sj.mp.4001937
    • Friedlich, A. L., Tanzi, R. E., and Rogers, J. T. (2007). The 5'-untranslated region of Parkinson's disease alpha-synuclein messengerRNA contains a predicted iron responsive element. Mol. Psychiatry 12, 222-223. doi: 10.1038/sj.mp.4001937
    • (2007) Mol. Psychiatry , vol.12 , pp. 222-223
    • Friedlich, A.L.1    Tanzi, R.E.2    Rogers, J.T.3
  • 52
    • 34147109175 scopus 로고    scopus 로고
    • Phenotypic variation in a large Swedish pedigree due to SNCA duplication and triplication
    • doi: 10.1212/01.wnl.0000254458.17630.c5
    • Fuchs, J., Nilsson, C., Kachergus, J., Munz, M., Larsson, E. M., Schule, B., et al. (2007). Phenotypic variation in a large Swedish pedigree due to SNCA duplication and triplication. Neurology 68, 916-922. doi: 10.1212/01.wnl.0000254458.17630.c5
    • (2007) Neurology , vol.68 , pp. 916-922
    • Fuchs, J.1    Nilsson, C.2    Kachergus, J.3    Munz, M.4    Larsson, E.M.5    Schule, B.6
  • 53
    • 34548767817 scopus 로고    scopus 로고
    • Voltage-gated calcium channels provide an alternate route for iron uptake in neuronal cell cultures
    • doi: 10.1007/s11064-007-9313-1
    • Gaasch, J. A., Geldenhuys, W. J., Lockman, P. R., Allen, D. D., and Van Der Schyf, C. J. (2007). Voltage-gated calcium channels provide an alternate route for iron uptake in neuronal cell cultures. Neurochem. Res. 32, 1686-1693. doi: 10.1007/s11064-007-9313-1
    • (2007) Neurochem. Res. , vol.32 , pp. 1686-1693
    • Gaasch, J.A.1    Geldenhuys, W.J.2    Lockman, P.R.3    Allen, D.D.4    Van Der Schyf, C.J.5
  • 54
    • 84855801337 scopus 로고    scopus 로고
    • Modest amyloid deposition is associated with iron dysregulation, microglial activation, and oxidative stress
    • doi: 10.3233/JAD-2011-110614
    • 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
  • 55
    • 34548636261 scopus 로고    scopus 로고
    • Immunohistochemical localization of TRPC6 in the rat substantia nigra
    • doi: 10.1016/j.neulet.2007.07.049
    • Giampa, C., Demarch, Z., Patassini, S., Bernardi, G., and Fusco, F. R. (2007). Immunohistochemical localization of TRPC6 in the rat substantia nigra. Neurosci. Lett. 424, 170-174. doi: 10.1016/j.neulet.2007.07.049
    • (2007) Neurosci. Lett. , vol.424 , pp. 170-174
    • Giampa, C.1    Demarch, Z.2    Patassini, S.3    Bernardi, G.4    Fusco, F.R.5
  • 56
    • 0034602442 scopus 로고    scopus 로고
    • Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions
    • doi: 10.1126/science.290.5493.985
    • Giasson, B. I., Duda, J. E., Murray, I. V., Chen, Q., Souza, J. M., Hurtig, H. I., et al. (2000). Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions. Science 290, 985-989. doi: 10.1126/science.290.5493.985
    • (2000) Science , vol.290 , pp. 985-989
    • Giasson, B.I.1    Duda, J.E.2    Murray, I.V.3    Chen, Q.4    Souza, J.M.5    Hurtig, H.I.6
  • 57
    • 0027193251 scopus 로고
    • Distribution of iron in the basal ganglia and neocortex in postmortem tissue in Parkinson's disease and Alzheimer's disease
    • Griffiths, P. D., and Crossman, A. R. (1993). Distribution of iron in the basal ganglia and neocortex in postmortem tissue in Parkinson's disease and Alzheimer's disease. Dementia 4, 61-65.
    • (1993) Dementia , vol.4 , pp. 61-65
    • Griffiths, P.D.1    Crossman, A.R.2
  • 58
    • 0025648873 scopus 로고
    • Ferritin is a component of the neuritic (senile) plaque in Alzheimer dementia
    • doi: 10.1007/BF00334497
    • 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
  • 59
    • 34249041646 scopus 로고    scopus 로고
    • Metal ions differentially influence the aggregation and deposition of Alzheimer's beta-amyloid on a solid template
    • doi: 10.1021/bi7000032
    • Ha, C., Ryu, J., and Park, C. B. (2007). Metal ions differentially influence the aggregation and deposition of Alzheimer's beta-amyloid on a solid template. Biochemistry 46, 6118-6125. doi: 10.1021/bi7000032
    • (2007) Biochemistry , vol.46 , pp. 6118-6125
    • Ha, C.1    Ryu, J.2    Park, C.B.3
  • 60
    • 13944261999 scopus 로고    scopus 로고
    • Imaging iron stores in the brain using magnetic resonance imaging
    • doi: 10.1016/j.mri.2004.10.001
    • Haacke, E. M., Cheng, N. Y., House, M. J., Liu, Q., Neelavalli, J., Ogg, R. J., et al. (2005). Imaging iron stores in the brain using magnetic resonance imaging. Magn. Reson. Imaging 23, 1-25. doi: 10.1016/j.mri.2004.10.001
    • (2005) Magn. Reson. Imaging , vol.23 , pp. 1-25
    • Haacke, E.M.1    Cheng, N.Y.2    House, M.J.3    Liu, Q.4    Neelavalli, J.5    Ogg, R.J.6
  • 61
    • 0000162325 scopus 로고
    • The catalytic decomposition of hydrogen peroxide by iron salts
    • doi: 10.1098/rspa.1934.0221
    • Haber, F., and Weiss, J. (1934). The catalytic decomposition of hydrogen peroxide by iron salts. Proc. R. Soc. Lond. A 147, 332-351. doi: 10.1098/rspa.1934.0221
    • (1934) Proc. R. Soc. Lond. A , vol.147 , pp. 332-351
    • Haber, F.1    Weiss, J.2
  • 62
    • 84887103102 scopus 로고    scopus 로고
    • A low-molecular-weight ferroxidase is increased in the CSF of sCJD cases: CSF ferroxidase and transferrin as diagnostic biomarkers for sCJD
    • doi: 10.1089/ars.2012.5032
    • Haldar, S., Beveridge, J., Wong, J., Singh, A., Galimberti, D., Borroni, B., et al. (2013). A low-molecular-weight ferroxidase is increased in the CSF of sCJD cases: CSF ferroxidase and transferrin as diagnostic biomarkers for sCJD. Antioxid. Redox Signal. 19, 1662-1675. doi: 10.1089/ars.2012.5032
    • (2013) Antioxid. Redox Signal. , vol.19 , pp. 1662-1675
    • Haldar, S.1    Beveridge, J.2    Wong, J.3    Singh, A.4    Galimberti, D.5    Borroni, B.6
  • 63
    • 76749134242 scopus 로고    scopus 로고
    • Prolyl-peptidyl isomerase, Pin1, phosphorylation is compromised in association with the expression of the HFE polymorphic allele, H63D
    • doi: 10.1016/j.bbadis.2010.01.004
    • Hall, E. C. II, Lee, S. Y., Simmons, Z., Neely, E. B., Nandar, W., and Connor, J. R. (2010). Prolyl-peptidyl isomerase, Pin1, phosphorylation is compromised in association with the expression of the HFE polymorphic allele, H63D. Biochim. Biophys. Acta 1802, 389-395. doi: 10.1016/j.bbadis.2010.01.004
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 389-395
    • Hall II, E.C.1    Lee, S.Y.2    Simmons, Z.3    Neely, E.B.4    Nandar, W.5    Connor, J.R.6
  • 64
    • 0026773281 scopus 로고
    • Oxygen radicals as key mediators in neurological disease: fact or fiction?
    • doi: 10.1002/ana.410320704
    • Halliwell, B. (1992). Oxygen radicals as key mediators in neurological disease: fact or fiction? Ann. Neurol. 32(Suppl.), S10-S15. doi: 10.1002/ana.410320704
    • (1992) Ann. Neurol. , vol.32 , Issue.SUPPL.
    • Halliwell, B.1
  • 65
    • 77957905690 scopus 로고    scopus 로고
    • Genetic analysis of pathways to Parkinson disease
    • doi: 10.1016/j.neuron.2010.10.014
    • Hardy, J. (2010). Genetic analysis of pathways to Parkinson disease. Neuron 68, 201-206. doi: 10.1016/j.neuron.2010.10.014
    • (2010) Neuron , vol.68 , pp. 201-206
    • Hardy, J.1
  • 66
    • 84900302515 scopus 로고    scopus 로고
    • An iron-dopamine index predicts risk of parkinsonian neurodegeneration in the substantia nigra pars compacta
    • doi: 10.1039/C3SC53461H [Epub ahead of print].
    • Hare, D. J., Lei, P., Ayton, S., Roberts, B. R., Grimm, R., George, J. L., et al. (2014). An iron-dopamine index predicts risk of parkinsonian neurodegeneration in the substantia nigra pars compacta. Chem. Sci. doi: 10.1039/C3SC53461H [Epub ahead of print].
    • (2014) Chem. Sci.
    • Hare, D.J.1    Lei, P.2    Ayton, S.3    Roberts, B.R.4    Grimm, R.5    George, J.L.6
  • 67
    • 70450189083 scopus 로고    scopus 로고
    • Selective neuronal requirement for huntingtin in the developing zebrafish
    • doi: 10.1093/hmg/ddp455
    • Henshall, T. L., Tucker, B., Lumsden, A. L., Nornes, S., Lardelli, M. T., and Richards, R. I. (2009). Selective neuronal requirement for huntingtin in the developing zebrafish. Hum. Mol. Genet. 18, 4830-4842. doi: 10.1093/hmg/ddp455
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 4830-4842
    • Henshall, T.L.1    Tucker, B.2    Lumsden, A.L.3    Nornes, S.4    Lardelli, M.T.5    Richards, R.I.6
  • 68
    • 84856404655 scopus 로고    scopus 로고
    • Thalassaemia
    • doi: 10.1016/S0140-6736(11)60283-3
    • Higgs, D. R., Engel, J. D., and Stamatoyannopoulos, G. (2012). Thalassaemia. Lancet 379, 373-383. doi: 10.1016/S0140-6736(11)60283-3
    • (2012) Lancet , vol.379 , pp. 373-383
    • Higgs, D.R.1    Engel, J.D.2    Stamatoyannopoulos, G.3
  • 69
    • 0034703860 scopus 로고    scopus 로고
    • Huntingtin: an iron-regulated protein essential for normal nuclear and perinuclear organelles
    • doi: 10.1093/hmg/9.19.2789
    • Hilditch-Maguire, P., Trettel, F., Passani, L. A., Auerbach, A., Persichetti, F., and Macdonald, M. E. (2000). Huntingtin: an iron-regulated protein essential for normal nuclear and perinuclear organelles. Hum. Mol. Genet. 9, 2789-2797. doi: 10.1093/hmg/9.19.2789
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2789-2797
    • Hilditch-Maguire, P.1    Trettel, F.2    Passani, L.A.3    Auerbach, A.4    Persichetti, F.5    Macdonald, M.E.6
  • 70
    • 34248569814 scopus 로고    scopus 로고
    • Altered regulation of iron transport and storage in Parkinson's disease
    • Hirsch, E. C. (2006). Altered regulation of iron transport and storage in Parkinson's disease. J. Neural Transm. Suppl. 201-204.
    • (2006) J. Neural Transm. Suppl. , pp. 201-204
    • Hirsch, E.C.1
  • 71
    • 84931266069 scopus 로고    scopus 로고
    • The amyloid precursor protein (APP) does not have a ferroxidase site in its E2 domain
    • doi: 10.1371/journal.pone.0072177
    • Honarmand Ebrahimi, K., Dienemann, C., Hoefgen, S., Than, M. E., Hagedoorn, P. L., and Hagen, W. R. (2013). The amyloid precursor protein (APP) does not have a ferroxidase site in its E2 domain. PLoS ONE 8:e72177. doi: 10.1371/journal.pone.0072177
    • (2013) PLoS ONE , vol.8
    • Honarmand Ebrahimi, K.1    Dienemann, C.2    Hoefgen, S.3    Than, M.E.4    Hagedoorn, P.L.5    Hagen, W.R.6
  • 72
    • 12144282992 scopus 로고    scopus 로고
    • Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer's Abeta peptides
    • doi: 10.1007/s00775-004-0602-8
    • Huang, X., Atwood, C. S., Moir, R. D., Hartshorn, M. A., Tanzi, R. E., and Bush, A. I. (2004). Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer's Abeta peptides. J. Biol. Inorg. Chem. 9, 954-960. doi: 10.1007/s00775-004-0602-8
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 954-960
    • Huang, X.1    Atwood, C.S.2    Moir, R.D.3    Hartshorn, M.A.4    Tanzi, R.E.5    Bush, A.I.6
  • 73
    • 0030848219 scopus 로고    scopus 로고
    • Carboxyl-terminal fragments of beta-amyloid precursor protein bind to microtubules and the associated protein tau
    • Islam, K., and Levy, E. (1997). Carboxyl-terminal fragments of beta-amyloid precursor protein bind to microtubules and the associated protein tau. Am. J. Pathol. 151, 265-271.
    • (1997) Am. J. Pathol. , vol.151 , pp. 265-271
    • Islam, K.1    Levy, E.2
  • 74
    • 27344439224 scopus 로고    scopus 로고
    • In vivo magnetic resonance microimaging of individual amyloid plaques in Alzheimer's transgenic mice
    • doi: 10.1523/JNEUROSCI.2588-05.2005
    • Jack, C. R. Jr., Wengenack, T. M., Reyes, D. A., Garwood, M., Curran, G. L., Borowski, B. J., et al. (2005). In vivo magnetic resonance microimaging of individual amyloid plaques in Alzheimer's transgenic mice. J. Neurosci. 25, 10041-10048. doi: 10.1523/JNEUROSCI.2588-05.2005
    • (2005) J. Neurosci. , vol.25 , pp. 10041-10048
    • Jack Jr., C.R.1    Wengenack, T.M.2    Reyes, D.A.3    Garwood, M.4    Curran, G.L.5    Borowski, B.J.6
  • 75
    • 84864923612 scopus 로고    scopus 로고
    • Physiologic implications of metal-ion transport by ZIP14 and ZIP8
    • doi: 10.1007/s10534-012-9526-x
    • Jenkitkasemwong, S., Wang, C. Y., Mackenzie, B., and Knutson, M. D. (2012). Physiologic implications of metal-ion transport by ZIP14 and ZIP8. Biometals 25, 643-655. doi: 10.1007/s10534-012-9526-x
    • (2012) Biometals , vol.25 , pp. 643-655
    • Jenkitkasemwong, S.1    Wang, C.Y.2    Mackenzie, B.3    Knutson, M.D.4
  • 76
    • 0038711587 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system
    • doi: 10.1074/jbc. M301988200
    • Jeong, S. Y., and David, S. (2003). Glycosylphosphatidylinositol-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system. J. Biol. Chem. 278, 27144-27148. doi: 10.1074/jbc. M301988200
    • (2003) J. Biol. Chem. , vol.278 , pp. 27144-27148
    • Jeong, S.Y.1    David, S.2
  • 77
    • 0242684415 scopus 로고    scopus 로고
    • Genetic or pharmacological iron chelation prevents MPTP-induced neurotoxicity in vivo: a novel therapy for Parkinson's disease
    • doi: 10.1016/S0896-6273(03)00126-0
    • Kaur, D., Yantiri, F., Rajagopalan, S., Kumar, J., Mo, J. Q., Boonplueang, R., et al. (2003). Genetic or pharmacological iron chelation prevents MPTP-induced neurotoxicity in vivo: a novel therapy for Parkinson's disease. Neuron 37, 899-909. doi: 10.1016/S0896-6273(03)00126-0
    • (2003) Neuron , vol.37 , pp. 899-909
    • Kaur, D.1    Yantiri, F.2    Rajagopalan, S.3    Kumar, J.4    Mo, J.Q.5    Boonplueang, R.6
  • 78
    • 34748899552 scopus 로고    scopus 로고
    • Brain iron metabolism: neurobiology and neurochemistry
    • doi: 10.1016/j.pneurobio.2007.07.009
    • Ke, Y., and Qian, Z. M. (2007). Brain iron metabolism: neurobiology and neurochemistry. Prog. Neurobiol. 83, 149-173. doi: 10.1016/j.pneurobio.2007.07.009
    • (2007) Prog. Neurobiol. , vol.83 , pp. 149-173
    • Ke, Y.1    Qian, Z.M.2
  • 79
    • 34447505975 scopus 로고    scopus 로고
    • Alteration of iron regulatory proteins (IRP1 and IRP2) and ferritin in the brains of scrapie-infected mice
    • doi: 10.1016/j.neulet.2007.05.061
    • Kim, B. H., Jun, Y. C., Jin, J. K., Kim, J. I., Kim, N. H., Leibold, E. A., et al. (2007). Alteration of iron regulatory proteins (IRP1 and IRP2) and ferritin in the brains of scrapie-infected mice. Neurosci. Lett. 422, 158-163. doi: 10.1016/j.neulet.2007.05.061
    • (2007) Neurosci. Lett. , vol.422 , pp. 158-163
    • Kim, B.H.1    Jun, Y.C.2    Jin, J.K.3    Kim, J.I.4    Kim, N.H.5    Leibold, E.A.6
  • 80
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease
    • doi: 10.1038/ng0298-106
    • Kruger, R., Kuhn, W., Muller, T., Woitalla, D., Graeber, M., Kosel, S., et al. (1998). Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease. Nat. Genet. 18, 106-108. doi: 10.1038/ng0298-106
    • (1998) Nat. Genet. , vol.18 , pp. 106-108
    • Kruger, R.1    Kuhn, W.2    Muller, T.3    Woitalla, D.4    Graeber, M.5    Kosel, S.6
  • 81
    • 78649734938 scopus 로고    scopus 로고
    • Two routes of iron accumulation in astrocytes: ascorbate-dependent ferrous iron uptake via the divalent metal transporter (DMT1) plus an independent route for ferric iron
    • doi: 10.1042/BJ20101317
    • Lane, D. J., Robinson, S. R., Czerwinska, H., Bishop, G. M., and Lawen, A. (2010). Two routes of iron accumulation in astrocytes: ascorbate-dependent ferrous iron uptake via the divalent metal transporter (DMT1) plus an independent route for ferric iron. Biochem. J. 432, 123-132. doi: 10.1042/BJ20101317
    • (2010) Biochem. J. , vol.432 , pp. 123-132
    • Lane, D.J.1    Robinson, S.R.2    Czerwinska, H.3    Bishop, G.M.4    Lawen, A.5
  • 82
    • 48949098573 scopus 로고    scopus 로고
    • Safety, efficacy, and biomarker findings of PBT2 in targeting Abeta as a modifying therapy for Alzheimer's disease: a phase IIa, double-blind, randomised, placebo-controlled trial
    • doi: 10.1016/S1474-4422(08)70167-4
    • Lannfelt, L., Blennow, K., Zetterberg, H., Batsman, S., Ames, D., Harrison, J., et al. (2008). Safety, efficacy, and biomarker findings of PBT2 in targeting Abeta as a modifying therapy for Alzheimer's disease: a phase IIa, double-blind, randomised, placebo-controlled trial. Lancet Neurol. 7, 779-786. doi: 10.1016/S1474-4422(08)70167-4
    • (2008) Lancet Neurol. , vol.7 , pp. 779-786
    • Lannfelt, L.1    Blennow, K.2    Zetterberg, H.3    Batsman, S.4    Ames, D.5    Harrison, J.6
  • 83
    • 84856708923 scopus 로고    scopus 로고
    • Tau deficiency induces parkinsonism with dementia by impairing APP-mediated iron export
    • doi: 10.1038/nm.2613
    • Lei, P., Ayton, S., Finkelstein, D. I., Spoerri, L., Ciccotosto, G. D., Wright, D. K., et al. (2012). Tau deficiency induces parkinsonism with dementia by impairing APP-mediated iron export. Nat. Med. 18, 291-295. doi: 10.1038/nm.2613
    • (2012) Nat. Med. , vol.18 , pp. 291-295
    • Lei, P.1    Ayton, S.2    Finkelstein, D.I.3    Spoerri, L.4    Ciccotosto, G.D.5    Wright, D.K.6
  • 84
    • 0030788672 scopus 로고    scopus 로고
    • Iron deposits in multiple sclerosis and Alzheimer's disease brains
    • doi: 10.1016/S0006-8993(97)00470-8
    • 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
  • 85
    • 79952996094 scopus 로고    scopus 로고
    • Iron promotes the toxicity of amyloid beta peptide by impeding its ordered aggregation
    • doi: 10.1074/jbc. M110.158980
    • Liu, B., Moloney, A., Meehan, S., Morris, K., Thomas, S. E., Serpell, L.C., et al. (2011). Iron promotes the toxicity of amyloid beta peptide by impeding its ordered aggregation. J. Biol. Chem. 286, 4248-4256. doi: 10.1074/jbc. M110.158980
    • (2011) J. Biol. Chem. , vol.286 , pp. 4248-4256
    • Liu, B.1    Moloney, A.2    Meehan, S.3    Morris, K.4    Thomas, S.E.5    Serpell, L.C.6
  • 86
    • 84856282075 scopus 로고    scopus 로고
    • Differential effect of nimodipine in attenuating iron-induced toxicity in brain- and blood-brain barrier-associated cell types
    • doi: 10.1007/s11064-011-0591-2
    • Lockman, J. A., Geldenhuys, W. J., Bohn, K. A., Desilva, S. F., Allen, D. D., and Van Der Schyf, C. J. (2012). Differential effect of nimodipine in attenuating iron-induced toxicity in brain- and blood-brain barrier-associated cell types. Neurochem. Res. 37, 134-142. doi: 10.1007/s11064-011-0591-2
    • (2012) Neurochem. Res. , vol.37 , pp. 134-142
    • Lockman, J.A.1    Geldenhuys, W.J.2    Bohn, K.A.3    Desilva, S.F.4    Allen, D.D.5    Van Der Schyf, C.J.6
  • 87
    • 0029153619 scopus 로고
    • Transferrin and iron in normal, Alzheimer's disease, and Parkinson's disease brain regions
    • doi: 10.1046/j.1471-4159.1995.65020710.x
    • Loeffler, D. A., Connor, J. R., Juneau, P. L., Snyder, B. S., Kanaley, L., Demaggio, A. J., et al. (1995). Transferrin and iron in normal, Alzheimer's disease, and Parkinson's disease brain regions. J. Neurochem. 65, 710-724. doi: 10.1046/j.1471-4159.1995.65020710.x
    • (1995) J. Neurochem. , vol.65 , pp. 710-724
    • Loeffler, D.A.1    Connor, J.R.2    Juneau, P.L.3    Snyder, B.S.4    Kanaley, L.5    Demaggio, A.J.6
  • 88
    • 0036884733 scopus 로고    scopus 로고
    • Pathogenesis of Parkinson's disease: dopamine, vesicles and alpha-synuclein
    • doi: 10.1038/nrn983
    • Lotharius, J., and Brundin, P. (2002). Pathogenesis of Parkinson's disease: dopamine, vesicles and alpha-synuclein. Nat. Rev. Neurosci. 3, 932-942. doi: 10.1038/nrn983
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 932-942
    • Lotharius, J.1    Brundin, P.2
  • 89
    • 12844250694 scopus 로고    scopus 로고
    • Induction of hyperphosphorylated tau in primary rat cortical neuron cultures mediated by oxidative stress and glycogen synthase kinase-3
    • discussion 673-681
    • Lovell, M. A., Xiong, S., Xie, C., Davies, P., and Markesbery, W. R. (2004). Induction of hyperphosphorylated tau in primary rat cortical neuron cultures mediated by oxidative stress and glycogen synthase kinase-3. J. Alzheimers Dis. 6, 659-671; discussion 673-681.
    • (2004) J. Alzheimers Dis. , vol.6 , pp. 659-671
    • Lovell, M.A.1    Xiong, S.2    Xie, C.3    Davies, P.4    Markesbery, W.R.5
  • 90
    • 34548406422 scopus 로고    scopus 로고
    • Huntingtin-deficient zebrafish exhibit defects in iron utilization and development
    • doi: 10.1093/hmg/ddm138
    • Lumsden, A. L., Henshall, T. L., Dayan, S., Lardelli, M. T., and Richards, R. I. (2007). Huntingtin-deficient zebrafish exhibit defects in iron utilization and development. Hum. Mol. Genet. 16, 1905-1920. doi: 10.1093/hmg/ddm138
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 1905-1920
    • Lumsden, A.L.1    Henshall, T.L.2    Dayan, S.3    Lardelli, M.T.4    Richards, R.I.5
  • 91
    • 33645407628 scopus 로고    scopus 로고
    • Copper binding properties of a tau peptide associated with Alzheimer's disease studied by CD, NMR, and MALDI-TOF MS
    • doi: 10.1016/j.peptides.2005.09.002
    • Ma, Q., Li, Y., Du, J., Liu, H., Kanazawa, K., Nemoto, T., et al. (2006). Copper binding properties of a tau peptide associated with Alzheimer's disease studied by CD, NMR, and MALDI-TOF MS. Peptides 27, 841-849. doi: 10.1016/j.peptides.2005.09.002
    • (2006) Peptides , vol.27 , pp. 841-849
    • Ma, Q.1    Li, Y.2    Du, J.3    Liu, H.4    Kanazawa, K.5    Nemoto, T.6
  • 92
    • 0033134765 scopus 로고    scopus 로고
    • Existing and emerging mechanisms for transport of iron and manganese to the brain
    • Malecki, E. A., Devenyi, A. G., Beard, J. L., and Connor, J. R. (1999). Existing and emerging mechanisms for transport of iron and manganese to the brain. J. Neurosci. Res. 56, 113-122.
    • (1999) J. Neurosci. Res. , vol.56 , pp. 113-122
    • Malecki, E.A.1    Devenyi, A.G.2    Beard, J.L.3    Connor, J.R.4
  • 93
    • 34147157711 scopus 로고    scopus 로고
    • Pyrrolidine dithiocarbamate activates Akt and improves spatial learning in APP/PS1 mice without affecting beta-amyloid burden
    • doi: 10.1523/JNEUROSCI.0059-07.2007
    • Malm, T. M., Iivonen, H., Goldsteins, G., Keksa-Goldsteine, V., Ahtoniemi, T., Kanninen, K., et al. (2007). Pyrrolidine dithiocarbamate activates Akt and improves spatial learning in APP/PS1 mice without affecting beta-amyloid burden. J. Neurosci. 27, 3712-3721. doi: 10.1523/JNEUROSCI.0059-07.2007
    • (2007) J. Neurosci. , vol.27 , pp. 3712-3721
    • Malm, T.M.1    Iivonen, H.2    Goldsteins, G.3    Keksa-Goldsteine, V.4    Ahtoniemi, T.5    Kanninen, K.6
  • 94
    • 66149090377 scopus 로고    scopus 로고
    • MRI and histological analysis of beta-amyloid plaques in both human Alzheimer's disease and APP/PS1 transgenic mice
    • doi: 10.1002/jmri.21731
    • 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
  • 95
    • 67349215018 scopus 로고    scopus 로고
    • MRI characteristics of the substantia nigra in Parkinson's disease: a combined quantitative T1 and DTI study
    • doi: 10.1016/j.neuroimage.2009.05.017
    • Menke, R. A., Scholz, J., Miller, K. L., Deoni, S., Jbabdi, S., Matthews, P. M., et al. (2009). MRI characteristics of the substantia nigra in Parkinson's disease: a combined quantitative T1 and DTI study. Neuroimage 47, 435-441. doi: 10.1016/j.neuroimage.2009.05.017
    • (2009) Neuroimage , vol.47 , pp. 435-441
    • Menke, R.A.1    Scholz, J.2    Miller, K.L.3    Deoni, S.4    Jbabdi, S.5    Matthews, P.M.6
  • 96
    • 44649108912 scopus 로고    scopus 로고
    • Neuroprotective actions of deferiprone in cultured cortical neurones and SHSY-5Y cells
    • doi: 10.1111/j.1471-4159.2008.05332.x
    • Molina-Holgado, F., Gaeta, A., Francis, P. T., Williams, R. J., and Hider, R. C. (2008). Neuroprotective actions of deferiprone in cultured cortical neurones and SHSY-5Y cells. J. Neurochem. 105, 2466-2476. doi: 10.1111/j.1471-4159.2008.05332.x
    • (2008) J. Neurochem. , vol.105 , pp. 2466-2476
    • Molina-Holgado, F.1    Gaeta, A.2    Francis, P.T.3    Williams, R.J.4    Hider, R.C.5
  • 97
    • 33750738079 scopus 로고    scopus 로고
    • Ferroportin in the postnatal rat brain: implications for axonal transport and neuronal export of iron
    • doi: 10.1016/j.spen.2006.08.003
    • Moos, T., and Rosengren Nielsen, T. (2006). Ferroportin in the postnatal rat brain: implications for axonal transport and neuronal export of iron. Semin. Pediatr. Neurol. 13, 149-157. doi: 10.1016/j.spen.2006.08.003
    • (2006) Semin. Pediatr. Neurol. , vol.13 , pp. 149-157
    • Moos, T.1    Rosengren Nielsen, T.2
  • 98
    • 0028694082 scopus 로고
    • Non-haem iron histochemistry of the normal and Alzheimer's disease hippocampus
    • Morris, C. M., Kerwin, J. M., and Edwardson, J. A. (1994). Non-haem iron histochemistry of the normal and Alzheimer's disease hippocampus. Neurodegeneration 3, 267-275.
    • (1994) Neurodegeneration , vol.3 , pp. 267-275
    • Morris, C.M.1    Kerwin, J.M.2    Edwardson, J.A.3
  • 99
    • 50949102412 scopus 로고    scopus 로고
    • Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network
    • doi: 10.1146/annurev.nutr.28.061807.155521
    • Muckenthaler, M. U., Galy, B., and Hentze, M. W. (2008). Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network. Annu. Rev. Nutr. 28, 197-213. doi: 10.1146/annurev.nutr.28.061807.155521
    • (2008) Annu. Rev. Nutr. , vol.28 , pp. 197-213
    • Muckenthaler, M.U.1    Galy, B.2    Hentze, M.W.3
  • 100
    • 1642545649 scopus 로고    scopus 로고
    • Role of transient receptor potential canonical 6 (TRPC6) in non-transferrin-bound iron uptake in neuronal phenotype PC12 cells
    • doi: 10.1042/BJ20031187
    • Mwanjewe, J., and Grover, A. K. (2004). Role of transient receptor potential canonical 6 (TRPC6) in non-transferrin-bound iron uptake in neuronal phenotype PC12 cells. Biochem. J. 378, 975-982. doi: 10.1042/BJ20031187
    • (2004) Biochem. J. , vol.378 , pp. 975-982
    • Mwanjewe, J.1    Grover, A.K.2
  • 101
    • 79955492902 scopus 로고    scopus 로고
    • HFE gene variants affect iron in the brain
    • doi: 10.3945/jn.110.130351
    • Nandar, W., and Connor, J. R. (2011). HFE gene variants affect iron in the brain. J. Nutr. 141, 729S-739S. doi: 10.3945/jn.110.130351
    • (2011) J. Nutr. , vol.141
    • Nandar, W.1    Connor, J.R.2
  • 102
    • 0035937523 scopus 로고    scopus 로고
    • Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity
    • doi: 10.1126/science.1056784
    • Nucifora, F. C. Jr., Sasaki, M., Peters, M. F., Huang, H., Cooper, J. K., Yamada, M., et al. (2001). Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity. Science 291, 2423-2428. doi: 10.1126/science.1056784
    • (2001) Science , vol.291 , pp. 2423-2428
    • Nucifora Jr., F.C.1    Sasaki, M.2    Peters, M.F.3    Huang, H.4    Cooper, J.K.5    Yamada, M.6
  • 103
    • 83455177604 scopus 로고    scopus 로고
    • Ceruloplasmin oxidation, a feature of Parkinson's disease CSF, inhibits ferroxidase activity and promotes cellular iron retention
    • doi: 10.1523/JNEUROSCI.3768-11.2011
    • Olivieri, S., Conti, A., Iannaccone, S., Cannistraci, C. V., Campanella, A., Barbariga, M., et al. (2011). Ceruloplasmin oxidation, a feature of Parkinson's disease CSF, inhibits ferroxidase activity and promotes cellular iron retention. J. Neurosci. 31, 18568-18577. doi: 10.1523/JNEUROSCI.3768-11.2011
    • (2011) J. Neurosci. , vol.31 , pp. 18568-18577
    • Olivieri, S.1    Conti, A.2    Iannaccone, S.3    Cannistraci, C.V.4    Campanella, A.5    Barbariga, M.6
  • 104
    • 0036327065 scopus 로고    scopus 로고
    • Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines
    • doi: 10.1038/nn884
    • Panov, A. V., Gutekunst, C. A., Leavitt, B. R., Hayden, M. R., Burke, J. R., Strittmatter, W. J., et al. (2002). Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines. Nat. Neurosci. 5, 731-736. doi: 10.1038/nn884
    • (2002) Nat. Neurosci. , vol.5 , pp. 731-736
    • Panov, A.V.1    Gutekunst, C.A.2    Leavitt, B.R.3    Hayden, M.R.4    Burke, J.R.5    Strittmatter, W.J.6
  • 105
    • 84155160629 scopus 로고    scopus 로고
    • Expression of divalent metal transporter 1 in primary hippocampal neurons: reconsidering its role in non-transferrin-bound iron influx
    • doi: 10.1111/j.1471-4159.2011.07578.x
    • Pelizzoni, I., Zacchetti, D., Smith, C. P., Grohovaz, F., and Codazzi, F. (2012). Expression of divalent metal transporter 1 in primary hippocampal neurons: reconsidering its role in non-transferrin-bound iron influx. J. Neurochem. 120, 269-278. doi: 10.1111/j.1471-4159.2011.07578.x
    • (2012) J. Neurochem. , vol.120 , pp. 269-278
    • Pelizzoni, I.1    Zacchetti, D.2    Smith, C.P.3    Grohovaz, F.4    Codazzi, F.5
  • 106
    • 26444549058 scopus 로고    scopus 로고
    • Redox metals and oxidative abnormalities in human prion diseases
    • doi: 10.1007/s00401-005-1034-4
    • Petersen, R. B., Siedlak, S. L., Lee, H. G., Kim, Y. S., Nunomura, A., Tagliavini, F., et al. (2005). Redox metals and oxidative abnormalities in human prion diseases. Acta Neuropathol. 110, 232-238. doi: 10.1007/s00401-005-1034-4
    • (2005) Acta Neuropathol. , vol.110 , pp. 232-238
    • Petersen, R.B.1    Siedlak, S.L.2    Lee, H.G.3    Kim, Y.S.4    Nunomura, A.5    Tagliavini, F.6
  • 107
    • 80053210392 scopus 로고    scopus 로고
    • Zip14 is a complex broad-scope metal-ion transporter whose functional properties support roles in the cellular uptake of zinc and nontransferrin-bound iron
    • doi: 10.1152/ajpcell.00479.2010
    • Pinilla-Tenas, J. J., Sparkman, B. K., Shawki, A., Illing, A. C., Mitchell, C. J., Zhao, N., et al. (2011). Zip14 is a complex broad-scope metal-ion transporter whose functional properties support roles in the cellular uptake of zinc and nontransferrin-bound iron. Am. J. Physiol. Cell Physiol. 301, C862-C871. doi: 10.1152/ajpcell.00479.2010
    • (2011) Am. J. Physiol. Cell Physiol. , vol.301
    • Pinilla-Tenas, J.J.1    Sparkman, B.K.2    Shawki, A.3    Illing, A.C.4    Mitchell, C.J.5    Zhao, N.6
  • 108
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the alpha-synuclein gene identified in families with Parkinson's disease
    • doi: 10.1126/science.276.5321.2045
    • Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., et al. (1997). Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science 276, 2045-2047. doi: 10.1126/science.276.5321.2045
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3    Ide, S.E.4    Dehejia, A.5    Dutra, A.6
  • 109
    • 84861525034 scopus 로고    scopus 로고
    • Deferiprone reduces amyloid-beta and tau phosphorylation levels but not reactive oxygen species generation in hippocampus of rabbits fed a cholesterol-enriched diet
    • doi: 10.3233/JAD-2012-111346
    • Prasanthi, J. R., Schrag, M., Dasari, B., Marwarha, G., Dickson, A., Kirsch, W. M., et al. (2012). Deferiprone reduces amyloid-beta and tau phosphorylation levels but not reactive oxygen species generation in hippocampus of rabbits fed a cholesterol-enriched diet. J. Alzheimers Dis. 30, 167-182. doi: 10.3233/JAD-2012-111346
    • (2012) J. Alzheimers Dis. , vol.30 , pp. 167-182
    • Prasanthi, J.R.1    Schrag, M.2    Dasari, B.3    Marwarha, G.4    Dickson, A.5    Kirsch, W.M.6
  • 110
    • 84864749266 scopus 로고    scopus 로고
    • The incidence and prevalence of Huntington's disease: a systematic review and meta-analysis
    • doi: 10.1002/mds.25075
    • Pringsheim, T., Wiltshire, K., Day, L., Dykeman, J., Steeves, T., and Jette, N. (2012). The incidence and prevalence of Huntington's disease: a systematic review and meta-analysis. Mov. Disord. 27, 1083-1091. doi: 10.1002/mds.25075
    • (2012) Mov. Disord. , vol.27 , pp. 1083-1091
    • Pringsheim, T.1    Wiltshire, K.2    Day, L.3    Dykeman, J.4    Steeves, T.5    Jette, N.6
  • 111
    • 0032506187 scopus 로고    scopus 로고
    • Prions
    • doi: 10.1073/pnas.95.23.13363
    • Prusiner, S. B. (1998). Prions. Proc. Natl. Acad. Sci. U.S.A. 95, 13363-13383. doi: 10.1073/pnas.95.23.13363
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 13363-13383
    • Prusiner, S.B.1
  • 112
    • 0041819578 scopus 로고    scopus 로고
    • Association of HFE mutations with neurodegeneration and oxidative stress in Alzheimer's disease and correlation with APOE
    • doi: 10.1002/ajmg.b.10069.
    • Pulliam, J. F., Jennings, C. D., Kryscio, R. J., Davis, D. G., Wilson, D., Montine, T. J., et al. (2003). Association of HFE mutations with neurodegeneration and oxidative stress in Alzheimer's disease and correlation with APOE. Am. J. Med. Genet. B Neuropsychiatr. Genet. 119B, 48-53. doi: 10.1002/ajmg.b.10069
    • (2003) Am. J. Med. Genet. B Neuropsychiatr. Genet. , vol.119 B , pp. 48-53
    • Pulliam, J.F.1    Jennings, C.D.2    Kryscio, R.J.3    Davis, D.G.4    Wilson, D.5    Montine, T.J.6
  • 113
    • 29844456397 scopus 로고    scopus 로고
    • Study of the localization of iron, ferritin, and hemosiderin in Alzheimer's disease hippocampus by analytical microscopy at the subcellular level
    • doi: 10.1016/j.jsb.2005.11.001
    • Quintana, C., Bellefqih, S., Laval, J. Y., Guerquin-Kern, J. L., Wu, T. D., Avila, J., et al. (2006). Study of the localization of iron, ferritin, and hemosiderin in Alzheimer's disease hippocampus by analytical microscopy at the subcellular level. J. Struct. Biol. 153, 42-54. doi: 10.1016/j.jsb.2005.11.001
    • (2006) J. Struct. Biol. , vol.153 , pp. 42-54
    • Quintana, C.1    Bellefqih, S.2    Laval, J.Y.3    Guerquin-Kern, J.L.4    Wu, T.D.5    Avila, J.6
  • 114
    • 1842608741 scopus 로고    scopus 로고
    • Novel chelators for central nervous system disorders that involve alterations in the metabolism of iron and other metal ions
    • doi: 10.1196/annals.1306.026
    • Richardson, D. R. (2004). Novel chelators for central nervous system disorders that involve alterations in the metabolism of iron and other metal ions. Ann. N. Y. Acad. Sci. 1012, 326-341. doi: 10.1196/annals.1306.026
    • (2004) Ann. N. Y. Acad. Sci. , vol.1012 , pp. 326-341
    • Richardson, D.R.1
  • 115
    • 64049096553 scopus 로고    scopus 로고
    • Fenton chemistry and oxidative stress mediate the toxicity of the beta-amyloid peptide in a Drosophila model of Alzheimer's disease
    • doi: 10.1111/j.1460-9568.2009.06701.x
    • Rival, T., Page, R. M., Chandraratna, D. S., Sendall, T. J., Ryder, E., Liu, B., et al. (2009). Fenton chemistry and oxidative stress mediate the toxicity of the beta-amyloid peptide in a Drosophila model of Alzheimer's disease. Eur. J. Neurosci. 29, 1335-1347. doi: 10.1111/j.1460-9568.2009.06701.x
    • (2009) Eur. J. Neurosci. , vol.29 , pp. 1335-1347
    • Rival, T.1    Page, R.M.2    Chandraratna, D.S.3    Sendall, T.J.4    Ryder, E.5    Liu, B.6
  • 116
    • 84655164280 scopus 로고    scopus 로고
    • The role of metallobiology and amyloid-beta peptides in Alzheimer's disease
    • doi: 10.1111/j.1471-4159.2011.07500.x
    • Roberts, B. R., Ryan, T. M., Bush, A. I., Masters, C. L., and Duce, J. A. (2012). The role of metallobiology and amyloid-beta peptides in Alzheimer's disease. J. Neurochem. 120(Suppl. 1), 149-166. doi: 10.1111/j.1471-4159.2011.07500.x
    • (2012) J. Neurochem. , vol.120 , Issue.SUPPL. 1 , pp. 149-166
    • Roberts, B.R.1    Ryan, T.M.2    Bush, A.I.3    Masters, C.L.4    Duce, J.A.5
  • 117
    • 1942469548 scopus 로고    scopus 로고
    • Synergy between the C2 allele of transferrin and the C282Y allele of the haemochromatosis gene (HFE) as risk factors for developing Alzheimer's disease
    • doi: 10.1136/jmg.2003.015552
    • Robson, K. J., Lehmann, D. J., Wimhurst, V. L., Livesey, K. J., Combrinck, M., Merryweather-Clarke, A. T., et al. (2004). Synergy between the C2 allele of transferrin and the C282Y allele of the haemochromatosis gene (HFE) as risk factors for developing Alzheimer's disease. J. Med. Genet. 41, 261-265. doi: 10.1136/jmg.2003.015552
    • (2004) J. Med. Genet. , vol.41 , pp. 261-265
    • Robson, K.J.1    Lehmann, D.J.2    Wimhurst, V.L.3    Livesey, K.J.4    Combrinck, M.5    Merryweather-Clarke, A.T.6
  • 118
    • 0347928847 scopus 로고    scopus 로고
    • An iron-responsive element type II in the 5'-untranslated region of the Alzheimer's amyloid precursor protein transcript
    • doi: 10.1074/jbc. M207435200
    • Rogers, J. T., Randall, J. D., Cahill, C. M., Eder, P. S., Huang, X., Gunshin, H., et al. (2002). An iron-responsive element type II in the 5'-untranslated region of the Alzheimer's amyloid precursor protein transcript. J. Biol. Chem. 277, 45518-45528. doi: 10.1074/jbc. M207435200
    • (2002) J. Biol. Chem. , vol.277 , pp. 45518-45528
    • Rogers, J.T.1    Randall, J.D.2    Cahill, C.M.3    Eder, P.S.4    Huang, X.5    Gunshin, H.6
  • 119
    • 84863806222 scopus 로고    scopus 로고
    • Alterations in brain transition metals in Huntington disease: an evolving and intricate story
    • doi: 10.1001/archneurol.2011.2945
    • Rosas, H. D., Chen, Y. I., Doros, G., Salat, D. H., Chen, N. K., Kwong, K. K., et al. (2012). Alterations in brain transition metals in Huntington disease: an evolving and intricate story. Arch. Neurol. 69, 887-893. doi: 10.1001/archneurol.2011.2945
    • (2012) Arch. Neurol. , vol.69 , pp. 887-893
    • Rosas, H.D.1    Chen, Y.I.2    Doros, G.3    Salat, D.H.4    Chen, N.K.5    Kwong, K.K.6
  • 120
    • 84880805523 scopus 로고    scopus 로고
    • Iron metabolism in the CNS: implications for neurodegenerative diseases
    • doi: 10.1038/nrn3453
    • Rouault, T. A. (2013). Iron metabolism in the CNS: implications for neurodegenerative diseases. Nat. Rev. Neurosci. 14, 551-564. doi: 10.1038/nrn3453
    • (2013) Nat. Rev. Neurosci. , vol.14 , pp. 551-564
    • Rouault, T.A.1
  • 121
    • 17144378216 scopus 로고    scopus 로고
    • Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis
    • doi: 10.1038/nrm1620
    • Rouault, T. A., and Tong, W. H. (2005). Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis. Nat. Rev. Mol. Cell Biol. 6, 345-351. doi: 10.1038/nrm1620
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 345-351
    • Rouault, T.A.1    Tong, W.H.2
  • 122
    • 57449092273 scopus 로고    scopus 로고
    • Divalent metal transporter 1 (DMT1) contributes to neurodegeneration in animal models of Parkinson's disease
    • doi: 10.1073/pnas.0804373105
    • Salazar, J., Mena, N., Hunot, S., Prigent, A., Alvarez-Fischer, D., Arredondo, M., et al. (2008). Divalent metal transporter 1 (DMT1) contributes to neurodegeneration in animal models of Parkinson's disease. Proc. Natl. Acad. Sci. U.S.A. 105, 18578-18583. doi: 10.1073/pnas.0804373105
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 18578-18583
    • Salazar, J.1    Mena, N.2    Hunot, S.3    Prigent, A.4    Alvarez-Fischer, D.5    Arredondo, M.6
  • 123
    • 0034964682 scopus 로고    scopus 로고
    • The hemochromatosis gene affects the age of onset of sporadic Alzheimer's disease
    • doi: 10.1016/S0197-4580(01)00219-6
    • Sampietro, M., Caputo, L., Casatta, A., Meregalli, M., Pellagatti, A., Tagliabue, J., et al. (2001). The hemochromatosis gene affects the age of onset of sporadic Alzheimer's disease. Neurobiol. Aging 22, 563-568. doi: 10.1016/S0197-4580(01)00219-6
    • (2001) Neurobiol. Aging , vol.22 , pp. 563-568
    • Sampietro, M.1    Caputo, L.2    Casatta, A.3    Meregalli, M.4    Pellagatti, A.5    Tagliabue, J.6
  • 124
    • 70349669073 scopus 로고    scopus 로고
    • Evolutionary descent of prion genes from the ZIP family of metal ion transporters
    • doi: 10.1371/journal.pone.0007208
    • Schmitt-Ulms, G., Ehsani, S., Watts, J. C., Westaway, D., and Wille, H. (2009). Evolutionary descent of prion genes from the ZIP family of metal ion transporters. PLoS ONE 4:e7208. doi: 10.1371/journal.pone.0007208
    • (2009) PLoS ONE , vol.4
    • Schmitt-Ulms, G.1    Ehsani, S.2    Watts, J.C.3    Westaway, D.4    Wille, H.5
  • 125
    • 80052923220 scopus 로고    scopus 로고
    • Iron efflux from oligodendrocytes is differentially regulated in gray and white matter
    • doi: 10.1523/JNEUROSCI.2838-11.2011
    • Schulz, K., Vulpe, C. D., Harris, L. Z., and David, S. (2011). Iron efflux from oligodendrocytes is differentially regulated in gray and white matter. J. Neurosci. 31, 13301-13311. doi: 10.1523/JNEUROSCI.2838-11.2011
    • (2011) J. Neurosci. , vol.31 , pp. 13301-13311
    • Schulz, K.1    Vulpe, C.D.2    Harris, L.Z.3    David, S.4
  • 126
    • 79952400329 scopus 로고    scopus 로고
    • Decreased CSF transferrin in sCJD: a potential pre-mortem diagnostic test for prion disorders
    • doi: 10.1371/journal.pone.0016804
    • Singh, A., Beveridge, A. J., and Singh, N. (2011). Decreased CSF transferrin in sCJD: a potential pre-mortem diagnostic test for prion disorders. PLoS ONE 6:e16804. doi: 10.1371/journal.pone.0016804
    • (2011) PLoS ONE , vol.6
    • Singh, A.1    Beveridge, A.J.2    Singh, N.3
  • 127
    • 84880237675 scopus 로고    scopus 로고
    • Prion protein regulates iron transport by functioning as a ferrireductase
    • doi: 10.3233/JAD-130218
    • Singh, A., Haldar, S., Horback, K., Tom, C., Zhou, L., Meyerson, H., et al. (2013). Prion protein regulates iron transport by functioning as a ferrireductase. J. Alzheimers Dis. 35, 541-552. doi: 10.3233/JAD-130218
    • (2013) J. Alzheimers Dis. , vol.35 , pp. 541-552
    • Singh, A.1    Haldar, S.2    Horback, K.3    Tom, C.4    Zhou, L.5    Meyerson, H.6
  • 128
    • 63449135100 scopus 로고    scopus 로고
    • Abnormal brain iron homeostasis in human and animal prion disorders
    • doi: 10.1371/journal.ppat.1000336
    • Singh, A., Isaac, A. O., Luo, X., Mohan, M. L., Cohen, M. L., Chen, F., et al. (2009a). Abnormal brain iron homeostasis in human and animal prion disorders. PLoS Pathog. 5:e1000336. doi: 10.1371/journal.ppat.1000336
    • (2009) PLoS Pathog. , vol.5
    • Singh, A.1    Isaac, A.O.2    Luo, X.3    Mohan, M.L.4    Cohen, M.L.5    Chen, F.6
  • 129
    • 67749133712 scopus 로고    scopus 로고
    • Prion protein (PrP) knock-out mice show altered iron metabolism: a functional role for PrP in iron uptake and transport
    • doi: 10.1371/journal.pone.0006115
    • Singh, A., Kong, Q., Luo, X., Petersen, R. B., Meyerson, H., and Singh, N. (2009b). Prion protein (PrP) knock-out mice show altered iron metabolism: a functional role for PrP in iron uptake and transport. PLoS ONE 4:e6115. doi: 10.1371/journal.pone.0006115
    • (2009) PLoS ONE , vol.4
    • Singh, A.1    Kong, Q.2    Luo, X.3    Petersen, R.B.4    Meyerson, H.5    Singh, N.6
  • 130
    • 84887212524 scopus 로고    scopus 로고
    • Prion protein modulates cellular iron uptake: a novel function with implications for prion disease pathogenesis
    • doi: 10.1371/journal.pone.0004468
    • Singh, A., Mohan, M. L., Isaac, A. O., Luo, X., Petrak, J., Vyoral, D., et al. (2009c). Prion protein modulates cellular iron uptake: a novel function with implications for prion disease pathogenesis. PLoS ONE 4:e4468. doi: 10.1371/journal.pone.0004468
    • (2009) PLoS ONE , vol.4
    • Singh, A.1    Mohan, M.L.2    Isaac, A.O.3    Luo, X.4    Petrak, J.5    Vyoral, D.6
  • 131
    • 84856574059 scopus 로고    scopus 로고
    • Change in the characteristics of ferritin induces iron imbalance in prion disease affected brains
    • doi: 10.1016/j.nbd.2011.12.012
    • Singh, A., Qing, L., Kong, Q., and Singh, N. (2012). Change in the characteristics of ferritin induces iron imbalance in prion disease affected brains. Neurobiol. Dis. 45, 930-938. doi: 10.1016/j.nbd.2011.12.012
    • (2012) Neurobiol. Dis. , vol.45 , pp. 930-938
    • Singh, A.1    Qing, L.2    Kong, Q.3    Singh, N.4
  • 132
    • 0242300619 scopus 로고    scopus 로고
    • alpha-Synuclein locus triplication causes Parkinson's disease
    • doi: 10.1126/science.1090278
    • Singleton, A. B., Farrer, M., Johnson, J., Singleton, A., Hague, S., Kachergus, J., et al. (2003). alpha-Synuclein locus triplication causes Parkinson's disease. Science 302:841. doi: 10.1126/science.1090278
    • (2003) Science , vol.302 , pp. 841
    • Singleton, A.B.1    Farrer, M.2    Johnson, J.3    Singleton, A.4    Hague, S.5    Kachergus, J.6
  • 133
    • 67349112729 scopus 로고    scopus 로고
    • Iron, the substantia nigra and related neurological disorders
    • doi: 10.1016/j.bbagen.2008.08.005
    • Snyder, A. M., and Connor, J. R. (2009). Iron, the substantia nigra and related neurological disorders. Biochim. Biophys. Acta 1790, 606-614. doi: 10.1016/j.bbagen.2008.08.005
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 606-614
    • Snyder, A.M.1    Connor, J.R.2
  • 134
    • 72649090521 scopus 로고    scopus 로고
    • Ferroportin 1 but not hephaestin contributes to iron accumulation in a cell model of Parkinson's disease
    • doi: 10.1016/j.freeradbiomed.2009.11.004
    • Song, N., Wang, J., Jiang, H., and Xie, J. (2010). Ferroportin 1 but not hephaestin contributes to iron accumulation in a cell model of Parkinson's disease. Free Radic. Biol. Med. 48, 332-341. doi: 10.1016/j.freeradbiomed.2009.11.004
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 332-341
    • Song, N.1    Wang, J.2    Jiang, H.3    Xie, J.4
  • 136
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's disease Collaborative Research Group.
    • The Huntington's disease Collaborative Research Group. (1993). A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 72, 971-983.
    • (1993) Cell , vol.72 , pp. 971-983
  • 137
    • 84880823246 scopus 로고    scopus 로고
    • Heme binding induces dimerization and nitration of truncated beta-amyloid peptide Abeta16 under oxidative stress
    • doi: 10.1002/anie.201302989
    • Thiabaud, G., Pizzocaro, S., Garcia-Serres, R., Latour, J. M., Monzani, E., and Casella, L. (2013). Heme binding induces dimerization and nitration of truncated beta-amyloid peptide Abeta16 under oxidative stress. Angew Chem. Int. Ed. Engl. 52, 8041-8044. doi: 10.1002/anie.201302989
    • (2013) Angew Chem. Int. Ed. Engl. , vol.52 , pp. 8041-8044
    • Thiabaud, G.1    Pizzocaro, S.2    Garcia-Serres, R.3    Latour, J.M.4    Monzani, E.5    Casella, L.6
  • 138
    • 78649519833 scopus 로고    scopus 로고
    • Case-control studies on ceruloplasmin and superoxide dismutase (SOD1) in neurodegenerative diseases: a short review
    • doi: 10.1016/j.jns.2010.08.047
    • Torsdottir, G., Kristinsson, J., Snaedal, J., Sveinbjornsdottir, S., Gudmundsson, G., Hreidarsson, S., et al. (2010). Case-control studies on ceruloplasmin and superoxide dismutase (SOD1) in neurodegenerative diseases: a short review. J. Neurol. Sci. 299, 51-54. doi: 10.1016/j.jns.2010.08.047
    • (2010) J. Neurol. Sci. , vol.299 , pp. 51-54
    • Torsdottir, G.1    Kristinsson, J.2    Snaedal, J.3    Sveinbjornsdottir, S.4    Gudmundsson, G.5    Hreidarsson, S.6
  • 139
    • 4444316194 scopus 로고    scopus 로고
    • Mutant huntingtin impairs axonal trafficking in mammalian neurons in vivo and in vitro
    • doi: 10.1128/MCB.24.18.8195-8209.2004
    • Trushina, E., Dyer, R. B., Badger, J. D. II, Ure, D., Eide, L., Tran, D. D., et al. (2004). Mutant huntingtin impairs axonal trafficking in mammalian neurons in vivo and in vitro. Mol. Cell. Biol. 24, 8195-8209. doi: 10.1128/MCB.24.18.8195-8209.2004
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8195-8209
    • Trushina, E.1    Dyer, R.B.2    Badger II, J.D.3    Ure, D.4    Eide, L.5    Tran, D.D.6
  • 140
    • 84874575900 scopus 로고    scopus 로고
    • Is R2* a new MRI biomarker for the progression of Parkinson's disease? A longitudinal follow-up
    • doi: 10.1371/journal.pone.0057904
    • Ulla, M., Bonny, J. M., Ouchchane, L., Rieu, I., Claise, B., and Durif, F. (2013). Is R2* a new MRI biomarker for the progression of Parkinson's disease? A longitudinal follow-up. PLoS ONE 8:e57904. doi: 10.1371/journal.pone.0057904
    • (2013) PLoS ONE , vol.8
    • Ulla, M.1    Bonny, J.M.2    Ouchchane, L.3    Rieu, I.4    Claise, B.5    Durif, F.6
  • 141
    • 68949170348 scopus 로고    scopus 로고
    • Metalloproteins and metal sensing
    • doi: 10.1038/nature08300
    • Waldron, K. J., Rutherford, J. C., Ford, D., and Robinson, N. J. (2009). Metalloproteins and metal sensing. Nature 460, 823-830. doi: 10.1038/nature08300
    • (2009) Nature , vol.460 , pp. 823-830
    • Waldron, K.J.1    Rutherford, J.C.2    Ford, D.3    Robinson, N.J.4
  • 142
    • 78650685650 scopus 로고    scopus 로고
    • beta-Amyloid peptide increases levels of iron content and oxidative stress in human cell and Caenorhabditis elegans models of Alzheimer disease
    • doi: 10.1016/j.freeradbiomed.2010.10.707
    • Wan, L., Nie, G., Zhang, J., Luo, Y., Zhang, P., Zhang, Z., et al. (2011). beta-Amyloid peptide increases levels of iron content and oxidative stress in human cell and Caenorhabditis elegans models of Alzheimer disease. Free Radic. Biol. Med. 50, 122-129. doi: 10.1016/j.freeradbiomed.2010.10.707
    • (2011) Free Radic. Biol. Med. , vol.50 , pp. 122-129
    • Wan, L.1    Nie, G.2    Zhang, J.3    Luo, Y.4    Zhang, P.5    Zhang, Z.6
  • 143
    • 84862845774 scopus 로고    scopus 로고
    • Overexpression of human wild-type amyloid-beta protein precursor decreases the iron content and increases the oxidative stress of neuroblastoma SH-SY5Y cells
    • doi: 10.3233/JAD-2012-111169
    • Wan, L., Nie, G., Zhang, J., and Zhao, B. (2012). Overexpression of human wild-type amyloid-beta protein precursor decreases the iron content and increases the oxidative stress of neuroblastoma SH-SY5Y cells. J. Alzheimers Dis. 30, 523-530. doi: 10.3233/JAD-2012-111169
    • (2012) J. Alzheimers Dis. , vol.30 , pp. 523-530
    • Wan, L.1    Nie, G.2    Zhang, J.3    Zhao, B.4
  • 144
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with bacterially expressed recombinant prion protein
    • doi: 10.1126/science.1183748
    • Wang, F., Wang, X., Yuan, C. G., and Ma, J. (2010). Generating a prion with bacterially expressed recombinant prion protein. Science 327, 1132-1135. doi: 10.1126/science.1183748
    • (2010) Science , vol.327 , pp. 1132-1135
    • Wang, F.1    Wang, X.2    Yuan, C.G.3    Ma, J.4
  • 145
    • 79952162002 scopus 로고    scopus 로고
    • Regulation of cellular iron metabolism
    • doi: 10.1042/BJ20101825
    • Wang, J., and Pantopoulos, K. (2011). Regulation of cellular iron metabolism. Biochem. J. 434, 365-381. doi: 10.1042/BJ20101825
    • (2011) Biochem. J. , vol.434 , pp. 365-381
    • Wang, J.1    Pantopoulos, K.2
  • 146
    • 84861899196 scopus 로고    scopus 로고
    • Chelating agents for neurodegenerative diseases
    • doi: 10.2174/092986712800609689
    • Ward, R. J., Dexter, D. T., and Crichton, R. R. (2012). Chelating agents for neurodegenerative diseases. Curr. Med. Chem. 19, 2760-2772. doi: 10.2174/092986712800609689
    • (2012) Curr. Med. Chem. , vol.19 , pp. 2760-2772
    • Ward, R.J.1    Dexter, D.T.2    Crichton, R.R.3
  • 148
    • 84884901205 scopus 로고    scopus 로고
    • Targeting dysregulation of brain iron homeostasis in Parkinson's disease by iron chelators
    • doi: 10.1016/j.freeradbiomed.2013.01.017
    • Weinreb, O., Mandel, S., Youdim, M. B., and Amit, T. (2013). Targeting dysregulation of brain iron homeostasis in Parkinson's disease by iron chelators. Free Radic. Biol. Med. 62, 52-64. doi: 10.1016/j.freeradbiomed.2013.01.017
    • (2013) Free Radic. Biol. Med. , vol.62 , pp. 52-64
    • Weinreb, O.1    Mandel, S.2    Youdim, M.B.3    Amit, T.4
  • 150
    • 0036724204 scopus 로고    scopus 로고
    • Iron (III) induces aggregation of hyperphosphorylated tau and its reduction to iron (II) reverses the aggregation: implications in the formation of neurofibrillary tangles of Alzheimer's disease
    • doi: 10.1046/j.1471-4159.2002.t01-1-01061.x
    • Yamamoto, A., Shin, R. W., Hasegawa, K., Naiki, H., Sato, H., Yoshimasu, F., et al. (2002). Iron (III) induces aggregation of hyperphosphorylated tau and its reduction to iron (II) reverses the aggregation: implications in the formation of neurofibrillary tangles of Alzheimer's disease. J. Neurochem. 82, 1137-1147. doi: 10.1046/j.1471-4159.2002.t01-1-01061.x
    • (2002) J. Neurochem. , vol.82 , pp. 1137-1147
    • Yamamoto, A.1    Shin, R.W.2    Hasegawa, K.3    Naiki, H.4    Sato, H.5    Yoshimasu, F.6
  • 151
    • 84874098495 scopus 로고    scopus 로고
    • Abeta interacts with both the iron center and the porphyrin ring of heme: mechanism of heme's action on Abeta aggregation and disaggregation
    • doi: 10.1021/tx300441e
    • Yuan, C., and Gao, Z. (2013). Abeta interacts with both the iron center and the porphyrin ring of heme: mechanism of heme's action on Abeta aggregation and disaggregation. Chem. Res. Toxicol. 26, 262-269. doi: 10.1021/tx300441e
    • (2013) Chem. Res. Toxicol. , vol.26 , pp. 262-269
    • Yuan, C.1    Gao, Z.2
  • 152
    • 10744230149 scopus 로고    scopus 로고
    • The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia
    • doi: 10.1002/ana.10795
    • Zarranz, J. J., Alegre, J., Gomez-Esteban, J. C., Lezcano, E., Ros, R., Ampuero, I., et al. (2004). The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia. Ann. Neurol. 55, 164-173. doi: 10.1002/ana.10795
    • (2004) Ann. Neurol. , vol.55 , pp. 164-173
    • Zarranz, J.J.1    Alegre, J.2    Gomez-Esteban, J.C.3    Lezcano, E.4    Ros, R.5    Ampuero, I.6
  • 153
    • 0035103932 scopus 로고    scopus 로고
    • Iron, neuromelanin and ferritin content in the substantia nigra of normal subjects at different ages: consequences for iron storage and neurodegenerative processes
    • doi: 10.1046/j.1471-4159.2001.00186.x
    • Zecca, L., Gallorini, M., Schunemann, V., Trautwein, A. X., Gerlach, M., Riederer, P., et al. (2001). Iron, neuromelanin and ferritin content in the substantia nigra of normal subjects at different ages: consequences for iron storage and neurodegenerative processes. J. Neurochem. 76, 1766-1773. doi: 10.1046/j.1471-4159.2001.00186.x
    • (2001) J. Neurochem. , vol.76 , pp. 1766-1773
    • Zecca, L.1    Gallorini, M.2    Schunemann, V.3    Trautwein, A.X.4    Gerlach, M.5    Riederer, P.6
  • 155
    • 0242285663 scopus 로고    scopus 로고
    • Neuromelanin of the substantia nigra: a neuronal black hole with protective and toxic characteristics
    • doi: 10.1016/j.tins.2003.08.009
    • Zecca, L., Zucca, F. A., Wilms, H., and Sulzer, D. (2003). Neuromelanin of the substantia nigra: a neuronal black hole with protective and toxic characteristics. Trends Neurosci. 26, 578-580. doi: 10.1016/j.tins.2003.08.009
    • (2003) Trends Neurosci. , vol.26 , pp. 578-580
    • Zecca, L.1    Zucca, F.A.2    Wilms, H.3    Sulzer, D.4
  • 156
    • 84881235827 scopus 로고    scopus 로고
    • Heme prevents amyloid beta peptide aggregation through hydrophobic interaction based on molecular dynamics simulation
    • doi: 10.1039/c3cp52354c
    • Zhao, L. N., Mu, Y., and Chew, L. Y. (2013). Heme prevents amyloid beta peptide aggregation through hydrophobic interaction based on molecular dynamics simulation. Phys. Chem. Chem. Phys. 15, 14098-14106. doi: 10.1039/c3cp52354c
    • (2013) Phys. Chem. Chem. Phys. , vol.15 , pp. 14098-14106
    • Zhao, L.N.1    Mu, Y.2    Chew, L.Y.3
  • 157
    • 84856489978 scopus 로고    scopus 로고
    • Regulation of brain iron and copper homeostasis by brain barrier systems: implication in neurodegenerative diseases
    • doi: 10.1016/j.pharmthera.2011.10.006
    • Zheng, W., and Monnot, A. D. (2012). Regulation of brain iron and copper homeostasis by brain barrier systems: implication in neurodegenerative diseases. Pharmacol. Ther. 133, 177-188. doi: 10.1016/j.pharmthera.2011.10.006
    • (2012) Pharmacol. Ther. , vol.133 , pp. 177-188
    • Zheng, W.1    Monnot, A.D.2
  • 158
    • 35348982797 scopus 로고    scopus 로고
    • Copper (II) modulates in vitro aggregation of a tau peptide
    • doi: 10.1016/j.peptides.2007.08.022
    • Zhou, L. X., Du, J. T., Zeng, Z. Y., Wu, W. H., Zhao, Y. F., Kanazawa, K., et al. (2007). Copper (II) modulates in vitro aggregation of a tau peptide. Peptides 28, 2229-2234. doi: 10.1016/j.peptides.2007.08.022
    • (2007) Peptides , vol.28 , pp. 2229-2234
    • Zhou, L.X.1    Du, J.T.2    Zeng, Z.Y.3    Wu, W.H.4    Zhao, Y.F.5    Kanazawa, K.6
  • 159
    • 84862882932 scopus 로고    scopus 로고
    • Design of iron chelators with therapeutic application
    • doi: 10.1039/c2dt12159j
    • Zhou, T., Ma, Y., Kong, X., and Hider, R. C. (2012). Design of iron chelators with therapeutic application. Dalton Trans. 41, 6371-6389. doi: 10.1039/c2dt12159j
    • (2012) Dalton Trans. , vol.41 , pp. 6371-6389
    • Zhou, T.1    Ma, Y.2    Kong, X.3    Hider, R.C.4
  • 160
    • 84862319391 scopus 로고    scopus 로고
    • Therapeutic advances in neurodegeneration with brain iron accumulation
    • doi: 10.1016/j.spen.2012.03.007
    • Zorzi, G., Zibordi, F., Chiapparini, L., and Nardocci, N. (2012). Therapeutic advances in neurodegeneration with brain iron accumulation. Semin. Pediatr. Neurol. 19, 82-86. doi: 10.1016/j.spen.2012.03.007
    • (2012) Semin. Pediatr. Neurol. , vol.19 , pp. 82-86
    • Zorzi, G.1    Zibordi, F.2    Chiapparini, L.3    Nardocci, N.4


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