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Volumn 123, Issue 4, 2016, Pages 389-399

Role of iron in neurodegenerative diseases

Author keywords

Iron; Neurodegeneration; Oxidative stress; Parkinson s disease

Indexed keywords

IRON;

EID: 84955261902     PISSN: 03009564     EISSN: 14351463     Source Type: Journal    
DOI: 10.1007/s00702-016-1508-7     Document Type: Review
Times cited : (101)

References (144)
  • 3
    • 84878398613 scopus 로고    scopus 로고
    • Ceruloplasmin dysfunction and therapeutic potential for Parkinson disease
    • COI: 1:CAS:528:DC%2BC3sXosFKitL8%3D, PID: 23424051
    • Ayton S, Lei P, Duce JA, Wong BX, Sedjahtera A, Adlard PA, Bush AI, Finkelstein DI (2013) Ceruloplasmin dysfunction and therapeutic potential for Parkinson disease. Ann Neurol 73(4):554–559. doi:10.1002/ana.23817
    • (2013) Ann Neurol , vol.73 , Issue.4 , pp. 554-559
    • Ayton, S.1    Lei, P.2    Duce, J.A.3    Wong, B.X.4    Sedjahtera, A.5    Adlard, P.A.6    Bush, A.I.7    Finkelstein, D.I.8
  • 4
    • 0030846021 scopus 로고    scopus 로고
    • Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog of frataxin
    • COI: 1:CAS:528:DyaK2sXjvV2mtLs%3D, PID: 9180083
    • Babcock M, de Silva D, Oaks R, Davis-Kaplan S, Jiralerspong S, Montermini L, Pandolfo M, Kaplan J (1997) Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog of frataxin. Science 276(5319):1709–1712
    • (1997) Science , vol.276 , Issue.5319 , pp. 1709-1712
    • Babcock, M.1    de Silva, D.2    Oaks, R.3    Davis-Kaplan, S.4    Jiralerspong, S.5    Montermini, L.6    Pandolfo, M.7    Kaplan, J.8
  • 5
    • 84923593287 scopus 로고    scopus 로고
    • Neuroprotective and neurorestorative activities of a novel iron chelator-brain selective monoamine oxidase-A/monoamine oxidase-B inhibitor in animal models of Parkinson’s disease and aging
    • COI: 1:CAS:528:DC%2BC2cXhvFSmsr3N, PID: 25499799
    • Bar-Am O, Amit T, Kupershmidt L, Aluf Y, Mechlovich D, Kabha H, Danovitch L, Zurawski VR, Youdim MB, Weinreb O (2015) Neuroprotective and neurorestorative activities of a novel iron chelator-brain selective monoamine oxidase-A/monoamine oxidase-B inhibitor in animal models of Parkinson’s disease and aging. Neurobiol Aging 36(3):1529–1542. doi:10.1016/j.neurobiolaging.2014.10.026
    • (2015) Neurobiol Aging , vol.36 , Issue.3 , pp. 1529-1542
    • Bar-Am, O.1    Amit, T.2    Kupershmidt, L.3    Aluf, Y.4    Mechlovich, D.5    Kabha, H.6    Danovitch, L.7    Zurawski, V.R.8    Youdim, M.B.9    Weinreb, O.10
  • 6
    • 0032890824 scopus 로고    scopus 로고
    • Increased basal ganglia iron levels in Huntington disease
    • COI: 1:STN:280:DyaK1M3lvVyjtg%3D%3D, PID: 10328252
    • Bartzokis G, Cummings J, Perlman S, Hance DB, Mintz J (1999) Increased basal ganglia iron levels in Huntington disease. Arch Neurol 56(5):569–574
    • (1999) Arch Neurol , vol.56 , Issue.5 , pp. 569-574
    • Bartzokis, G.1    Cummings, J.2    Perlman, S.3    Hance, D.B.4    Mintz, J.5
  • 7
    • 34548790267 scopus 로고    scopus 로고
    • Myelin breakdown and iron changes in Huntington’s disease: pathogenesis and treatment implications
    • COI: 1:CAS:528:DC%2BD2sXhtVGmsL3N, PID: 17484051
    • Bartzokis G, Lu PH, Tishler TA, Fong SM, Oluwadara B, Finn JP, Huang D, Bordelon Y, Mintz J, Perlman S (2007) Myelin breakdown and iron changes in Huntington’s disease: pathogenesis and treatment implications. Neurochem Res 32(10):1655–1664. doi:10.1007/s11064-007-9352-7
    • (2007) Neurochem Res , vol.32 , Issue.10 , pp. 1655-1664
    • Bartzokis, G.1    Lu, P.H.2    Tishler, T.A.3    Fong, S.M.4    Oluwadara, B.5    Finn, J.P.6    Huang, D.7    Bordelon, Y.8    Mintz, J.9    Perlman, S.10
  • 8
    • 84903818809 scopus 로고    scopus 로고
    • Iron overload accelerates neuronal amyloid-beta production and cognitive impairment in transgenic mice model of Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BC2cXoslCms70%3D, PID: 24863668
    • Becerril-Ortega J, Bordji K, Freret T, Rush T, Buisson A (2014) Iron overload accelerates neuronal amyloid-beta production and cognitive impairment in transgenic mice model of Alzheimer’s disease. Neurobiol Aging 35(10):2288–2301. doi:10.1016/j.neurobiolaging.2014.04.019
    • (2014) Neurobiol Aging , vol.35 , Issue.10 , pp. 2288-2301
    • Becerril-Ortega, J.1    Bordji, K.2    Freret, T.3    Rush, T.4    Buisson, A.5
  • 9
    • 0028869760 scopus 로고
    • Degeneration of substantia nigra in chronic Parkinson’s disease visualized by transcranial color-coded real-time sonography
    • COI: 1:STN:280:DyaK2M7isVGguw%3D%3D, PID: 7824114
    • Becker G, Seufert J, Bogdahn U, Reichmann H, Reiners K (1995) Degeneration of substantia nigra in chronic Parkinson’s disease visualized by transcranial color-coded real-time sonography. Neurology 45(1):182–184
    • (1995) Neurology , vol.45 , Issue.1 , pp. 182-184
    • Becker, G.1    Seufert, J.2    Bogdahn, U.3    Reichmann, H.4    Reiners, K.5
  • 10
    • 33846133709 scopus 로고    scopus 로고
    • Substantia nigra echomorphology in the healthy very old: correlation with motor slowing
    • COI: 1:STN:280:DC%2BD2s%2Fis1ajtQ%3D%3D, PID: 17141529
    • Behnke S, Double KL, Duma S, Broe GA, Guenther V, Becker G, Halliday GM (2007) Substantia nigra echomorphology in the healthy very old: correlation with motor slowing. Neuroimage 34(3):1054–1059. doi:10.1016/j.neuroimage.2006.10.010
    • (2007) Neuroimage , vol.34 , Issue.3 , pp. 1054-1059
    • Behnke, S.1    Double, K.L.2    Duma, S.3    Broe, G.A.4    Guenther, V.5    Becker, G.6    Halliday, G.M.7
  • 11
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: nature’s modular, multipurpose structures
    • COI: 1:CAS:528:DyaK2sXltVSntb4%3D, PID: 9235882
    • Beinert H, Holm RH, Munck E (1997) Iron-sulfur clusters: nature’s modular, multipurpose structures. Science 277(5326):653–659
    • (1997) Science , vol.277 , Issue.5326 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Munck, E.3
  • 12
    • 79957616581 scopus 로고    scopus 로고
    • Hyperechogenicity of the substantia nigra: pitfalls in assessment and specificity for Parkinson’s disease
    • COI: 1:CAS:528:DC%2BC3MXjsFyqsbg%3D
    • Berg D (2011) Hyperechogenicity of the substantia nigra: pitfalls in assessment and specificity for Parkinson’s disease. J Neural Trans 118(3):453–461. doi:10.1007/s00702-010-0469-5
    • (2011) J Neural Trans , vol.118 , Issue.3 , pp. 453-461
    • Berg, D.1
  • 13
    • 0034935922 scopus 로고    scopus 로고
    • Echogenicity of the substantia nigra in Parkinson’s disease and its relation to clinical findings
    • COI: 1:STN:280:DC%2BD3MritFWltQ%3D%3D, PID: 11569897
    • Berg D, Siefker C, Becker G (2001) Echogenicity of the substantia nigra in Parkinson’s disease and its relation to clinical findings. J Neurol 248(8):684–689
    • (2001) J Neurol , vol.248 , Issue.8 , pp. 684-689
    • Berg, D.1    Siefker, C.2    Becker, G.3
  • 15
    • 0028873173 scopus 로고
    • Iron levels modulate alpha-secretase cleavage of amyloid precursor protein
    • COI: 1:CAS:528:DyaK2MXislSjtrw%3D, PID: 7798927
    • Bodovitz S, Falduto MT, Frail DE, Klein WL (1995) Iron levels modulate alpha-secretase cleavage of amyloid precursor protein. J Neurochem 64(1):307–315
    • (1995) J Neurochem , vol.64 , Issue.1 , pp. 307-315
    • Bodovitz, S.1    Falduto, M.T.2    Frail, D.E.3    Klein, W.L.4
  • 16
    • 84858285794 scopus 로고    scopus 로고
    • Brain iron deposition fingerprints in Parkinson’s disease and progressive supranuclear palsy
    • PID: 22290788
    • Boelmans K, Holst B, Hackius M, Finsterbusch J, Gerloff C, Fiehler J, Munchau A (2012) Brain iron deposition fingerprints in Parkinson’s disease and progressive supranuclear palsy. Mov Disord 27(3):421–427. doi:10.1002/mds.24926
    • (2012) Mov Disord , vol.27 , Issue.3 , pp. 421-427
    • Boelmans, K.1    Holst, B.2    Hackius, M.3    Finsterbusch, J.4    Gerloff, C.5    Fiehler, J.6    Munchau, A.7
  • 17
    • 34249697099 scopus 로고    scopus 로고
    • Forecasting the global burden of Alzheimer’s disease
    • PID: 19595937
    • Brookmeyer R, Johnson E, Ziegler-Graham K, Arrighi HM (2007) Forecasting the global burden of Alzheimer’s disease. Alzheimers Dement 3(3):186–191. doi:10.1016/j.jalz.2007.04.381
    • (2007) Alzheimers Dement , vol.3 , Issue.3 , pp. 186-191
    • Brookmeyer, R.1    Johnson, E.2    Ziegler-Graham, K.3    Arrighi, H.M.4
  • 18
    • 3042763187 scopus 로고    scopus 로고
    • Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity
    • COI: 1:CAS:528:DC%2BD2cXlsV2gsbs%3D, PID: 15247478
    • Bulteau AL, O’Neill HA, Kennedy MC, Ikeda-Saito M, Isaya G, Szweda LI (2004) Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science 305(5681):242–245. doi:10.1126/science.1098991
    • (2004) Science , vol.305 , Issue.5681 , pp. 242-245
    • Bulteau, A.L.1    O’Neill, H.A.2    Kennedy, M.C.3    Ikeda-Saito, M.4    Isaya, G.5    Szweda, L.I.6
  • 19
    • 84897930584 scopus 로고    scopus 로고
    • Labile iron in cells and body fluids: physiology, pathology, and pharmacology
    • PID: 24659969
    • Cabantchik ZI (2014) Labile iron in cells and body fluids: physiology, pathology, and pharmacology. Front Pharmacol 5:45. doi:10.3389/fphar.2014.00045
    • (2014) Front Pharmacol , vol.5 , pp. 45
    • Cabantchik, Z.I.1
  • 20
    • 79960164018 scopus 로고    scopus 로고
    • Changes in iron-regulatory gene expression occur in human cell culture models of Parkinson’s disease
    • COI: 1:CAS:528:DC%2BC3MXoslWrsr8%3D, PID: 21672570
    • Carroll CB, Zeissler ML, Chadborn N, Gibson K, Williams G, Zajicek JP, Morrison KE, Hanemann CO (2011) Changes in iron-regulatory gene expression occur in human cell culture models of Parkinson’s disease. Neurochem Int 59(1):73–80. doi:10.1016/j.neuint.2011.05.006
    • (2011) Neurochem Int , vol.59 , Issue.1 , pp. 73-80
    • Carroll, C.B.1    Zeissler, M.L.2    Chadborn, N.3    Gibson, K.4    Williams, G.5    Zajicek, J.P.6    Morrison, K.E.7    Hanemann, C.O.8
  • 21
    • 84862817976 scopus 로고    scopus 로고
    • The role of iron as a mediator of oxidative stress in Alzheimer disease
    • COI: 1:CAS:528:DC%2BC38Xlslahurk%3D, PID: 22447715
    • Castellani RJ, Moreira PI, Perry G, Zhu X (2012) The role of iron as a mediator of oxidative stress in Alzheimer disease. BioFactors 38(2):133–138. doi:10.1002/biof.1010
    • (2012) BioFactors , vol.38 , Issue.2 , pp. 133-138
    • Castellani, R.J.1    Moreira, P.I.2    Perry, G.3    Zhu, X.4
  • 22
    • 57249095767 scopus 로고    scopus 로고
    • Lipid peroxidation of membrane phospholipids generates hydroxy-alkenals and oxidized phospholipids active in physiological and/or pathological conditions
    • COI: 1:CAS:528:DC%2BD1cXhsV2gtbzI, PID: 18977338
    • Catala A (2009) Lipid peroxidation of membrane phospholipids generates hydroxy-alkenals and oxidized phospholipids active in physiological and/or pathological conditions. Chem Phys Lipids 157(1):1–11. doi:10.1016/j.chemphyslip.2008.09.004
    • (2009) Chem Phys Lipids , vol.157 , Issue.1 , pp. 1-11
    • Catala, A.1
  • 23
    • 84885404060 scopus 로고    scopus 로고
    • Iron accumulates in Huntington’s disease neurons: protection by deferoxamine
    • COI: 1:CAS:528:DC%2BC3sXhs1Cqu7fK, PID: 24146952
    • Chen J, Marks E, Lai B, Zhang Z, Duce JA, Lam LQ, Volitakis I, Bush AI, Hersch S, Fox JH (2013) Iron accumulates in Huntington’s disease neurons: protection by deferoxamine. PLoS ONE 8(10):e77023. doi:10.1371/journal.pone.0077023
    • (2013) PLoS ONE , vol.8 , Issue.10 , pp. e77023
    • Chen, J.1    Marks, E.2    Lai, B.3    Zhang, Z.4    Duce, J.A.5    Lam, L.Q.6    Volitakis, I.7    Bush, A.I.8    Hersch, S.9    Fox, J.H.10
  • 24
    • 0026513756 scopus 로고
    • A histochemical study of iron, transferrin, and ferritin in Alzheimer’s diseased brains
    • COI: 1:CAS:528:DyaK38Xht1Kitrc%3D, PID: 1613823
    • Connor JR, Menzies SL, St Martin SM, Mufson EJ (1992) A histochemical study of iron, transferrin, and ferritin in Alzheimer’s diseased brains. J Neurosci Res 31(1):75–83. doi:10.1002/jnr.490310111
    • (1992) J Neurosci Res , vol.31 , Issue.1 , pp. 75-83
    • Connor, J.R.1    Menzies, S.L.2    St Martin, S.M.3    Mufson, E.J.4
  • 25
    • 0027327899 scopus 로고
    • Ceruloplasmin levels in the human superior temporal gyrus in aging and Alzheimer’s disease
    • COI: 1:CAS:528:DyaK2cXltFKlug%3D%3D, PID: 8264985
    • Connor JR, Tucker P, Johnson M, Snyder B (1993) Ceruloplasmin levels in the human superior temporal gyrus in aging and Alzheimer’s disease. Neurosci Lett 159(1–2):88–90
    • (1993) Neurosci Lett , vol.159 , Issue.1-2 , pp. 88-90
    • Connor, J.R.1    Tucker, P.2    Johnson, M.3    Snyder, B.4
  • 26
    • 0028350924 scopus 로고
    • Isoforms of ferritin have a specific cellular distribution in the brain
    • COI: 1:CAS:528:DyaK2cXitFegsbY%3D, PID: 8021970
    • Connor JR, Boeshore KL, Benkovic SA, Menzies SL (1994) Isoforms of ferritin have a specific cellular distribution in the brain. J Neurosci Res 37(4):461–465. doi:10.1002/jnr.490370405
    • (1994) J Neurosci Res , vol.37 , Issue.4 , pp. 461-465
    • Connor, J.R.1    Boeshore, K.L.2    Benkovic, S.A.3    Menzies, S.L.4
  • 27
    • 0029092802 scopus 로고
    • A quantitative analysis of isoferritins in select regions of aged, parkinsonian, and Alzheimer’s diseased brains
    • COI: 1:CAS:528:DyaK2MXntFGgsbo%3D, PID: 7616228
    • Connor JR, Snyder BS, Arosio P, Loeffler DA, LeWitt P (1995) A quantitative analysis of isoferritins in select regions of aged, parkinsonian, and Alzheimer’s diseased brains. J Neurochem 65(2):717–724
    • (1995) J Neurochem , vol.65 , Issue.2 , pp. 717-724
    • Connor, J.R.1    Snyder, B.S.2    Arosio, P.3    Loeffler, D.A.4    LeWitt, P.5
  • 30
    • 80051658907 scopus 로고    scopus 로고
    • Brain iron metabolism and its perturbation in neurological diseases
    • COI: 1:CAS:528:DC%2BC3MXjsFyqsbs%3D, PID: 20809066
    • Crichton RR, Dexter DT, Ward RJ (2011) Brain iron metabolism and its perturbation in neurological diseases. J Neural Transm 118(3):301–314. doi:10.1007/s00702-010-0470-z
    • (2011) J Neural Transm , vol.118 , Issue.3 , pp. 301-314
    • Crichton, R.R.1    Dexter, D.T.2    Ward, R.J.3
  • 31
    • 79251572323 scopus 로고    scopus 로고
    • Alpha-synuclein is a cellular ferrireductase
    • COI: 1:CAS:528:DC%2BC3MXhtVSisb4%3D, PID: 21249223
    • Davies P, Moualla D, Brown DR (2011) Alpha-synuclein is a cellular ferrireductase. PLoS ONE 6(1):e15814. doi:10.1371/journal.pone.0015814
    • (2011) PLoS ONE , vol.6 , Issue.1 , pp. e15814
    • Davies, P.1    Moualla, D.2    Brown, D.R.3
  • 32
    • 34250800318 scopus 로고    scopus 로고
    • Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin
    • PID: 17541408
    • De Domenico I, Ward DM, di Patti MC, Jeong SY, David S, Musci G, Kaplan J (2007) Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin. EMBO J 26(12):2823–2831. doi:10.1038/sj.emboj.7601735
    • (2007) EMBO J , vol.26 , Issue.12 , pp. 2823-2831
    • De Domenico, I.1    Ward, D.M.2    di Patti, M.C.3    Jeong, S.Y.4    David, S.5    Musci, G.6    Kaplan, J.7
  • 33
    • 0030297178 scopus 로고    scopus 로고
    • Copper, iron, and zinc imbalances in severely degenerated brain regions in Alzheimer’s disease: possible relation to oxidative stress
    • COI: 1:CAS:528:DyaK2sXisFOrtA%3D%3D, PID: 8981312
    • Deibel MA, Ehmann WD, Markesbery WR (1996) Copper, iron, and zinc imbalances in severely degenerated brain regions in Alzheimer’s disease: possible relation to oxidative stress. J Neurol Sci 143(1–2):137–142
    • (1996) J Neurol Sci , vol.143 , Issue.1-2 , pp. 137-142
    • Deibel, M.A.1    Ehmann, W.D.2    Markesbery, W.R.3
  • 34
    • 44049099669 scopus 로고    scopus 로고
    • Mitochondrial import and accumulation of alpha-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain
    • COI: 1:CAS:528:DC%2BD1cXjslyruro%3D, PID: 18245082
    • Devi L, Raghavendran V, Prabhu BM, Avadhani NG, Anandatheerthavarada HK (2008) Mitochondrial import and accumulation of alpha-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain. J Biol Chem 283(14):9089–9100. doi:10.1074/jbc.M710012200
    • (2008) J Biol Chem , vol.283 , Issue.14 , pp. 9089-9100
    • Devi, L.1    Raghavendran, V.2    Prabhu, B.M.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5
  • 36
    • 0024356620 scopus 로고
    • Increased nigral iron content and alterations in other metal ions occurring in brain in Parkinson’s disease
    • COI: 1:CAS:528:DyaL1MXkslGrs7k%3D, PID: 2723638
    • Dexter DT, Wells FR, Lees AJ, Agid F, Agid Y, Jenner P, Marsden CD (1989) Increased nigral iron content and alterations in other metal ions occurring in brain in Parkinson’s disease. J Neurochem 52(6):1830–1836
    • (1989) J Neurochem , vol.52 , Issue.6 , pp. 1830-1836
    • Dexter, D.T.1    Wells, F.R.2    Lees, A.J.3    Agid, F.4    Agid, Y.5    Jenner, P.6    Marsden, C.D.7
  • 38
    • 79955852987 scopus 로고    scopus 로고
    • Clinically available iron chelators induce neuroprotection in the 6-OHDA model of Parkinson’s disease after peripheral administration
    • COI: 1:CAS:528:DC%2BC3MXivVOhtrw%3D
    • Dexter DT, Statton SA, Whitmore C, Freinbichler W, Weinberger P, Tipton KF, Della Corte L, Ward RJ, Crichton RR (2011) Clinically available iron chelators induce neuroprotection in the 6-OHDA model of Parkinson’s disease after peripheral administration. J Neural Trans 118(2):223–231. doi:10.1007/s00702-010-0531-3
    • (2011) J Neural Trans , vol.118 , Issue.2 , pp. 223-231
    • Dexter, D.T.1    Statton, S.A.2    Whitmore, C.3    Freinbichler, W.4    Weinberger, P.5    Tipton, K.F.6    Della Corte, L.7    Ward, R.J.8    Crichton, R.R.9
  • 39
    • 84961601969 scopus 로고    scopus 로고
    • A pilot 6 months efficacy and safety study utilising the iron chelator deferiprone in early stage Parkinson’s disease [abstract]
    • Dexter DT, Martin-Bastida A, Kabba C, Piccini P, Sharp D, Ward R, Newbold R (2014) A pilot 6 months efficacy and safety study utilising the iron chelator deferiprone in early stage Parkinson’s disease [abstract]. Mov Disord 29(Suppl 1):633
    • (2014) Mov Disord , vol.29 , pp. 633
    • Dexter, D.T.1    Martin-Bastida, A.2    Kabba, C.3    Piccini, P.4    Sharp, D.5    Ward, R.6    Newbold, R.7
  • 44
    • 0036798434 scopus 로고    scopus 로고
    • Lack of up-regulation of ferritin is associated with sustained iron regulatory protein-1 binding activity in the substantia nigra of patients with Parkinson’s disease
    • COI: 1:CAS:528:DC%2BD38XotFyltLc%3D, PID: 12423242
    • Faucheux BA, Martin ME, Beaumont C, Hunot S, Hauw JJ, Agid Y, Hirsch EC (2002) Lack of up-regulation of ferritin is associated with sustained iron regulatory protein-1 binding activity in the substantia nigra of patients with Parkinson’s disease. J Neurochem 83(2):320–330
    • (2002) J Neurochem , vol.83 , Issue.2 , pp. 320-330
    • Faucheux, B.A.1    Martin, M.E.2    Beaumont, C.3    Hunot, S.4    Hauw, J.J.5    Agid, Y.6    Hirsch, E.C.7
  • 45
    • 33751080354 scopus 로고    scopus 로고
    • Huntingtin inclusion bodies are iron-dependent centers of oxidative events
    • COI: 1:CAS:528:DC%2BD2sXjvVCi, PID: 17116244
    • Firdaus WJ, Wyttenbach A, Giuliano P, Kretz-Remy C, Currie RW, Arrigo AP (2006) Huntingtin inclusion bodies are iron-dependent centers of oxidative events. FEBS J 273(23):5428–5441. doi:10.1111/j.1742-4658.2006.05537.x
    • (2006) FEBS J , vol.273 , Issue.23 , 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
  • 46
    • 84875719721 scopus 로고    scopus 로고
    • Genetics and iron in the systems biology of Parkinson’s disease and some related disorders
    • COI: 1:CAS:528:DC%2BC3sXhtlCisr4%3D, PID: 23220386
    • Funke C, Schneider SA, Berg D, Kell DB (2013) Genetics and iron in the systems biology of Parkinson’s disease and some related disorders. Neurochem Int 62(5):637–652. doi:10.1016/j.neuint.2012.11.015
    • (2013) Neurochem Int , vol.62 , Issue.5 , pp. 637-652
    • Funke, C.1    Schneider, S.A.2    Berg, D.3    Kell, D.B.4
  • 47
    • 84865452207 scopus 로고    scopus 로고
    • Ferritin up-regulation and transient ROS production in cultured brain astrocytes after loading with iron oxide nanoparticles
    • COI: 1:CAS:528:DC%2BC38Xht1KkurjK, PID: 22750736
    • Geppert M, Hohnholt MC, Nurnberger S, Dringen R (2012) Ferritin up-regulation and transient ROS production in cultured brain astrocytes after loading with iron oxide nanoparticles. Acta Biomater 8(10):3832–3839. doi:10.1016/j.actbio.2012.06.029
    • (2012) Acta Biomater , vol.8 , Issue.10 , pp. 3832-3839
    • Geppert, M.1    Hohnholt, M.C.2    Nurnberger, S.3    Dringen, R.4
  • 48
    • 80051635783 scopus 로고    scopus 로고
    • Iron-dependent functions of mitochondria—relation to neurodegeneration
    • COI: 1:CAS:528:DC%2BC3MXjsFyqtr0%3D, PID: 21161302
    • Gille G, Reichmann H (2011) Iron-dependent functions of mitochondria—relation to neurodegeneration. J Neural Transm 118(3):349–359. doi:10.1007/s00702-010-0503-7
    • (2011) J Neural Transm , vol.118 , Issue.3 , pp. 349-359
    • Gille, G.1    Reichmann, H.2
  • 49
    • 77953381979 scopus 로고    scopus 로고
    • New developments in depression, anxiety, compulsiveness, and hallucinations in Parkinson’s disease
    • PID: 20187250
    • Goetz CG (2010) New developments in depression, anxiety, compulsiveness, and hallucinations in Parkinson’s disease. Mov Disord 25(Suppl 1):S104–S109. doi:10.1002/mds.22636
    • (2010) Mov Disord , vol.25 , pp. S104-S109
    • Goetz, C.G.1
  • 50
    • 0037013194 scopus 로고    scopus 로고
    • Magnesium inhibits spontaneous and iron-induced aggregation of alpha-synuclein
    • COI: 1:CAS:528:DC%2BD38Xjs1Wjtb4%3D, PID: 11850416
    • Golts N, Snyder H, Frasier M, Theisler C, Choi P, Wolozin B (2002) Magnesium inhibits spontaneous and iron-induced aggregation of alpha-synuclein. J Biol Chem 277(18):16116–16123. doi:10.1074/jbc.M107866200
    • (2002) J Biol Chem , vol.277 , Issue.18 , pp. 16116-16123
    • Golts, N.1    Snyder, H.2    Frasier, M.3    Theisler, C.4    Choi, P.5    Wolozin, B.6
  • 51
    • 0026573467 scopus 로고
    • Selective accumulation of aluminum and iron in the neurofibrillary tangles of Alzheimer’s disease: a laser microprobe (LAMMA) study
    • COI: 1:STN:280:DyaK38zksVentA%3D%3D, PID: 1637136
    • Good PF, Perl DP, Bierer LM, Schmeidler J (1992) Selective accumulation of aluminum and iron in the neurofibrillary tangles of Alzheimer’s disease: a laser microprobe (LAMMA) study. Ann Neurol 31(3):286–292. doi:10.1002/ana.410310310
    • (1992) Ann Neurol , vol.31 , Issue.3 , pp. 286-292
    • Good, P.F.1    Perl, D.P.2    Bierer, L.M.3    Schmeidler, J.4
  • 53
    • 67849106894 scopus 로고    scopus 로고
    • Clioquinol decreases amyloid-beta burden and reduces working memory impairment in a transgenic mouse model of Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BD1MXmvVOhs7w%3D, PID: 19363260
    • Grossi C, Francese S, Casini A, Rosi MC, Luccarini I, Fiorentini A, Gabbiani C, Messori L, Moneti G, Casamenti F (2009) Clioquinol decreases amyloid-beta burden and reduces working memory impairment in a transgenic mouse model of Alzheimer’s disease. J Alzheimers Dis 17(2):423–440. doi:10.3233/JAD-2009-1063
    • (2009) J Alzheimers Dis , vol.17 , Issue.2 , pp. 423-440
    • Grossi, C.1    Francese, S.2    Casini, A.3    Rosi, M.C.4    Luccarini, I.5    Fiorentini, A.6    Gabbiani, C.7    Messori, L.8    Moneti, G.9    Casamenti, F.10
  • 55
    • 84871958441 scopus 로고    scopus 로고
    • Deferoxamine inhibits iron induced hippocampal tau phosphorylation in the Alzheimer transgenic mouse brain
    • COI: 1:CAS:528:DC%2BC3sXitVGiu78%3D, PID: 23262393
    • Guo C, Wang P, Zhong ML, Wang T, Huang XS, Li JY, Wang ZY (2013a) Deferoxamine inhibits iron induced hippocampal tau phosphorylation in the Alzheimer transgenic mouse brain. Neurochem Int 62(2):165–172. doi:10.1016/j.neuint.2012.12.005
    • (2013) Neurochem Int , vol.62 , Issue.2 , pp. 165-172
    • Guo, C.1    Wang, P.2    Zhong, M.L.3    Wang, T.4    Huang, X.S.5    Li, J.Y.6    Wang, Z.Y.7
  • 56
    • 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
    • COI: 1:CAS:528:DC%2BC38XovVansrY%3D, PID: 22717236
    • Guo C, Wang T, Zheng W, Shan ZY, Teng WP, Wang ZY (2013b) Intranasal deferoxamine reverses iron-induced memory deficits and inhibits amyloidogenic APP processing in a transgenic mouse model of Alzheimer’s disease. Neurobiol Aging 34(2):562–575. doi:10.1016/j.neurobiolaging.2012.05.009
    • (2013) Neurobiol Aging , vol.34 , Issue.2 , pp. 562-575
    • Guo, C.1    Wang, T.2    Zheng, W.3    Shan, Z.Y.4    Teng, W.P.5    Wang, Z.Y.6
  • 57
    • 34249051016 scopus 로고    scopus 로고
    • Olfactory loss may be a first sign of idiopathic Parkinson’s disease
    • PID: 17357143
    • Haehner A, Hummel T, Hummel C, Sommer U, Junghanns S, Reichmann H (2007) Olfactory loss may be a first sign of idiopathic Parkinson’s disease. Mov Disord 22(6):839–842. doi:10.1002/mds.21413
    • (2007) Mov Disord , vol.22 , Issue.6 , pp. 839-842
    • Haehner, A.1    Hummel, T.2    Hummel, C.3    Sommer, U.4    Junghanns, S.5    Reichmann, H.6
  • 58
    • 0033525437 scopus 로고    scopus 로고
    • Expression of ferritin protein and subunit mRNAs in normal and iron deficient rat brain
    • COI: 1:CAS:528:DyaK1MXhtFeju78%3D, PID: 10064889
    • Hansen TM, Nielsen H, Bernth N, Moos T (1999) Expression of ferritin protein and subunit mRNAs in normal and iron deficient rat brain. Brain Res Mol Brain Res 65(2):186–197
    • (1999) Brain Res Mol Brain Res , vol.65 , Issue.2 , pp. 186-197
    • Hansen, T.M.1    Nielsen, H.2    Bernth, N.3    Moos, T.4
  • 60
    • 84955726895 scopus 로고    scopus 로고
    • Region-specific disturbed iron distribution in early idiopathic Parkinson’s disease measured by quantitative susceptibility mapping
    • He N, Ling H, Ding B, Huang J, Zhang Y, Zhang Z, Liu C, Chen K, Yan F (2015) Region-specific disturbed iron distribution in early idiopathic Parkinson’s disease measured by quantitative susceptibility mapping. Hum Brain Mapp. doi:10.1002/hbm.22928
    • (2015) Hum Brain Mapp
    • He, N.1    Ling, H.2    Ding, B.3    Huang, J.4    Zhang, Y.5    Zhang, Z.6    Liu, C.7    Chen, K.8    Yan, F.9
  • 61
    • 44549088704 scopus 로고    scopus 로고
    • The biochemistry of heme biosynthesis
    • COI: 1:CAS:528:DC%2BD1cXmvFeks7s%3D, PID: 18314007
    • Heinemann IU, Jahn M, Jahn D (2008) The biochemistry of heme biosynthesis. Arch Biochem Biophys 474(2):238–251. doi:10.1016/j.abb.2008.02.015
    • (2008) Arch Biochem Biophys , vol.474 , Issue.2 , pp. 238-251
    • Heinemann, I.U.1    Jahn, M.2    Jahn, D.3
  • 62
    • 0034703860 scopus 로고    scopus 로고
    • Huntingtin: an iron-regulated protein essential for normal nuclear and perinuclear organelles
    • COI: 1:CAS:528:DC%2BD3cXoslWms7Y%3D, PID: 11092755
    • Hilditch-Maguire P, Trettel F, Passani LA, Auerbach A, Persichetti F, MacDonald ME (2000) Huntingtin: an iron-regulated protein essential for normal nuclear and perinuclear organelles. Hum Mol Genet 9(19):2789–2797
    • (2000) Hum Mol Genet , vol.9 , Issue.19 , pp. 2789-2797
    • Hilditch-Maguire, P.1    Trettel, F.2    Passani, L.A.3    Auerbach, A.4    Persichetti, F.5    MacDonald, M.E.6
  • 63
    • 1442323987 scopus 로고    scopus 로고
    • Iron accumulation, iron-mediated toxicity and altered levels of ferritin and transferrin receptor in cultured astrocytes during incubation with ferric ammonium citrate
    • COI: 1:CAS:528:DC%2BD2cXhvFOru7w%3D, PID: 15009675
    • Hoepken HH, Korten T, Robinson SR, Dringen R (2004) Iron accumulation, iron-mediated toxicity and altered levels of ferritin and transferrin receptor in cultured astrocytes during incubation with ferric ammonium citrate. J Neurochem 88(5):1194–1202
    • (2004) J Neurochem , vol.88 , Issue.5 , pp. 1194-1202
    • Hoepken, H.H.1    Korten, T.2    Robinson, S.R.3    Dringen, R.4
  • 64
    • 0026635461 scopus 로고
    • Oxidative stress as a cause of nigral cell death in Parkinson’s disease and incidental Lewy body disease. The Royal Kings and Queens Parkinson’s Disease Research Group
    • COI: 1:CAS:528:DyaK3sXnvVSntQ%3D%3D, PID: 1510385
    • Jenner P, Dexter DT, Sian J, Schapira AH, Marsden CD (1992) Oxidative stress as a cause of nigral cell death in Parkinson’s disease and incidental Lewy body disease. The Royal Kings and Queens Parkinson’s Disease Research Group. Ann Neurol 32(Suppl):S82–S87
    • (1992) Ann Neurol , vol.32 , pp. S82-S87
    • Jenner, P.1    Dexter, D.T.2    Sian, J.3    Schapira, A.H.4    Marsden, C.D.5
  • 65
    • 77949261597 scopus 로고    scopus 로고
    • Up-regulation of divalent metal transporter 1 in 6-hydroxydopamine intoxication is IRE/IRP dependent
    • COI: 1:CAS:528:DC%2BC3cXisFejtb8%3D, PID: 20125122
    • Jiang H, Song N, Xu H, Zhang S, Wang J, Xie J (2010) Up-regulation of divalent metal transporter 1 in 6-hydroxydopamine intoxication is IRE/IRP dependent. Cell Res 20(3):345–356. doi:10.1038/cr.2010.20
    • (2010) Cell Res , vol.20 , Issue.3 , pp. 345-356
    • Jiang, H.1    Song, N.2    Xu, H.3    Zhang, S.4    Wang, J.5    Xie, J.6
  • 66
    • 78650695967 scopus 로고    scopus 로고
    • Decreased serum ceruloplasmin levels characteristically aggravate nigral iron deposition in Parkinson’s disease
    • PID: 21109502
    • Jin L, Wang J, Zhao L, Jin H, Fei G, Zhang Y, Zeng M, Zhong C (2011) Decreased serum ceruloplasmin levels characteristically aggravate nigral iron deposition in Parkinson’s disease. Brain 134(Pt 1):50–58. doi:10.1093/brain/awq319
    • (2011) Brain , vol.134 , pp. 50-58
    • Jin, L.1    Wang, J.2    Zhao, L.3    Jin, H.4    Fei, G.5    Zhang, Y.6    Zeng, M.7    Zhong, C.8
  • 68
    • 0034648298 scopus 로고    scopus 로고
    • The Haber–Weiss reaction and mechanisms of toxicity
    • COI: 1:CAS:528:DC%2BD3cXlvV2htrs%3D, PID: 10963860
    • Kehrer JP (2000) The Haber–Weiss reaction and mechanisms of toxicity. Toxicology 149(1):43–50
    • (2000) Toxicology , vol.149 , Issue.1 , pp. 43-50
    • Kehrer, J.P.1
  • 69
    • 0030465238 scopus 로고    scopus 로고
    • Superoxide accelerates DNA damage by elevating free-iron levels
    • COI: 1:CAS:528:DyaK28Xnt1Ggu7s%3D, PID: 8942986
    • Keyer K, Imlay JA (1996) Superoxide accelerates DNA damage by elevating free-iron levels. Proc Natl Acad Sci USA 93(24):13635–13640
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.24 , pp. 13635-13640
    • Keyer, K.1    Imlay, J.A.2
  • 70
    • 0027452550 scopus 로고
    • Regulating the fate of mRNA: the control of cellular iron metabolism
    • COI: 1:CAS:528:DyaK3sXht1Wgtbg%3D, PID: 8380757
    • Klausner RD, Rouault TA, Harford JB (1993) Regulating the fate of mRNA: the control of cellular iron metabolism. Cell 72(1):19–28
    • (1993) Cell , vol.72 , Issue.1 , pp. 19-28
    • Klausner, R.D.1    Rouault, T.A.2    Harford, J.B.3
  • 74
    • 79960895695 scopus 로고    scopus 로고
    • Novel molecular targets of the neuroprotective/neurorescue multimodal iron chelating drug M30 in the mouse brain
    • COI: 1:CAS:528:DC%2BC3MXpsFaqu7o%3D, PID: 21570450
    • Kupershmidt L, Weinreb O, Amit T, Mandel S, Bar-Am O, Youdim MB (2011) Novel molecular targets of the neuroprotective/neurorescue multimodal iron chelating drug M30 in the mouse brain. Neuroscience 189:345–358. doi:10.1016/j.neuroscience.2011.03.040
    • (2011) Neuroscience , vol.189 , pp. 345-358
    • Kupershmidt, L.1    Weinreb, O.2    Amit, T.3    Mandel, S.4    Bar-Am, O.5    Youdim, M.B.6
  • 76
    • 84923547839 scopus 로고    scopus 로고
    • Cellular iron uptake, trafficking and metabolism: key molecules and mechanisms and their roles in disease
    • COI: 1:CAS:528:DC%2BC2MXitl2qtLg%3D, PID: 25661197
    • Lane DJ, Merlot AM, Huang ML, Bae DH, Jansson PJ, Sahni S, Kalinowski DS, Richardson DR (2015) Cellular iron uptake, trafficking and metabolism: key molecules and mechanisms and their roles in disease. Biochim Biophys Acta 1853(5):1130–1144. doi:10.1016/j.bbamcr.2015.01.021
    • (2015) Biochim Biophys Acta , vol.1853 , Issue.5 , pp. 1130-1144
    • Lane, D.J.1    Merlot, A.M.2    Huang, M.L.3    Bae, D.H.4    Jansson, P.J.5    Sahni, S.6    Kalinowski, D.S.7    Richardson, D.R.8
  • 77
    • 84911093882 scopus 로고    scopus 로고
    • 7 Tesla magnetic resonance imaging: a closer look at substantia nigra anatomy in Parkinson’s disease
    • COI: 1:CAS:528:DC%2BC2cXhvVKmsLbL, PID: 25308960
    • Lehericy S, Bardinet E, Poupon C, Vidailhet M, Francois C (2014) 7 Tesla magnetic resonance imaging: a closer look at substantia nigra anatomy in Parkinson’s disease. Mov Disord 29(13):1574–1581. doi:10.1002/mds.26043
    • (2014) Mov Disord , vol.29 , Issue.13 , pp. 1574-1581
    • Lehericy, S.1    Bardinet, E.2    Poupon, C.3    Vidailhet, M.4    Francois, C.5
  • 79
    • 84857373169 scopus 로고    scopus 로고
    • Functional roles of transferrin in the brain
    • COI: 1:CAS:528:DC%2BC38Xit12itr4%3D, PID: 22138408
    • Leitner DF, Connor JR (2012) Functional roles of transferrin in the brain. Biochim Biophys Acta 1820(3):393–402. doi:10.1016/j.bbagen.2011.10.016
    • (2012) Biochim Biophys Acta , vol.1820 , Issue.3 , pp. 393-402
    • Leitner, D.F.1    Connor, J.R.2
  • 80
    • 84937514651 scopus 로고    scopus 로고
    • Transcranial sonography of the substantia nigra and its correlation with DAT-SPECT in the diagnosis of Parkinson’s disease
    • PID: 26066091
    • Li DH, Zhang LY, Hu YY, Jiang XF, Zhou HY, Yang Q, Kang WY, Liu J, Chen SD (2015) Transcranial sonography of the substantia nigra and its correlation with DAT-SPECT in the diagnosis of Parkinson’s disease. Parkinsonism Relat Disord 21(8):923–928. doi:10.1016/j.parkreldis.2015.05.024
    • (2015) Parkinsonism Relat Disord , vol.21 , Issue.8 , pp. 923-928
    • Li, D.H.1    Zhang, L.Y.2    Hu, Y.Y.3    Jiang, X.F.4    Zhou, H.Y.5    Yang, Q.6    Kang, W.Y.7    Liu, J.8    Chen, S.D.9
  • 82
    • 0020443202 scopus 로고
    • Synthesis of the proteins of complex III of the mitochondrial respiratory chain in heme-deficient cells
    • COI: 1:CAS:528:DyaL3sXhsVWrtg%3D%3D, PID: 6295756
    • Lin CI, Gollub EG, Beattie DS (1982) Synthesis of the proteins of complex III of the mitochondrial respiratory chain in heme-deficient cells. Eur J Biochem 128(2–3):309–313
    • (1982) Eur J Biochem , vol.128 , Issue.2-3 , pp. 309-313
    • Lin, C.I.1    Gollub, E.G.2    Beattie, D.S.3
  • 83
    • 84892475141 scopus 로고    scopus 로고
    • Susceptibility-weighted imaging changes suggesting brain iron accumulation in Huntington’s disease: an epiphenomenon which causes diagnostic difficulty
    • COI: 1:STN:280:DC%2BC2cvosVWhsw%3D%3D, PID: 24571106
    • Macerollo A, Perry R, Stamelou M, Batla A, Mazumder AA, Adams ME, Bhatia KP (2014) Susceptibility-weighted imaging changes suggesting brain iron accumulation in Huntington’s disease: an epiphenomenon which causes diagnostic difficulty. Eur J Neurol 21(2):e16–e17. doi:10.1111/ene.12298
    • (2014) Eur J Neurol , vol.21 , Issue.2 , pp. e16-e17
    • Macerollo, A.1    Perry, R.2    Stamelou, M.3    Batla, A.4    Mazumder, A.A.5    Adams, M.E.6    Bhatia, K.P.7
  • 84
    • 77953518555 scopus 로고    scopus 로고
    • Alzheimer’s disease: clinical trials and drug development
    • COI: 1:CAS:528:DC%2BC3cXpsFajur8%3D, PID: 20610346
    • Mangialasche F, Solomon A, Winblad B, Mecocci P, Kivipelto M (2010) Alzheimer’s disease: clinical trials and drug development. Lancet Neurol 9(7):702–716. doi:10.1016/S1474-4422(10)70119-8
    • (2010) Lancet Neurol , vol.9 , Issue.7 , pp. 702-716
    • Mangialasche, F.1    Solomon, A.2    Winblad, B.3    Mecocci, P.4    Kivipelto, M.5
  • 85
    • 84904734583 scopus 로고    scopus 로고
    • Dysregulation of cellular iron metabolism in Friedreich ataxia: from primary iron-sulfur cluster deficit to mitochondrial iron accumulation
    • PID: 24917819
    • Martelli A, Puccio H (2014) Dysregulation of cellular iron metabolism in Friedreich ataxia: from primary iron-sulfur cluster deficit to mitochondrial iron accumulation. Front Pharmacol 5:130. doi:10.3389/fphar.2014.00130
    • (2014) Front Pharmacol , vol.5 , pp. 130
    • Martelli, A.1    Puccio, H.2
  • 86
    • 42049123661 scopus 로고    scopus 로고
    • Midbrain iron content in early Parkinson disease: a potential biomarker of disease status
    • COI: 1:CAS:528:DC%2BD1cXksFantr8%3D, PID: 18172063
    • Martin WR, Wieler M, Gee M (2008) Midbrain iron content in early Parkinson disease: a potential biomarker of disease status. Neurology 70(16 Pt 2):1411–1417. doi:10.1212/01.wnl.0000286384.31050.b5
    • (2008) Neurology , vol.70 , pp. 1411-1417
    • Martin, W.R.1    Wieler, M.2    Gee, M.3
  • 87
    • 67349106731 scopus 로고    scopus 로고
    • A novel transferrin/TfR2-mediated mitochondrial iron transport system is disrupted in Parkinson's disease
    • COI: 1:CAS:528:DC%2BD1MXmtVeks7w%3D, PID: 19250966
    • Mastroberardino PG, Hoffman EK, Horowitz MP, Betarbet R, Taylor G, Cheng D,Anderson M (2009) A novel transferrin/TfR2-mediated mitochondrial iron transport system is disrupted in Parkinson's disease. Neurobiol dis 34(3):417–431
    • (2009) Neurobiol dis , vol.34 , Issue.3 , pp. 417-431
    • Mastroberardino, P.G.1    Hoffman, E.K.2    Horowitz, M.P.3    Betarbet, R.4    Taylor, G.5    Cheng, D.6    Anderson, M.7
  • 88
    • 84923070858 scopus 로고    scopus 로고
    • Mitochondrial iron homeostasis and its dysfunctions in neurodegenerative disorders
    • COI: 1:CAS:528:DC%2BC2MXis1aqt7Y%3D, PID: 25667951
    • Mena NP, Urrutia PJ, Lourido F, Carrasco CM, Nunez MT (2015) Mitochondrial iron homeostasis and its dysfunctions in neurodegenerative disorders. Mitochondrion 21:92–105. doi:10.1016/j.mito.2015.02.001
    • (2015) Mitochondrion , vol.21 , pp. 92-105
    • Mena, N.P.1    Urrutia, P.J.2    Lourido, F.3    Carrasco, C.M.4    Nunez, M.T.5
  • 89
    • 34147107527 scopus 로고    scopus 로고
    • Assessment of brain iron and neuronal integrity in patients with Parkinson’s disease using novel MRI contrasts
    • PID: 17149719
    • Michaeli S, Oz G, Sorce DJ, Garwood M, Ugurbil K, Majestic S, Tuite P (2007) Assessment of brain iron and neuronal integrity in patients with Parkinson’s disease using novel MRI contrasts. Mov Disord 22(3):334–340. doi:10.1002/mds.21227
    • (2007) Mov Disord , vol.22 , Issue.3 , pp. 334-340
    • Michaeli, S.1    Oz, G.2    Sorce, D.J.3    Garwood, M.4    Ugurbil, K.5    Majestic, S.6    Tuite, P.7
  • 90
    • 84881543414 scopus 로고    scopus 로고
    • Neuroimaging of rapid eye movement sleep behavior disorder: transcranial ultrasound, single-photon emission computed tomography, and positron emission tomography scan data
    • PID: 23648146
    • Miyamoto M, Miyamoto T (2013) Neuroimaging of rapid eye movement sleep behavior disorder: transcranial ultrasound, single-photon emission computed tomography, and positron emission tomography scan data. Sleep Med 14(8):739–743. doi:10.1016/j.sleep.2013.03.004
    • (2013) Sleep Med , vol.14 , Issue.8 , pp. 739-743
    • Miyamoto, M.1    Miyamoto, T.2
  • 91
    • 0029976834 scopus 로고    scopus 로고
    • Immunohistochemical localization of intraneuronal transferrin receptor immunoreactivity in the adult mouse central nervous system
    • COI: 1:CAS:528:DyaK28XntFCitLg%3D, PID: 8930792
    • Moos T (1996) Immunohistochemical localization of intraneuronal transferrin receptor immunoreactivity in the adult mouse central nervous system. J Comp Neurol 375(4):675–692. doi:10.1002/(SICI)1096-9861(19961125)375:4<675:AID-CNE8>3.0.CO;2-Z
    • (1996) J Comp Neurol , vol.375 , Issue.4 , pp. 675-692
    • Moos, T.1
  • 92
    • 0347993815 scopus 로고    scopus 로고
    • The significance of the mutated divalent metal transporter (DMT1) on iron transport into the Belgrade rat brain
    • COI: 1:CAS:528:DC%2BD2cXktV2isw%3D%3D, PID: 14675167
    • Moos T, Morgan EH (2004) The significance of the mutated divalent metal transporter (DMT1) on iron transport into the Belgrade rat brain. J Neurochem 88(1):233–245
    • (2004) J Neurochem , vol.88 , Issue.1 , pp. 233-245
    • Moos, T.1    Morgan, E.H.2
  • 93
    • 33750738079 scopus 로고    scopus 로고
    • Ferroportin in the postnatal rat brain: implications for axonal transport and neuronal export of iron
    • PID: 17101453
    • Moos T, Rosengren Nielsen T (2006) Ferroportin in the postnatal rat brain: implications for axonal transport and neuronal export of iron. Semin Pediatr Neurol 13(3):149–157. doi:10.1016/j.spen.2006.08.003
    • (2006) Semin Pediatr Neurol , vol.13 , Issue.3 , pp. 149-157
    • Moos, T.1    Rosengren Nielsen, T.2
  • 94
    • 0032585035 scopus 로고    scopus 로고
    • Expression of the neuronal transferrin receptor is age dependent and susceptible to iron deficiency
    • COI: 1:CAS:528:DyaK1cXltVSisr4%3D, PID: 9714152
    • Moos T, Oates PS, Morgan EH (1998) Expression of the neuronal transferrin receptor is age dependent and susceptible to iron deficiency. J Comp Neurol 398(3):420–430
    • (1998) J Comp Neurol , vol.398 , Issue.3 , pp. 420-430
    • Moos, T.1    Oates, P.S.2    Morgan, E.H.3
  • 95
    • 33748090285 scopus 로고    scopus 로고
    • Brain capillary endothelial cells mediate iron transport into the brain by segregating iron from transferrin without the involvement of divalent metal transporter 1
    • COI: 1:CAS:528:DC%2BD28XhtVCksb%2FN, PID: 16879716
    • Moos T, Skjoerringe T, Gosk S, Morgan EH (2006) Brain capillary endothelial cells mediate iron transport into the brain by segregating iron from transferrin without the involvement of divalent metal transporter 1. J Neurochem 98(6):1946–1958. doi:10.1111/j.1471-4159.2006.04023.x
    • (2006) J Neurochem , vol.98 , Issue.6 , pp. 1946-1958
    • Moos, T.1    Skjoerringe, T.2    Gosk, S.3    Morgan, E.H.4
  • 96
    • 84904684637 scopus 로고    scopus 로고
    • Iron dysregulation in Huntington’s disease
    • COI: 1:CAS:528:DC%2BC2cXhtFOlsb7I, PID: 24717009
    • Muller M, Leavitt BR (2014) Iron dysregulation in Huntington’s disease. J Neurochem 130(3):328–350. doi:10.1111/jnc.12739
    • (2014) J Neurochem , vol.130 , Issue.3 , pp. 328-350
    • Muller, M.1    Leavitt, B.R.2
  • 97
    • 0034468706 scopus 로고    scopus 로고
    • Crosslinking of alpha-synuclein by advanced glycation endproducts—an early pathophysiological step in Lewy body formation?
    • COI: 1:CAS:528:DC%2BD3MXht1Oqtrc%3D, PID: 11207423
    • Munch G, Luth HJ, Wong A, Arendt T, Hirsch E, Ravid R, Riederer P (2000) Crosslinking of alpha-synuclein by advanced glycation endproducts—an early pathophysiological step in Lewy body formation? J Chem Neuroanat 20(3–4):253–257
    • (2000) J Chem Neuroanat , vol.20 , Issue.3-4 , pp. 253-257
    • Munch, G.1    Luth, H.J.2    Wong, A.3    Arendt, T.4    Hirsch, E.5    Ravid, R.6    Riederer, P.7
  • 100
    • 0034663039 scopus 로고    scopus 로고
    • The A53T alpha-synuclein mutation increases iron-dependent aggregation and toxicity
    • COI: 1:CAS:528:DC%2BD3cXlvVGjs7k%3D, PID: 10934254
    • Ostrerova-Golts N, Petrucelli L, Hardy J, Lee JM, Farer M, Wolozin B (2000) The A53T alpha-synuclein mutation increases iron-dependent aggregation and toxicity. J Neurosci 20(16):6048–6054
    • (2000) J Neurosci , vol.20 , Issue.16 , pp. 6048-6054
    • Ostrerova-Golts, N.1    Petrucelli, L.2    Hardy, J.3    Lee, J.M.4    Farer, M.5    Wolozin, B.6
  • 102
    • 0028236018 scopus 로고
    • Electron transport chain defects in Alzheimer’s disease brain
    • PID: 8208407
    • Parker WD Jr, Parks J, Filley CM, Kleinschmidt-DeMasters BK (1994) Electron transport chain defects in Alzheimer’s disease brain. Neurology 44(6):1090–1096
    • (1994) Neurology , vol.44 , Issue.6 , pp. 1090-1096
    • Parker, W.D.1    Parks, J.2    Filley, C.M.3    Kleinschmidt-DeMasters, B.K.4
  • 103
    • 84877340972 scopus 로고    scopus 로고
    • Iron uptake in quiescent and inflammation-activated astrocytes: a potentially neuroprotective control of iron burden
    • COI: 1:CAS:528:DC%2BC3sXptV2nsbo%3D, PID: 23583428
    • Pelizzoni I, Zacchetti D, Campanella A, Grohovaz F, Codazzi F (2013) Iron uptake in quiescent and inflammation-activated astrocytes: a potentially neuroprotective control of iron burden. Biochim Biophys Acta 1832(8):1326–1333. doi:10.1016/j.bbadis.2013.04.007
    • (2013) Biochim Biophys Acta , vol.1832 , Issue.8 , pp. 1326-1333
    • Pelizzoni, I.1    Zacchetti, D.2    Campanella, A.3    Grohovaz, F.4    Codazzi, F.5
  • 105
    • 85005921759 scopus 로고    scopus 로고
    • The systemic iron-regulatory proteins hepcidin and ferroportin are reduced in the brain in Alzheimer’s disease
    • PID: 24252754
    • Raha AA, Vaishnav RA, Friedland RP, Bomford A, Raha-Chowdhury R (2013) The systemic iron-regulatory proteins hepcidin and ferroportin are reduced in the brain in Alzheimer’s disease. Acta Neuropathol Commun 1:55. doi:10.1186/2051-5960-1-55
    • (2013) Acta Neuropathol Commun , vol.1 , pp. 55
    • Raha, A.A.1    Vaishnav, R.A.2    Friedland, R.P.3    Bomford, A.4    Raha-Chowdhury, R.5
  • 106
    • 84858078783 scopus 로고    scopus 로고
    • Iron homeostasis in astrocytes and microglia is differentially regulated by TNF-alpha and TGF-beta1
    • PID: 22298416
    • Rathore KI, Redensek A, David S (2012) Iron homeostasis in astrocytes and microglia is differentially regulated by TNF-alpha and TGF-beta1. Glia 60(5):738–750. doi:10.1002/glia.22303
    • (2012) Glia , vol.60 , Issue.5 , pp. 738-750
    • Rathore, K.I.1    Redensek, A.2    David, S.3
  • 107
    • 0024557734 scopus 로고
    • Transition metals, ferritin, glutathione, and ascorbic acid in parkinsonian brains
    • COI: 1:CAS:528:DyaL1MXhtFals78%3D, PID: 2911028
    • Riederer P, Sofic E, Rausch WD, Schmidt B, Reynolds GP, Jellinger K, Youdim MB (1989) Transition metals, ferritin, glutathione, and ascorbic acid in parkinsonian brains. J Neurochem 52(2):515–520
    • (1989) J Neurochem , vol.52 , Issue.2 , pp. 515-520
    • Riederer, P.1    Sofic, E.2    Rausch, W.D.3    Schmidt, B.4    Reynolds, G.P.5    Jellinger, K.6    Youdim, M.B.7
  • 109
    • 84879250235 scopus 로고    scopus 로고
    • Clinical MRI for iron detection in Parkinson’s disease
    • PID: 23522789
    • Rossi M, Ruottinen H, Soimakallio S, Elovaara I, Dastidar P (2013) Clinical MRI for iron detection in Parkinson’s disease. Clin Imaging 37(4):631–636. doi:10.1016/j.clinimag.2013.02.001
    • (2013) Clin Imaging , vol.37 , Issue.4 , pp. 631-636
    • Rossi, M.1    Ruottinen, H.2    Soimakallio, S.3    Elovaara, I.4    Dastidar, P.5
  • 110
    • 0031253821 scopus 로고    scopus 로고
    • Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia
    • COI: 1:CAS:528:DyaK2sXmsFantLk%3D, PID: 9326946
    • Rotig A, de Lonlay P, Chretien D, Foury F, Koenig M, Sidi D, Munnich A, Rustin P (1997) Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia. Nat Genet 17(2):215–217. doi:10.1038/ng1097-215
    • (1997) Nat Genet , vol.17 , Issue.2 , pp. 215-217
    • Rotig, A.1    de Lonlay, P.2    Chretien, D.3    Foury, F.4    Koenig, M.5    Sidi, D.6    Munnich, A.7    Rustin, P.8
  • 111
    • 33746361251 scopus 로고    scopus 로고
    • The role of iron regulatory proteins in mammalian iron homeostasis and disease
    • COI: 1:CAS:528:DC%2BD28XmvFyqsrg%3D, PID: 16850017
    • Rouault TA (2006) The role of iron regulatory proteins in mammalian iron homeostasis and disease. Nat Chem Biol 2(8):406–414. doi:10.1038/nchembio807
    • (2006) Nat Chem Biol , vol.2 , Issue.8 , pp. 406-414
    • Rouault, T.A.1
  • 115
    • 84916606763 scopus 로고    scopus 로고
    • The role of iron in gray matter degeneration in Huntington’s disease: a magnetic resonance imaging study
    • PID: 25145324
    • Sanchez-Castaneda C, Squitieri F, Di Paola M, Dayan M, Petrollini M, Sabatini U (2015) The role of iron in gray matter degeneration in Huntington’s disease: a magnetic resonance imaging study. Hum Brain Mapp 36(1):50–66. doi:10.1002/hbm.22612
    • (2015) Hum Brain Mapp , vol.36 , Issue.1 , pp. 50-66
    • Sanchez-Castaneda, C.1    Squitieri, F.2    Di Paola, M.3    Dayan, M.4    Petrollini, M.5    Sabatini, U.6
  • 116
    • 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
    • COI: 1:CAS:528:DC%2BD3cXlt12k, PID: 10617129
    • Sayre LM, Perry G, Harris PL, Liu Y, Schubert KA, Smith MA (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(1):270–279
    • (2000) J Neurochem , vol.74 , Issue.1 , 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
  • 117
    • 0346849912 scopus 로고    scopus 로고
    • Neuroprotection by a novel brain permeable iron chelator, VK-28, against 6-hydroxydopamine lession in rats
    • PID: 14680763
    • Shachar DB, Kahana N, Kampel V, Warshawsky A, Youdim MB (2004) Neuroprotection by a novel brain permeable iron chelator, VK-28, against 6-hydroxydopamine lession in rats. Neuropharmacology 46(2):254–263
    • (2004) Neuropharmacology , vol.46 , Issue.2 , pp. 254-263
    • Shachar, D.B.1    Kahana, N.2    Kampel, V.3    Warshawsky, A.4    Youdim, M.B.5
  • 118
    • 65849373277 scopus 로고    scopus 로고
    • Oxidative stress induces degradation of mitochondrial DNA
    • COI: 1:CAS:528:DC%2BD1MXlslertbs%3D, PID: 19264794
    • Shokolenko I, Venediktova N, Bochkareva A, Wilson GL, Alexeyev MF (2009) Oxidative stress induces degradation of mitochondrial DNA. Nucleic Acids Res 37(8):2539–2548. doi:10.1093/nar/gkp100
    • (2009) Nucleic Acids Res , vol.37 , Issue.8 , pp. 2539-2548
    • Shokolenko, I.1    Venediktova, N.2    Bochkareva, A.3    Wilson, G.L.4    Alexeyev, M.F.5
  • 119
    • 54049133647 scopus 로고    scopus 로고
    • A potential pathogenetic role of iron in Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BD1cXhsVarsbbE, PID: 18466351
    • Silvestri L, Camaschella C (2008) A potential pathogenetic role of iron in Alzheimer’s disease. J Cell Mol Med 12(5A):1548–1550. doi:10.1111/j.1582-4934.2008.00356.x
    • (2008) J Cell Mol Med , vol.12 , Issue.5A , pp. 1548-1550
    • Silvestri, L.1    Camaschella, C.2
  • 120
    • 38349194098 scopus 로고    scopus 로고
    • Furin-mediated release of soluble hemojuvelin: a new link between hypoxia and iron homeostasis
    • COI: 1:CAS:528:DC%2BD1cXns1Ckug%3D%3D, PID: 17938254
    • Silvestri L, Pagani A, Camaschella C (2008) Furin-mediated release of soluble hemojuvelin: a new link between hypoxia and iron homeostasis. Blood 111(2):924–931. doi:10.1182/blood-2007-07-100677
    • (2008) Blood , vol.111 , Issue.2 , pp. 924-931
    • Silvestri, L.1    Pagani, A.2    Camaschella, C.3
  • 121
    • 84935859016 scopus 로고    scopus 로고
    • Divalent metal transporter 1 (DMT1) in the brain: implications for a role in iron transport at the blood-brain barrier, and neuronal and glial pathology
    • PID: 26106291
    • Skjorringe T, Burkhart A, Johnsen KB, Moos T (2015) Divalent metal transporter 1 (DMT1) in the brain: implications for a role in iron transport at the blood-brain barrier, and neuronal and glial pathology. Front Mol Neurosci 8:19. doi:10.3389/fnmol.2015.00019
    • (2015) Front Mol Neurosci , vol.8 , pp. 19
    • Skjorringe, T.1    Burkhart, A.2    Johnsen, K.B.3    Moos, T.4
  • 122
    • 0031981072 scopus 로고    scopus 로고
    • Amyloid-beta deposition in Alzheimer transgenic mice is associated with oxidative stress
    • COI: 1:CAS:528:DyaK1cXislWgs70%3D, PID: 9572310
    • Smith MA, Hirai K, Hsiao K, Pappolla MA, Harris PL, Siedlak SL, Tabaton M, Perry G (1998) Amyloid-beta deposition in Alzheimer transgenic mice is associated with oxidative stress. J Neurochem 70(5):2212–2215
    • (1998) J Neurochem , vol.70 , Issue.5 , pp. 2212-2215
    • Smith, M.A.1    Hirai, K.2    Hsiao, K.3    Pappolla, M.A.4    Harris, P.L.5    Siedlak, S.L.6    Tabaton, M.7    Perry, G.8
  • 123
    • 72649090521 scopus 로고    scopus 로고
    • Ferroportin 1 but not hephaestin contributes to iron accumulation in a cell model of Parkinson’s disease
    • COI: 1:CAS:528:DC%2BC3cXps1Cg, PID: 19913091
    • Song N, Wang J, Jiang H, 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(2):332–341. doi:10.1016/j.freeradbiomed.2009.11.004
    • (2010) Free Radic Biol Med , vol.48 , Issue.2 , pp. 332-341
    • Song, N.1    Wang, J.2    Jiang, H.3    Xie, J.4
  • 124
    • 33750710080 scopus 로고    scopus 로고
    • Protein oxidation and aging
    • COI: 1:CAS:528:DC%2BD28XhtlGqs7jF, PID: 17090414
    • Stadtman ER (2006) Protein oxidation and aging. Free Radic Res 40(12):1250–1258. doi:10.1080/10715760600918142
    • (2006) Free Radic Res , vol.40 , Issue.12 , pp. 1250-1258
    • Stadtman, E.R.1
  • 125
    • 56749156761 scopus 로고    scopus 로고
    • Tim-2 is the receptor for H-ferritin on oligodendrocytes
    • COI: 1:CAS:528:DC%2BD1MXis1Sksw%3D%3D, PID: 19014383
    • Todorich B, Zhang X, Slagle-Webb B, Seaman WE, Connor JR (2008) Tim-2 is the receptor for H-ferritin on oligodendrocytes. J Neurochem 107(6):1495–1505. doi:10.1111/j.1471-4159.2008.05678.x
    • (2008) J Neurochem , vol.107 , Issue.6 , pp. 1495-1505
    • Todorich, B.1    Zhang, X.2    Slagle-Webb, B.3    Seaman, W.E.4    Connor, J.R.5
  • 126
    • 34249075719 scopus 로고    scopus 로고
    • Transcranial color-coded sonography helps differentiation between idiopathic Parkinson’s disease and vascular parkinsonism
    • PID: 17401518
    • Tsai CF, Wu RM, Huang YW, Chen LL, Yip PK, Jeng JS (2007) Transcranial color-coded sonography helps differentiation between idiopathic Parkinson’s disease and vascular parkinsonism. J Neurol 254(4):501–507. doi:10.1007/s00415-006-0403-9
    • (2007) J Neurol , vol.254 , Issue.4 , pp. 501-507
    • Tsai, C.F.1    Wu, R.M.2    Huang, Y.W.3    Chen, L.L.4    Yip, P.K.5    Jeng, J.S.6
  • 127
    • 84897952229 scopus 로고    scopus 로고
    • The interplay between iron accumulation, mitochondrial dysfunction, and inflammation during the execution step of neurodegenerative disorders
    • PID: 24653700
    • Urrutia PJ, Mena NP, Nunez MT (2014) The interplay between iron accumulation, mitochondrial dysfunction, and inflammation during the execution step of neurodegenerative disorders. Front Pharmacol 5:38. doi:10.3389/fphar.2014.00038
    • (2014) Front Pharmacol , vol.5 , pp. 38
    • Urrutia, P.J.1    Mena, N.P.2    Nunez, M.T.3
  • 129
    • 3042836954 scopus 로고    scopus 로고
    • Characterization and modulation of the transferrin receptor on brain capillary endothelial cells
    • COI: 1:CAS:528:DC%2BD2cXjs1Kisrs%3D, PID: 15180331
    • Visser CC, Voorwinden LH, Crommelin DJ, Danhof M, de Boer AG (2004) Characterization and modulation of the transferrin receptor on brain capillary endothelial cells. Pharm Res 21(5):761–769
    • (2004) Pharm Res , vol.21 , Issue.5 , pp. 761-769
    • Visser, C.C.1    Voorwinden, L.H.2    Crommelin, D.J.3    Danhof, M.4    de Boer, A.G.5
  • 130
    • 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
    • COI: 1:CAS:528:DC%2BC3MXht1Kltw%3D%3D, PID: 21034809
    • Wan L, Nie G, Zhang J, Luo Y, Zhang P, Zhang Z, Zhao B (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(1):122–129. doi:10.1016/j.freeradbiomed.2010.10.707
    • (2011) Free Radic Biol Med , vol.50 , Issue.1 , pp. 122-129
    • Wan, L.1    Nie, G.2    Zhang, J.3    Luo, Y.4    Zhang, P.5    Zhang, Z.6    Zhao, B.7
  • 131
    • 58049218922 scopus 로고    scopus 로고
    • Amyloid-beta overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins
    • COI: 1:CAS:528:DC%2BD1cXhsFamu73E, PID: 19050078
    • Wang X, Su B, Siedlak SL, Moreira PI, Fujioka H, Wang Y, Casadesus G, Zhu X (2008) Amyloid-beta overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins. Proc Natl Acad Sci USA 105(49):19318–19323. doi:10.1073/pnas.0804871105
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.49 , pp. 19318-19323
    • Wang, X.1    Su, B.2    Siedlak, S.L.3    Moreira, P.I.4    Fujioka, H.5    Wang, Y.6    Casadesus, G.7    Zhu, X.8
  • 132
    • 84907999177 scopus 로고    scopus 로고
    • The role of iron in brain ageing and neurodegenerative disorders
    • COI: 1:CAS:528:DC%2BC2cXhsFyrt7zN, PID: 25231526
    • Ward RJ, Zucca FA, Duyn JH, Crichton RR, Zecca L (2014) The role of iron in brain ageing and neurodegenerative disorders. Lancet Neurol 13(10):1045–1060. doi:10.1016/S1474-4422(14)70117-6
    • (2014) Lancet Neurol , vol.13 , Issue.10 , pp. 1045-1060
    • Ward, R.J.1    Zucca, F.A.2    Duyn, J.H.3    Crichton, R.R.4    Zecca, L.5
  • 133
    • 0030008268 scopus 로고    scopus 로고
    • Fenton chemistry: an introduction
    • COI: 1:CAS:528:DyaK28XislCmu7c%3D, PID: 8619017
    • Wardman P, Candeias LP (1996) Fenton chemistry: an introduction. Radiat Res 145(5):523–531
    • (1996) Radiat Res , vol.145 , Issue.5 , pp. 523-531
    • Wardman, P.1    Candeias, L.P.2
  • 134
    • 84923261559 scopus 로고    scopus 로고
    • Longitudinal midbrain changes in early Parkinson’s disease: iron content estimated from R2*/MRI
    • PID: 25534153
    • Wieler M, Gee M, Martin WR (2015) Longitudinal midbrain changes in early Parkinson’s disease: iron content estimated from R2*/MRI. Parkinsonism Relat Disord 21(3):179–183. doi:10.1016/j.parkreldis.2014.11.017
    • (2015) Parkinsonism Relat Disord , vol.21 , Issue.3 , pp. 179-183
    • Wieler, M.1    Gee, M.2    Martin, W.R.3
  • 135
    • 84901058201 scopus 로고    scopus 로고
    • The iron regulatory capability of the major protein participants in prevalent neurodegenerative disorders
    • PID: 24795635
    • Wong BX, Duce JA (2014) The iron regulatory capability of the major protein participants in prevalent neurodegenerative disorders. Front Pharmacol 5:81. doi:10.3389/fphar.2014.00081
    • (2014) Front Pharmacol , vol.5 , pp. 81
    • Wong, B.X.1    Duce, J.A.2
  • 136
    • 0036724204 scopus 로고    scopus 로고
    • Iron(III) induces aggregation of hyperphosphorylated τ and its reduction to iron(II) reverses the aggregation: implications in the formation of neurofibrillary tangles of Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BD38XmvVertLk%3D, PID: 12358761
    • Yamamoto A, Shin RW, Hasegawa K, Naiki H, Sato H, Yoshimasu F, Kitamoto T (2002) Iron(III) induces aggregation of hyperphosphorylated τ and its reduction to iron(II) reverses the aggregation: implications in the formation of neurofibrillary tangles of Alzheimer’s disease. J Neurochem 82(5):1137–1147
    • (2002) J Neurochem , vol.82 , Issue.5 , pp. 1137-1147
    • Yamamoto, A.1    Shin, R.W.2    Hasegawa, K.3    Naiki, H.4    Sato, H.5    Yoshimasu, F.6    Kitamoto, T.7
  • 137
    • 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
    • COI: 1:CAS:528:DC%2BD3MXitlSkt74%3D, PID: 11259494
    • Zecca L, Gallorini M, Schunemann V, Trautwein AX, Gerlach M, Riederer P, Vezzoni P, Tampellini D (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(6):1766–1773
    • (2001) J Neurochem , vol.76 , Issue.6 , pp. 1766-1773
    • Zecca, L.1    Gallorini, M.2    Schunemann, V.3    Trautwein, A.X.4    Gerlach, M.5    Riederer, P.6    Vezzoni, P.7    Tampellini, D.8
  • 138
    • 0037116582 scopus 로고    scopus 로고
    • The absolute concentration of nigral neuromelanin, assayed by a new sensitive method, increases throughout the life and is dramatically decreased in Parkinson’s disease
    • COI: 1:CAS:528:DC%2BD38XktFegtw%3D%3D, PID: 11801257
    • Zecca L, Fariello R, Riederer P, Sulzer D, Gatti A, Tampellini D (2002) The absolute concentration of nigral neuromelanin, assayed by a new sensitive method, increases throughout the life and is dramatically decreased in Parkinson’s disease. FEBS Lett 510(3):216–220
    • (2002) FEBS Lett , vol.510 , Issue.3 , pp. 216-220
    • Zecca, L.1    Fariello, R.2    Riederer, P.3    Sulzer, D.4    Gatti, A.5    Tampellini, D.6
  • 139
    • 27844547163 scopus 로고    scopus 로고
    • In vivo detection of iron and neuromelanin by transcranial sonography: a new approach for early detection of substantia nigra damage
    • PID: 15986424
    • Zecca L, Berg D, Arzberger T, Ruprecht P, Rausch WD, Musicco M, Tampellini D, Riederer P, Gerlach M, Becker G (2005) In vivo detection of iron and neuromelanin by transcranial sonography: a new approach for early detection of substantia nigra damage. Mov Disord 20(10):1278–1285. doi:10.1002/mds.20550
    • (2005) Mov Disord , vol.20 , Issue.10 , pp. 1278-1285
    • Zecca, L.1    Berg, D.2    Arzberger, T.3    Ruprecht, P.4    Rausch, W.D.5    Musicco, M.6    Tampellini, D.7    Riederer, P.8    Gerlach, M.9    Becker, G.10
  • 140
    • 84940467351 scopus 로고    scopus 로고
    • Activated iron-containing microglia in the human hippocampus identified by magnetic resonance imaging in Alzheimer disease
    • COI: 1:CAS:528:DC%2BC2MXhtVKmt7%2FO, PID: 26190634
    • Zeineh MM, Chen Y, Kitzler HH, Hammond R, Vogel H, Rutt BK (2015) Activated iron-containing microglia in the human hippocampus identified by magnetic resonance imaging in Alzheimer disease. Neurobiol Aging 36(9):2483–2500. doi:10.1016/j.neurobiolaging.2015.05.022
    • (2015) Neurobiol Aging , vol.36 , Issue.9 , pp. 2483-2500
    • Zeineh, M.M.1    Chen, Y.2    Kitzler, H.H.3    Hammond, R.4    Vogel, H.5    Rutt, B.K.6
  • 142
    • 72749101173 scopus 로고    scopus 로고
    • Divalent metal transporter 1 is involved in amyloid precursor protein processing and Abeta generation
    • COI: 1:CAS:528:DC%2BD1MXhsFCgur%2FL, PID: 19679638
    • Zheng W, Xin N, Chi ZH, Zhao BL, Zhang J, Li JY, Wang ZY (2009) Divalent metal transporter 1 is involved in amyloid precursor protein processing and Abeta generation. FASEB J 23(12):4207–4217. doi:10.1096/fj.09-135749
    • (2009) FASEB J , vol.23 , Issue.12 , pp. 4207-4217
    • Zheng, W.1    Xin, N.2    Chi, Z.H.3    Zhao, B.L.4    Zhang, J.5    Li, J.Y.6    Wang, Z.Y.7
  • 143
    • 84891859053 scopus 로고    scopus 로고
    • Neuromelanin of the human substantia nigra: an update
    • COI: 1:CAS:528:DC%2BC2cXkvFGksA%3D%3D, PID: 24155156
    • Zucca FA, Basso E, Cupaioli FA, Ferrari E, Sulzer D, Casella L, Zecca L (2014) Neuromelanin of the human substantia nigra: an update. Neurotox Res 25(1):13–23. doi:10.1007/s12640-013-9435-y
    • (2014) Neurotox Res , vol.25 , Issue.1 , pp. 13-23
    • Zucca, F.A.1    Basso, E.2    Cupaioli, F.A.3    Ferrari, E.4    Sulzer, D.5    Casella, L.6    Zecca, L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.