메뉴 건너뛰기




Volumn 11, Issue APR, 2017, Pages

Metallothionein, copper and alpha-synuclein in alpha-synucleinopathies

Author keywords

A synuclein; Copper; Dementia with lewy bodies; Metallothionein; Multiple system atrophy; Parkinson's disease

Indexed keywords

ALPHA SYNUCLEIN; COPPER; DEXAMETHASONE; MENKES PROTEIN; METALLOTHIONEIN; METALLOTHIONEIN I; METALLOTHIONEIN II; METALLOTHIONEIN III; NEUROMELANIN; REACTIVE OXYGEN METABOLITE;

EID: 85018403205     PISSN: 16624548     EISSN: 1662453X     Source Type: Journal    
DOI: 10.3389/fnins.2017.00114     Document Type: Short Survey
Times cited : (58)

References (139)
  • 2
    • 46149107512 scopus 로고    scopus 로고
    • Rapid restoration of cognition in Alzheimer's transgenic mice with 8-hydroxy quinoline analogs is associated with decreased interstitial Aß
    • Adlard, P. A., Cherny, R. A., Finkelstein, D. I., Gautier, E., Robb, E., Cortes, M., et al. (2008). Rapid restoration of cognition in Alzheimer's transgenic mice with 8-hydroxy quinoline analogs is associated with decreased interstitial Aß. Neuron 59, 43-55. doi: 10.1016/j.neuron.2008.06.018
    • (2008) Neuron , vol.59 , pp. 43-55
    • Adlard, P.A.1    Cherny, R.A.2    Finkelstein, D.I.3    Gautier, E.4    Robb, E.5    Cortes, M.6
  • 3
    • 84950331777 scopus 로고    scopus 로고
    • Overexpression of alpha-synuclein at non-toxic levels increases dopaminergic cell death induced by copper exposure via modulation of protein degradation pathways
    • Anandhan, A., Rodriguez-Rocha, H., Bohovych, I., Griggs, A. M., Zavala-Flores, L., Reyes-Reyes, E. M., et al. (2015). Overexpression of alpha-synuclein at non-toxic levels increases dopaminergic cell death induced by copper exposure via modulation of protein degradation pathways. Neurobiol. Dis. 81, 76-93. doi: 10.1016/j.nbd.2014.11.018
    • (2015) Neurobiol. Dis , vol.81 , pp. 76-93
    • Anandhan, A.1    Rodriguez-Rocha, H.2    Bohovych, I.3    Griggs, A.M.4    Zavala-Flores, L.5    Reyes-Reyes, E.M.6
  • 4
    • 77049115153 scopus 로고    scopus 로고
    • Clinical utility of copper, ceruloplasmin, and metallothionein plasma determinations in human neurodegenerative patients and their first-degree relatives
    • Arnal, N., Cristalli, D. O., de Alaniz, M. J., and Marra, C. A. (2010). Clinical utility of copper, ceruloplasmin, and metallothionein plasma determinations in human neurodegenerative patients and their first-degree relatives. Brain Res. 1319, 118-130. doi: 10.1016/j.brainres.2009.11.085
    • (2010) Brain Res , vol.1319 , pp. 118-130
    • Arnal, N.1    Cristalli, D.O.2    de Alaniz, M.J.3    Marra, C.A.4
  • 5
    • 84936846732 scopus 로고    scopus 로고
    • Inhibition of amyloid-[beta] plaque formation by [alpha]-synuclein
    • Bachhuber, T., Katzmarski, N., McCarter, J. F., Loreth, D., Tahirovic, S., Kamp, F., et al. (2015). Inhibition of amyloid-[beta] plaque formation by [alpha]-synuclein. Nat. Med. 21, 802-807. doi: 10.1038/nm.3885
    • (2015) Nat. Med , vol.21 , pp. 802-807
    • Bachhuber, T.1    Katzmarski, N.2    McCarter, J.F.3    Loreth, D.4    Tahirovic, S.5    Kamp, F.6
  • 6
    • 43049150678 scopus 로고    scopus 로고
    • Metals in alzheimer's and parkinsons diseases
    • Barnham, K. J., and Bush, A. I. (2008). Metals in alzheimer's and parkinsons diseases. Curr. Opin. Chem. Biol. 12, 222-228. doi: 10.1016/j.cbpa.2008.02.019
    • (2008) Curr. Opin. Chem. Biol , vol.12 , pp. 222-228
    • Barnham, K.J.1    Bush, A.I.2
  • 7
    • 1642308134 scopus 로고    scopus 로고
    • Neurodegenerative diseases and oxidative stress-a report
    • Barnham, K. J., Masters, C. L., and Bush, A. I. (2004). Neurodegenerative diseases and oxidative stress-a report. Nat. Rev. Drug Discov. 3, 205-210. doi: 10.1038/nrd1330
    • (2004) Nat. Rev. Drug Discov , vol.3 , pp. 205-210
    • Barnham, K.J.1    Masters, C.L.2    Bush, A.I.3
  • 11
    • 77049088538 scopus 로고    scopus 로고
    • Risks of copper and iron toxicity during aging in humans
    • Brewer, G. J. (2009). Risks of copper and iron toxicity during aging in humans. Chem. Res. Toxicol. 23, 319-326. doi: 10.1021/tx900338d
    • (2009) Chem. Res. Toxicol , vol.23 , pp. 319-326
    • Brewer, G.J.1
  • 12
    • 84873355344 scopus 로고    scopus 로고
    • Copper (I)-a-synuclein interaction: structural description of two independent and competing metal binding sites
    • Camponeschi, F., Valensin, D., Tessari, I., Bubacco, L., Dell'Acqua, S., Casella, L., et al. (2013). Copper (I)-a-synuclein interaction: structural description of two independent and competing metal binding sites. Inorg. Chem. 52, 1358-1367. doi: 10.1021/ic302050m
    • (2013) Inorg. Chem , vol.52 , pp. 1358-1367
    • Camponeschi, F.1    Valensin, D.2    Tessari, I.3    Bubacco, L.4    Dell'Acqua, S.5    Casella, L.6
  • 13
    • 84924975806 scopus 로고    scopus 로고
    • Insights on the interaction of alpha-synuclein and metals in the pathophysiology of Parkinson's disease
    • Carboni, E., and Lingor, P. (2015). Insights on the interaction of alpha-synuclein and metals in the pathophysiology of Parkinson's disease. Metallomics 7, 395-404. doi: 10.1039/c4mt00339j
    • (2015) Metallomics , vol.7 , pp. 395-404
    • Carboni, E.1    Lingor, P.2
  • 14
    • 36248968195 scopus 로고    scopus 로고
    • Metallothionein functions and structural characteristics
    • Carpenè, E., Andreani, G., and Isani, G. (2007). Metallothionein functions and structural characteristics. J. Trace Elem. Med. Biol. 21, 35-39. doi: 10.1016/j.jtemb.2007.09.011
    • (2007) J. Trace Elem. Med. Biol , vol.21 , pp. 35-39
    • Carpenè, E.1    Andreani, G.2    Isani, G.3
  • 16
    • 84894066177 scopus 로고    scopus 로고
    • Metallothioneins as dynamic markers for brain disease in lysosomal disorders
    • Cesani, M., Cavalca, E., Macco, R., Leoncini, G., Terreni, M. R., Lorioli, L., et al. (2014). Metallothioneins as dynamic markers for brain disease in lysosomal disorders. Ann. Neurol. 75, 127-137. doi: 10.1002/ana.24053
    • (2014) Ann. Neurol , vol.75 , pp. 127-137
    • Cesani, M.1    Cavalca, E.2    Macco, R.3    Leoncini, G.4    Terreni, M.R.5    Lorioli, L.6
  • 17
    • 84894075304 scopus 로고    scopus 로고
    • Genetic insights into sporadic Parkinson's disease pathogenesis
    • Chai, C., and Lim, K.-L. (2013). Genetic insights into sporadic Parkinson's disease pathogenesis. Curr. Genomics 14, 486-501. doi: 10.2174/1389202914666131210195808
    • (2013) Curr. Genomics , vol.14 , pp. 486-501
    • Chai, C.1    Lim, K.-L.2
  • 18
    • 17844406856 scopus 로고    scopus 로고
    • a-Synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease
    • Chen, L. I., and Feany, M. B. (2005). a-Synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease. Nat. Neurosci. 8, 657-663. doi: 10.1038/nn1443
    • (2005) Nat. Neurosci , vol.8 , pp. 657-663
    • Chen, L.I.1    Feany, M.B.2
  • 19
    • 0034964390 scopus 로고    scopus 로고
    • Treatment with a copper-zinc chelator markedly and rapidly inhibits ß-amyloid accumulation in Alzheimer's disease transgenic mice
    • Cherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., et al. (2001). Treatment with a copper-zinc chelator markedly and rapidly inhibits ß-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron 30, 665-676. doi: 10.1016/s0896-6273(01)00317-8
    • (2001) Neuron , vol.30 , pp. 665-676
    • Cherny, R.A.1    Atwood, C.S.2    Xilinas, M.E.3    Gray, D.N.4    Jones, W.D.5    McLean, C.A.6
  • 20
    • 57649158930 scopus 로고    scopus 로고
    • Copper transport to the brain by the blood-brain barrier and blood-CSF barrier
    • Choi, B.-S., and Zheng, W. (2009). Copper transport to the brain by the blood-brain barrier and blood-CSF barrier. Brain Res. 1248, 14-21. doi: 10.1016/j.brainres.2008.10.056
    • (2009) Brain Res , vol.1248 , pp. 14-21
    • Choi, B.-S.1    Zheng, W.2
  • 21
    • 77957774530 scopus 로고    scopus 로고
    • The native copper-and zinc-binding protein metallothionein blocks copper-mediated Aß aggregation and toxicity in rat cortical neurons
    • Chung, R. S., Howells, C., Eaton, E. D., Shabala, L., Zovo, K., Palumaa, P., et al. (2010). The native copper-and zinc-binding protein metallothionein blocks copper-mediated Aß aggregation and toxicity in rat cortical neurons. PLoS ONE 5:e12030. doi: 10.1371/journal.pone.0012030
    • (2010) PLoS ONE , vol.5
    • Chung, R.S.1    Howells, C.2    Eaton, E.D.3    Shabala, L.4    Zovo, K.5    Palumaa, P.6
  • 22
    • 70449528753 scopus 로고    scopus 로고
    • Metallothionein treatment attenuates microglial activation and expression of neurotoxic quinolinic acid following traumatic brain injury
    • Chung, R. S., Leung, Y. K., Butler, C. W., Chen, Y., Eaton, E. D., Pankhurst, M. W., et al. (2009). Metallothionein treatment attenuates microglial activation and expression of neurotoxic quinolinic acid following traumatic brain injury. Neurotox. Res. 15, 381-389. doi: 10.1007/s12640-009-9044-y
    • (2009) Neurotox. Res , vol.15 , pp. 381-389
    • Chung, R.S.1    Leung, Y.K.2    Butler, C.W.3    Chen, Y.4    Eaton, E.D.5    Pankhurst, M.W.6
  • 23
    • 47249146602 scopus 로고    scopus 로고
    • Redefining the role of metallothionein within the injured brain Extracellular metallothioneins play an important role in the astrocyte-neuron response to injury
    • Chung, R. S., Penkowa, M., Dittmann, J., King, C. E., Bartlett, C., Asmussen, J. W., et al. (2008). Redefining the role of metallothionein within the injured brain Extracellular metallothioneins play an important role in the astrocyte-neuron response to injury. J. Biol. Chem. 283, 15349-15358. doi: 10.1074/jbc.M708446200
    • (2008) J. Biol. Chem , vol.283 , pp. 15349-15358
    • Chung, R.S.1    Penkowa, M.2    Dittmann, J.3    King, C.E.4    Bartlett, C.5    Asmussen, J.W.6
  • 24
    • 0037996720 scopus 로고    scopus 로고
    • Metallothionein-IIA promotes initial neurite elongation and postinjury reactive neurite growth and facilitates healing after focal cortical brain injury
    • Chung, R. S., Vickers, J. C., Chuah, M. I., and West, A. K. (2003). Metallothionein-IIA promotes initial neurite elongation and postinjury reactive neurite growth and facilitates healing after focal cortical brain injury. J. Neurosci. 23, 3336-3342
    • (2003) J. Neurosci , vol.23 , pp. 3336-3342
    • Chung, R.S.1    Vickers, J.C.2    Chuah, M.I.3    West, A.K.4
  • 25
    • 84898775157 scopus 로고    scopus 로고
    • Pharmacological treatment of Parkinson disease: a review
    • Connolly, B. S., and Lang, A. E. (2014). Pharmacological treatment of Parkinson disease: a review. JAMA 311, 1670-1683. doi: 10.1001/jama.2014.3654
    • (2014) JAMA , vol.311 , pp. 1670-1683
    • Connolly, B.S.1    Lang, A.E.2
  • 26
    • 84861563520 scopus 로고    scopus 로고
    • Direct observation of the interconversion of normal and toxic forms of a-synuclein
    • Cremades, N., Cohen, S. I. A., Deas, E., Abramov, A. Y., Chen, A. Y., Orte, A., et al. (2012). Direct observation of the interconversion of normal and toxic forms of a-synuclein. Cell 149, 1048-1059. doi: 10.1016/j.cell.2012.03.037
    • (2012) Cell , vol.149 , pp. 1048-1059
    • Cremades, N.1    Cohen, S.I.A.2    Deas, E.3    Abramov, A.Y.4    Chen, A.Y.5    Orte, A.6
  • 27
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: mechanism and models
    • Dauer, W., and Prezedborski, S. (2003). Parkinson's disease: mechanism and models. Neuron 39, 889-909. doi: 10.1016/S0896-6273(03)00568-3
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Prezedborski, S.2
  • 28
    • 84891373057 scopus 로고    scopus 로고
    • Copper pathology in vulnerable brain regions in Parkinson's disease
    • Davies, K. M., Bohic, S., Carmona, A., Ortega, R., Cottam, V., Hare, D. J., et al. (2014). Copper pathology in vulnerable brain regions in Parkinson's disease. Neurobiol. Aging 35, 858-866. doi: 10.1016/j.neurobiolaging.2013.09.034
    • (2014) Neurobiol. Aging , vol.35 , pp. 858-866
    • Davies, K.M.1    Bohic, S.2    Carmona, A.3    Ortega, R.4    Cottam, V.5    Hare, D.J.6
  • 29
    • 84871796736 scopus 로고    scopus 로고
    • Localization of copper and copper transporters in the human brain
    • Davies, K. M., Hare, D. J., Cottam, V., Chen, N., Hilgers, L., Halliday, G., et al. (2013). Localization of copper and copper transporters in the human brain. Metallomics 5, 43-51. doi: 10.1039/C2MT20151H
    • (2013) Metallomics , vol.5 , pp. 43-51
    • Davies, K.M.1    Hare, D.J.2    Cottam, V.3    Chen, N.4    Hilgers, L.5    Halliday, G.6
  • 30
    • 84973563260 scopus 로고    scopus 로고
    • Copper dyshomoeostasis in Parkinson's disease: implications for pathogenesis and indications for novel therapeutics
    • Davies, K. M., Mercer, J. F., Chen, N., and Double, K. L. (2016). Copper dyshomoeostasis in Parkinson's disease: implications for pathogenesis and indications for novel therapeutics. Clin. Sci. 130, 565-574. doi: 10.1042/CS20150153
    • (2016) Clin. Sci , vol.130 , pp. 565-574
    • Davies, K.M.1    Mercer, J.F.2    Chen, N.3    Double, K.L.4
  • 31
    • 84929591023 scopus 로고    scopus 로고
    • Remote His50 acts as a coordination switch in the high-affinity N-terminal centered copper (II) site of a-synuclein
    • De Ricco, R., Valensin, D., Dell'Acqua, S., Casella, L., Dorlet, P., Faller, P., et al. (2015a). Remote His50 acts as a coordination switch in the high-affinity N-terminal centered copper (II) site of a-synuclein. Inorg. Chem. 54, 4744-4751. doi: 10.1021/acs.inorgchem.5b00120
    • (2015) Inorg. Chem , vol.54 , pp. 4744-4751
    • De Ricco, R.1    Valensin, D.2    Dell'Acqua, S.3    Casella, L.4    Dorlet, P.5    Faller, P.6
  • 32
    • 84945189873 scopus 로고    scopus 로고
    • Copper (I/II), a/ß-Synuclein and Amyloid-ß: menage à Trois?
    • De Ricco, R., Valensin, D., Dell'Acqua, S., Casella, L., Hureau, C., and Faller, P. (2015b). Copper (I/II), a/ß-Synuclein and Amyloid-ß: menage à Trois? ChemBioChem 16, 2319-2328. doi: 10.1002/cbic.201500425
    • (2015) ChemBioChem , vol.16 , pp. 2319-2328
    • De Ricco, R.1    Valensin, D.2    Dell'Acqua, S.3    Casella, L.4    Hureau, C.5    Faller, P.6
  • 33
    • 84916631717 scopus 로고    scopus 로고
    • Balance between metallothionein and metal response element binding transcription factor 1 is mediated by zinc ions (Review)
    • Dong, G., Chen, H., Qi, M., Dou, Y., and Wang, Q. (2015). Balance between metallothionein and metal response element binding transcription factor 1 is mediated by zinc ions (Review). Mol. Med. Rep. 11, 1582-1586. doi: 10.3892/mmr.2014.2969
    • (2015) Mol. Med. Rep , vol.11 , pp. 1582-1586
    • Dong, G.1    Chen, H.2    Qi, M.3    Dou, Y.4    Wang, Q.5
  • 34
    • 45249097302 scopus 로고    scopus 로고
    • Cu2+ binding modes of recombinant a-synuclein-insights from EPR spectroscopy
    • Drew, S. C., Ling Leong, S., Pham, C. L., Tew, D. J., Masters, C. L., Miles, L. A., et al. (2008). Cu2+ binding modes of recombinant a-synuclein-insights from EPR spectroscopy. J. Am. Chem. Soc. 130, 7766-7773. doi: 10.1021/ja800708x
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 7766-7773
    • Drew, S.C.1    Ling Leong, S.2    Pham, C.L.3    Tew, D.J.4    Masters, C.L.5    Miles, L.A.6
  • 35
    • 84878892468 scopus 로고    scopus 로고
    • Calcium entry and a-synuclein inclusions elevate dendritic mitochondrial oxidant stress in dopaminergic neurons
    • Dryanovski, D. I., Guzman, J. N., Xie, Z., Galteri, D. J., Volpicelli-Daley, L. A., Lee, V. M. Y., et al. (2013). Calcium entry and a-synuclein inclusions elevate dendritic mitochondrial oxidant stress in dopaminergic neurons. J. Neurosci. 33, 10154-10164. doi: 10.1523/jneurosci.5311-12.2013
    • (2013) J. Neurosci , vol.33 , pp. 10154-10164
    • Dryanovski, D.I.1    Guzman, J.N.2    Xie, Z.3    Galteri, D.J.4    Volpicelli-Daley, L.A.5    Lee, V.M.Y.6
  • 36
    • 33749610125 scopus 로고    scopus 로고
    • Metallothioneins 1 and 2 attenuate peroxynitrite-induced oxidative stress in Parkinson disease
    • Ebadi, M., and Sharma, S. (2006). Metallothioneins 1 and 2 attenuate peroxynitrite-induced oxidative stress in Parkinson disease. Exp. Biol. Med. 231, 1576-1583. doi: 10.1177/153537020623100919
    • (2006) Exp. Biol. Med , vol.231 , pp. 1576-1583
    • Ebadi, M.1    Sharma, S.2
  • 37
    • 15744373545 scopus 로고    scopus 로고
    • Metallothionein-mediated neuroprotection in genetically engineered mouse models of Parkinson's disease
    • Ebadi, M., Brown-Borg, H., El Refaey, H., Singh, B. B., Garrett, S., Shavali, S., et al. (2005). Metallothionein-mediated neuroprotection in genetically engineered mouse models of Parkinson's disease. Brain Res. Mol. Brain Res. 134, 67-75. doi: 10.1016/j.molbrainres.2004.09.011
    • (2005) Brain Res. Mol. Brain Res , vol.134 , pp. 67-75
    • Ebadi, M.1    Brown-Borg, H.2    El Refaey, H.3    Singh, B.B.4    Garrett, S.5    Shavali, S.6
  • 38
    • 85013757375 scopus 로고    scopus 로고
    • Biomarker-driven phenotyping in Parkinson's disease: a translational missing link in disease-modifying clinical trials
    • Espay, A. J., Schwarzschild, M. A., Tanner, C. M., Fernandez, H. H., Simon, D. K., Leverenz, J. B., et al. (2017). Biomarker-driven phenotyping in Parkinson's disease: a translational missing link in disease-modifying clinical trials. Mov. Disord. 32, 319-324. doi: 10.1002/mds.26913
    • (2017) Mov. Disord , vol.32 , pp. 319-324
    • Espay, A.J.1    Schwarzschild, M.A.2    Tanner, C.M.3    Fernandez, H.H.4    Simon, D.K.5    Leverenz, J.B.6
  • 39
    • 77954377635 scopus 로고    scopus 로고
    • Neuronal growth inhibitory factor (metallothionein-3): reactivity and structure of metal-thiolate clusters
    • Faller, P. (2010). Neuronal growth inhibitory factor (metallothionein-3): reactivity and structure of metal-thiolate clusters. FEBS J. 277, 2921-2930. doi: 10.1111/j.1742-4658.2010.07717.x
    • (2010) FEBS J , vol.277 , pp. 2921-2930
    • Faller, P.1
  • 40
    • 84955581925 scopus 로고    scopus 로고
    • Clioquinol improves cognitive, motor function, and microanatomy of the Alpha-synuclein hA53T transgenic mice
    • Finkelstein, D. I., Hare, D. J., Billings, J. L., Sedjahtera, A., Nurjono, M., Arthofer, E., et al. (2016). Clioquinol improves cognitive, motor function, and microanatomy of the Alpha-synuclein hA53T transgenic mice. ACS Chem. Neurosci. 7, 119-129. doi: 10.1021/acschemneuro.5b00253
    • (2016) ACS Chem. Neurosci , vol.7 , pp. 119-129
    • Finkelstein, D.I.1    Hare, D.J.2    Billings, J.L.3    Sedjahtera, A.4    Nurjono, M.5    Arthofer, E.6
  • 41
    • 34848813494 scopus 로고    scopus 로고
    • Metallothionein-IIA promotes neurite growth via the megalin receptor
    • Fitzgerald, M., Nairn, P., Bartlett, C. A., Chung, R. S., West, A. K., and Beazley, L. D. (2007). Metallothionein-IIA promotes neurite growth via the megalin receptor. Exp. Brain Res. 183, 171-180. doi: 10.1007/s00221-007-1032-y
    • (2007) Exp. Brain Res , vol.183 , pp. 171-180
    • Fitzgerald, M.1    Nairn, P.2    Bartlett, C.A.3    Chung, R.S.4    West, A.K.5    Beazley, L.D.6
  • 42
    • 84892489531 scopus 로고    scopus 로고
    • The Vps35 D620N mutation linked to Parkinson's disease disrupts the cargo sorting function of retromer
    • Follett, J., Norwood, S. J., Hamilton, N. A., Mohan, M., Kovtun, O., Tay, S., et al. (2014). The Vps35 D620N mutation linked to Parkinson's disease disrupts the cargo sorting function of retromer. Traffic 15, 230-244. doi: 10.1111/tra.12136
    • (2014) Traffic , vol.15 , pp. 230-244
    • Follett, J.1    Norwood, S.J.2    Hamilton, N.A.3    Mohan, M.4    Kovtun, O.5    Tay, S.6
  • 43
    • 0034796353 scopus 로고    scopus 로고
    • Role of free radicals in the neurodegenerative diseases
    • Halliwell, B. (2001). Role of free radicals in the neurodegenerative diseases. Drugs Aging 18, 685-716. doi: 10.2165/00002512-200118090-00004
    • (2001) Drugs Aging , vol.18 , pp. 685-716
    • Halliwell, B.1
  • 44
    • 67651160657 scopus 로고    scopus 로고
    • Neuroprotection trials in Parkinson's disease: systematic review
    • Hart, R. G., Pearce, L. A., Ravina, B. M., Yaltho, T. C., and Marler, J. R. (2009). Neuroprotection trials in Parkinson's disease: systematic review. Mov. Disord. 24, 647-654. doi: 10.1002/mds.22432
    • (2009) Mov. Disord , vol.24 , pp. 647-654
    • Hart, R.G.1    Pearce, L.A.2    Ravina, B.M.3    Yaltho, T.C.4    Marler, J.R.5
  • 45
    • 77954350284 scopus 로고    scopus 로고
    • Neuronal growth-inhibitory factor (metallothionein-3): evaluation of the biological function of growth-inhibitory factor in the injured and neurodegenerative brain
    • Howells, C., West, A. K., and Chung, R. S. (2010). Neuronal growth-inhibitory factor (metallothionein-3): evaluation of the biological function of growth-inhibitory factor in the injured and neurodegenerative brain. FEBS J. 277, 2931-2939. doi: 10.1111/j.1742-4658.2010.07718.x
    • (2010) FEBS J , vol.277 , pp. 2931-2939
    • Howells, C.1    West, A.K.2    Chung, R.S.3
  • 46
    • 84878770600 scopus 로고    scopus 로고
    • Roles and therapeutic potential of metallothioneins in neurodegenerative diseases
    • Hozumi, I. (2013). Roles and therapeutic potential of metallothioneins in neurodegenerative diseases. Curr. Pharm. Biotechnol. 14, 408-413. doi: 10.2174/1389201011314040004
    • (2013) Curr. Pharm. Biotechnol , vol.14 , pp. 408-413
    • Hozumi, I.1
  • 47
    • 24744431646 scopus 로고    scopus 로고
    • Metallothioneins and neurodegenerative diseases
    • Hozumi, I., Asanuma, M., Yamada, M., and Uchida, Y. (2004). Metallothioneins and neurodegenerative diseases. J. Health Sci. 50, 323-331. doi: 10.1248/jhs.50.323
    • (2004) J. Health Sci , vol.50 , pp. 323-331
    • Hozumi, I.1    Asanuma, M.2    Yamada, M.3    Uchida, Y.4
  • 48
    • 79952816599 scopus 로고    scopus 로고
    • Patterns of levels of biological metals in CSF differ among neurodegenerative diseases
    • Hozumi, I., Hasegawa, T., Honda, A., Ozawa, K., Hayashi, Y., Hashimoto, K., et al. (2011). Patterns of levels of biological metals in CSF differ among neurodegenerative diseases. J. Neurol. Sci. 303, 95-99. doi: 10.1016/j.jns.2011.01.003
    • (2011) J. Neurol. Sci , vol.303 , pp. 95-99
    • Hozumi, I.1    Hasegawa, T.2    Honda, A.3    Ozawa, K.4    Hayashi, Y.5    Hashimoto, K.6
  • 49
    • 84863655953 scopus 로고    scopus 로고
    • Current concepts in parkinson's disease and other movement disorders
    • Jankovic, J. J. (2012). Current concepts in parkinson's disease and other movement disorders. Curr. Opin. Neurol. 25, 429-432. doi: 10.1097/WCO.0b013e3283550cdd
    • (2012) Curr. Opin. Neurol , vol.25 , pp. 429-432
    • Jankovic, J.J.1
  • 50
    • 84918784686 scopus 로고    scopus 로고
    • Neuropathology of multiple system atrophy: new thoughts about pathogenesis
    • Jellinger, K. A. (2014). Neuropathology of multiple system atrophy: new thoughts about pathogenesis. Mov. Disord. 29, 1720-1741. doi: 10.1002/mds.26052
    • (2014) Mov. Disord , vol.29 , pp. 1720-1741
    • Jellinger, K.A.1
  • 51
    • 84880229894 scopus 로고    scopus 로고
    • Parkinson's disease-the debate on the clinical phenomenology, aetiology, pathology and pathogenesis
    • Jenner, P., Morris, H. R., Robbins, T. W., Goedert, M., Hardy, J., Ben-Shlomo, Y., et al. (2013). Parkinson's disease-the debate on the clinical phenomenology, aetiology, pathology and pathogenesis. J. Parkinson's Dis. 3, 1-11. doi: 10.3233/JPD-130175
    • (2013) J. Parkinson's Dis , vol.3 , pp. 1-11
    • Jenner, P.1    Morris, H.R.2    Robbins, T.W.3    Goedert, M.4    Hardy, J.5    Ben-Shlomo, Y.6
  • 52
    • 84883688262 scopus 로고    scopus 로고
    • Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
    • Jucker, M., and Walker, L. C. (2013). Self-propagation of pathogenic protein aggregates in neurodegenerative diseases. Nature 501, 45-51. doi: 10.1038/nature12481
    • (2013) Nature , vol.501 , pp. 45-51
    • Jucker, M.1    Walker, L.C.2
  • 53
    • 0001593597 scopus 로고
    • Metallothionein: a cadmium-and zinc-containing protein from equine renal cortex
    • Kägi, J. H., and Vallee, B. L. (1960). Metallothionein: a cadmium-and zinc-containing protein from equine renal cortex. J. Biol. Chem. 235, 3460-3465
    • (1960) J. Biol. Chem , vol.235 , pp. 3460-3465
    • Kägi, J.H.1    Vallee, B.L.2
  • 54
    • 0021242444 scopus 로고
    • Characterization of DNA sequences through which cadmium and glucocorticoid hormones induce human metallothionein-IIA gene
    • Karin, M., Haslinger, A., Holtgreve, H., Richards, R. I., Krauter, P., Westphal, H. M., et al. (1984). Characterization of DNA sequences through which cadmium and glucocorticoid hormones induce human metallothionein-IIA gene. Nature 308, 513-519. doi: 10.1038/308513a0
    • (1984) Nature , vol.308 , pp. 513-519
    • Karin, M.1    Haslinger, A.2    Holtgreve, H.3    Richards, R.I.4    Krauter, P.5    Westphal, H.M.6
  • 55
    • 0018819295 scopus 로고
    • Primary induction of metallothionein by dexamethasone in cultured rat hepatocytes
    • Karin, M., Herschman, H. R., and Weinstein, D. (1980). Primary induction of metallothionein by dexamethasone in cultured rat hepatocytes. Biochem. Biophys. Res. Commun. 92, 1052-1059. doi: 10.1016/0006-291X(80)90808-6
    • (1980) Biochem. Biophys. Res. Commun , vol.92 , pp. 1052-1059
    • Karin, M.1    Herschman, H.R.2    Weinstein, D.3
  • 56
    • 0029948054 scopus 로고    scopus 로고
    • A murine model of Menkes disease reveals a physiological function of metallothionein
    • Kelly, E. J., and Palmiter, R. D. (1996). A murine model of Menkes disease reveals a physiological function of metallothionein. Nat. Genet. 13, 219-222. doi: 10.1038/ng0696-219
    • (1996) Nat. Genet , vol.13 , pp. 219-222
    • Kelly, E.J.1    Palmiter, R.D.2
  • 57
    • 44849144623 scopus 로고    scopus 로고
    • Function of metallothionein in gene expression and signal transduction: newly found protective role of metallothionein
    • Kimura, T., and Itoh, N. (2008). Function of metallothionein in gene expression and signal transduction: newly found protective role of metallothionein. J. Health Sci. 54, 251-260. doi: 10.1248/jhs.54.251
    • (2008) J. Health Sci , vol.54 , pp. 251-260
    • Kimura, T.1    Itoh, N.2
  • 58
    • 0036550101 scopus 로고    scopus 로고
    • Parkinson-like neurodegeneration induced by targeted overexpression of a-synuclein in the nigrostriatal system
    • Kirik, D., Rosenblad, C., Burger, C., Lundberg, C., Johansen, T. E., Muzyczka, N., et al. (2002). Parkinson-like neurodegeneration induced by targeted overexpression of a-synuclein in the nigrostriatal system. J. Neurosci. 22, 2780-2791
    • (2002) J. Neurosci , vol.22 , pp. 2780-2791
    • Kirik, D.1    Rosenblad, C.2    Burger, C.3    Lundberg, C.4    Johansen, T.E.5    Muzyczka, N.6
  • 59
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • Kitada, T., Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., et al. (1998). Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392, 605-608. doi: 10.1038/33416
    • (1998) Nature , vol.392 , pp. 605-608
    • Kitada, T.1    Kitada, T.2    Asakawa, S.3    Hattori, N.4    Matsumine, H.5    Yamamura, Y.6
  • 60
    • 0019440985 scopus 로고
    • Induction of metallothionein by adrenocortical steroids
    • Klaassen, C. D. (1981). Induction of metallothionein by adrenocortical steroids. Toxicology 20, 275-279. doi: 10.1016/0300-483X(81)90034-2
    • (1981) Toxicology , vol.20 , pp. 275-279
    • Klaassen, C.D.1
  • 61
    • 0022414628 scopus 로고
    • Effects of dexamethasone on metallothionein induction by Zn, Cu and Cd in chang liver cells
    • Kobayashi, S., Okada, T., and Kimura, M. (1985). Effects of dexamethasone on metallothionein induction by Zn, Cu and Cd in chang liver cells. Chem. Biol. Interact. 55, 347-356. doi: 10.1016/S0009-2797(85)80141-1
    • (1985) Chem. Biol. Interact , vol.55 , pp. 347-356
    • Kobayashi, S.1    Okada, T.2    Kimura, M.3
  • 63
    • 34047228896 scopus 로고    scopus 로고
    • Blood metallothionein, neuron specific enolase, and protein S100B in patients with traumatic brain injury
    • Kukacka, J., Vajtr, D., Huska, D., Prusa, R., Houstava, L., Samal, F., et al. (2006). Blood metallothionein, neuron specific enolase, and protein S100B in patients with traumatic brain injury. Neuroendocrinol. Lett. 27, 116-120
    • (2006) Neuroendocrinol. Lett , vol.27 , pp. 116-120
    • Kukacka, J.1    Vajtr, D.2    Huska, D.3    Prusa, R.4    Houstava, L.5    Samal, F.6
  • 64
    • 0031958413 scopus 로고    scopus 로고
    • Copper metabolism in the kidney of rats administered copper and copper-metallothionein
    • Kurasaki, M., Okabe, M., Saito, S., and Suzuki-Kurasaki, M. (1998). Copper metabolism in the kidney of rats administered copper and copper-metallothionein. Am. J. Physiol. 274, F783-F790
    • (1998) Am. J. Physiol , vol.274 , pp. F783-F790
    • Kurasaki, M.1    Okabe, M.2    Saito, S.3    Suzuki-Kurasaki, M.4
  • 66
    • 84954501770 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor-related proteins in a novel mechanism of axon guidance and peripheral nerve regeneration
    • Landowski, L. M., Pavez, M., Brown, L. S., Gasperini, R., Taylor, B. V., West, A. K., et al. (2016). Low-density lipoprotein receptor-related proteins in a novel mechanism of axon guidance and peripheral nerve regeneration. J. Biol. Chem. 291, 1092-1102. doi: 10.1074/jbc.M115.668996
    • (2016) J. Biol. Chem , vol.291 , pp. 1092-1102
    • Landowski, L.M.1    Pavez, M.2    Brown, L.S.3    Gasperini, R.4    Taylor, B.V.5    West, A.K.6
  • 67
    • 66949152096 scopus 로고    scopus 로고
    • Parkinson's disease
    • Lees, A. J., Hardy, J., and Revesz, T. (2009). Parkinson's disease. Lancet 373, 2055-2066. doi: 10.1016/S0140-6736(09)60492-X
    • (2009) Lancet , vol.373 , pp. 2055-2066
    • Lees, A.J.1    Hardy, J.2    Revesz, T.3
  • 68
    • 84869404121 scopus 로고    scopus 로고
    • Distribution of exogenous metallothionein following intraperitoneal and intramuscular injection of metallothionein-deficient mice
    • Lewis, K. E., Chung, R. S., West, A. K., and Chuah, M. I. (2012). Distribution of exogenous metallothionein following intraperitoneal and intramuscular injection of metallothionein-deficient mice. Histol. Histopathol. 27, 1459-1470. doi: 10.14670/HH-27.1459
    • (2012) Histol. Histopathol , vol.27 , pp. 1459-1470
    • Lewis, K.E.1    Chung, R.S.2    West, A.K.3    Chuah, M.I.4
  • 69
    • 84869109864 scopus 로고    scopus 로고
    • Pathological a-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice
    • Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O'Brien, P., Trojanowski, J. Q., et al. (2012). Pathological a-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science 338, 949-953. doi: 10.1126/science.1227157
    • (2012) Science , vol.338 , pp. 949-953
    • Luk, K.C.1    Kehm, V.2    Carroll, J.3    Zhang, B.4    O'Brien, P.5    Trojanowski, J.Q.6
  • 70
    • 34447510930 scopus 로고    scopus 로고
    • Function and regulation of human copper-transporting ATPases
    • Lutsenko, S., Barnes, N. L., Bartee, M. Y., and Dmitriev, O. Y. (2007). Function and regulation of human copper-transporting ATPases. Physiol. Rev. 87, 1011-1046. doi: 10.1152/physrev.00004.2006
    • (2007) Physiol. Rev , vol.87 , pp. 1011-1046
    • Lutsenko, S.1    Barnes, N.L.2    Bartee, M.Y.3    Dmitriev, O.Y.4
  • 71
    • 34247120546 scopus 로고    scopus 로고
    • Iron, copper, and iron regulatory protein 2 in Alzheimer's disease and related dementias
    • Magaki, S., Raghavan, R., Mueller, C., Oberg, K. C., Vinters, H. V., and Kirsch, W. M. (2007). Iron, copper, and iron regulatory protein 2 in Alzheimer's disease and related dementias. Neurosci. Lett. 418, 72-76. doi: 10.1016/j.neulet.2007.02.077
    • (2007) Neurosci. Lett , vol.418 , pp. 72-76
    • Magaki, S.1    Raghavan, R.2    Mueller, C.3    Oberg, K.C.4    Vinters, H.V.5    Kirsch, W.M.6
  • 73
    • 84867849376 scopus 로고    scopus 로고
    • Characterization of the role of metallothionein-3 in an animal model of Alzheimer's disease
    • Manso, Y., Carrasco, J., Comes, G., Meloni, G., Adlard, P. A., Bush, A. I., et al. (2012a). Characterization of the role of metallothionein-3 in an animal model of Alzheimer's disease. Cell. Mol. Life Sci. 69, 3683-3700. doi: 10.1007/s00018-012-1047-9
    • (2012) Cell. Mol. Life Sci , vol.69 , pp. 3683-3700
    • Manso, Y.1    Carrasco, J.2    Comes, G.3    Meloni, G.4    Adlard, P.A.5    Bush, A.I.6
  • 74
    • 84867872169 scopus 로고    scopus 로고
    • Characterization of the role of the antioxidant proteins metallothioneins 1 and 2 in an animal model of Alzheimer's disease
    • Manso, Y., Carrasco, J., Comes, G., Adlard, P. A., Bush, A. I., and Hidalgo, J. (2012b). Characterization of the role of the antioxidant proteins metallothioneins 1 and 2 in an animal model of Alzheimer's disease. Cell. Mol. Life Sci. 69, 3665-3681. doi: 10.1007/s00018-012-1045-y
    • (2012) Cell. Mol. Life Sci , vol.69 , pp. 3665-3681
    • Manso, Y.1    Carrasco, J.2    Comes, G.3    Adlard, P.A.4    Bush, A.I.5    Hidalgo, J.6
  • 75
    • 84960080530 scopus 로고    scopus 로고
    • Overexpression of metallothionein-1 modulates the phenotype of the Tg2576 mouse model of Alzheimer's disease
    • Manso, Y., Comes, G., López-Ramos, J. C., Belfiore, M., Molinero, A., Giralt, M., et al. (2016). Overexpression of metallothionein-1 modulates the phenotype of the Tg2576 mouse model of Alzheimer's disease. J. Alzheimers Dis. 51, 81-95. doi: 10.3233/JAD-151025
    • (2016) J. Alzheimers Dis , vol.51 , pp. 81-95
    • Manso, Y.1    Comes, G.2    López-Ramos, J.C.3    Belfiore, M.4    Molinero, A.5    Giralt, M.6
  • 76
    • 33947463103 scopus 로고
    • A cadmium protein from equine kidney cortex
    • Margoshes, M., and Vallee, B. L. (1957). A cadmium protein from equine kidney cortex. J. Am. Chem. Soc. 79, 4813-4814. doi: 10.1021/ja01574a064
    • (1957) J. Am. Chem. Soc , vol.79 , pp. 4813-4814
    • Margoshes, M.1    Vallee, B.L.2
  • 77
    • 84864870837 scopus 로고    scopus 로고
    • Alpha-synuclein: from secretion to dysfunction and death
    • Marques, O., and Outeiro, T. F. (2012). Alpha-synuclein: from secretion to dysfunction and death. Cell Death Dis. 3, e350. doi: 10.1038/cddis.2012.94
    • (2012) Cell Death Dis , vol.3
    • Marques, O.1    Outeiro, T.F.2
  • 78
    • 0019507564 scopus 로고
    • Glucocorticoid regulation of metallothionein-I mRNA synthesis in cultured mouse cells
    • Mayo, K. E., and Palmiter, R. D. (1981). Glucocorticoid regulation of metallothionein-I mRNA synthesis in cultured mouse cells. J. Biol. Chem. 256, 2621-2624
    • (1981) J. Biol. Chem , vol.256 , pp. 2621-2624
    • Mayo, K.E.1    Palmiter, R.D.2
  • 79
    • 33744735681 scopus 로고    scopus 로고
    • Down-regulation of microglial activation may represent a practical strategy for combating neurodegenerative disorders
    • McCarty, M. F. (2006). Down-regulation of microglial activation may represent a practical strategy for combating neurodegenerative disorders. Med. Hypotheses 67, 251-269. doi: 10.1016/j.mehy.2006.01.013
    • (2006) Med. Hypotheses , vol.67 , pp. 251-269
    • McCarty, M.F.1
  • 80
    • 79955630377 scopus 로고    scopus 로고
    • Redox activity of a-synuclein-Cu is silenced by Zn 7-metallothionein-3
    • Meloni, G., and Vašák, M. (2011). Redox activity of a-synuclein-Cu is silenced by Zn 7-metallothionein-3. Free Radic. Biol. Med. 50, 1471-1479. doi: 10.1016/j.freeradbiomed.2011.02.003
    • (2011) Free Radic. Biol. Med , vol.50 , pp. 1471-1479
    • Meloni, G.1    Vašák, M.2
  • 81
    • 43749104422 scopus 로고    scopus 로고
    • Metal swap between Zn7-metallothionein-3 and amyloid-ß-Cu protects against amyloid-ß toxicity
    • Meloni, G., Sonois, V., Delaine, T., Guilloreau, L., Gillet, A., Teissié, J., et al. (2008). Metal swap between Zn7-metallothionein-3 and amyloid-ß-Cu protects against amyloid-ß toxicity. Nat. Chem. Biol. 4, 366-372. doi: 10.1038/nchembio.89
    • (2008) Nat. Chem. Biol , vol.4 , pp. 366-372
    • Meloni, G.1    Sonois, V.2    Delaine, T.3    Guilloreau, L.4    Gillet, A.5    Teissié, J.6
  • 82
  • 83
    • 84855289046 scopus 로고    scopus 로고
    • Up-regulation of metallothionein gene expression in parkinsonian astrocytes
    • Michael, G. J., Esmailzadeh, S., Moran, L. B., Christian, L., Pearce, R. K., and Graeber, M. B. (2011). Up-regulation of metallothionein gene expression in parkinsonian astrocytes. Neurogenetics 12, 295-305. doi: 10.1007/s10048-011-0294-5
    • (2011) Neurogenetics , vol.12 , pp. 295-305
    • Michael, G.J.1    Esmailzadeh, S.2    Moran, L.B.3    Christian, L.4    Pearce, R.K.5    Graeber, M.B.6
  • 84
    • 84899831410 scopus 로고    scopus 로고
    • Site-specific copper-catalyzed oxidation of a-synuclein: tightening the link between metal binding and protein oxidative damage in Parkinson's disease
    • Miotto, M. C., Rodriguez, E. E., Valiente-Gabioud, A. A., Torres-Monserrat, V., Binolfi, A., Quintanar, L., et al. (2014). Site-specific copper-catalyzed oxidation of a-synuclein: tightening the link between metal binding and protein oxidative damage in Parkinson's disease. Inorg. Chem. 53, 4350-4358. doi: 10.1021/ic4031377
    • (2014) Inorg. Chem , vol.53 , pp. 4350-4358
    • Miotto, M.C.1    Rodriguez, E.E.2    Valiente-Gabioud, A.A.3    Torres-Monserrat, V.4    Binolfi, A.5    Quintanar, L.6
  • 86
    • 2342439603 scopus 로고    scopus 로고
    • Comparison of dementia with Lewy bodies to Alzheimer's disease and Parkinson's disease with dementia
    • Noe, E., Marder, K., Bell, K. L., Jacobs, D. M., Manly, J. J., and Stern, Y. (2004). Comparison of dementia with Lewy bodies to Alzheimer's disease and Parkinson's disease with dementia. Mov. Disord. 19, 60-67. doi: 10.1002/mds.10633
    • (2004) Mov. Disord , vol.19 , pp. 60-67
    • Noe, E.1    Marder, K.2    Bell, K.L.3    Jacobs, D.M.4    Manly, J.J.5    Stern, Y.6
  • 87
    • 0031926361 scopus 로고    scopus 로고
    • Metallothioneins: historical review and state of knowledge
    • Nordberg, M. (1998). Metallothioneins: historical review and state of knowledge. Talanta 46, 243-254. doi: 10.1016/s0039-9140(97)00345-7
    • (1998) Talanta , vol.46 , pp. 243-254
    • Nordberg, M.1
  • 88
    • 85033782889 scopus 로고    scopus 로고
    • Genetics of synucleinopathies
    • [Epub ahead of print]
    • Nussbaum, R. L. (2017). Genetics of synucleinopathies. Cold Spring Harb. Perspect. Med. doi: 10.1101/cshperspect.a024109. [Epub ahead of print]
    • (2017) Cold Spring Harb. Perspect. Med
    • Nussbaum, R.L.1
  • 89
    • 24744459855 scopus 로고    scopus 로고
    • Transcriptional regulation of the metallothionein genes
    • Otsuka, F. (2004). Transcriptional regulation of the metallothionein genes. J. Health Sci. 50, 332-335. doi: 10.1248/jhs.50.332
    • (2004) J. Health Sci , vol.50 , pp. 332-335
    • Otsuka, F.1
  • 90
    • 0033564726 scopus 로고    scopus 로고
    • Copper (II)-induced self-oligomerization of a-synuclein
    • Paik, S. R., Shin, H. J., Lee, J. H., Chang, C. S., and Kim, J. (1999). Copper (II)-induced self-oligomerization of a-synuclein. Biochem. J. 340, 821-828. doi: 10.1042/bj3400821
    • (1999) Biochem. J , vol.340 , pp. 821-828
    • Paik, S.R.1    Shin, H.J.2    Lee, J.H.3    Chang, C.S.4    Kim, J.5
  • 91
    • 0023237555 scopus 로고
    • Raised cerebrospinal-fluid copper concentration in Parkinson's disease
    • Pall, H. S., Blake, D. R., Gutteridge, J. M., Williams, A. C., Lunec, J., Hall, M., et al. (1987). Raised cerebrospinal-fluid copper concentration in Parkinson's disease. Lancet 330, 238-241. doi: 10.1016/S0140-6736(87)90827-0
    • (1987) Lancet , vol.330 , pp. 238-241
    • Pall, H.S.1    Blake, D.R.2    Gutteridge, J.M.3    Williams, A.C.4    Lunec, J.5    Hall, M.6
  • 92
    • 0026631182 scopus 로고
    • MT-III, a brain-specific member of the metallothionein gene family
    • Palmiter, R. D., Findley, S. D., Whitmore, T. E., and Durnam, D. M. (1992). MT-III, a brain-specific member of the metallothionein gene family. Proc. Natl. Acad. Sci. U.S.A. 89, 6333-6337. doi: 10.1073/pnas.89.14.6333
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 6333-6337
    • Palmiter, R.D.1    Findley, S.D.2    Whitmore, T.E.3    Durnam, D.M.4
  • 93
  • 94
    • 84994032287 scopus 로고    scopus 로고
    • Persisting neurobehavioral effects of developmental copper exposure in wildtype and metallothionein 1 and 2 knockout mice
    • Petro, A., Sexton, H. G., Miranda, C., Rastogi, A., Freedman, J. H., and Levin, E. D. (2016). Persisting neurobehavioral effects of developmental copper exposure in wildtype and metallothionein 1 and 2 knockout mice. BMC Pharmacol. Toxicol. 17:55. doi: 10.1186/s40360-016-0096-3
    • (2016) BMC Pharmacol. Toxicol , vol.17 , pp. 55
    • Petro, A.1    Sexton, H.G.2    Miranda, C.3    Rastogi, A.4    Freedman, J.H.5    Levin, E.D.6
  • 95
    • 84962440535 scopus 로고    scopus 로고
    • Pioglitazone ameliorates the phenotype of a novel Parkinson's disease mouse model by reducing neuroinflammation
    • Pinto, M., Nissanka, N., Peralta, S., Brambilla, R., Diaz, F., and Moraes, C. T. (2016). Pioglitazone ameliorates the phenotype of a novel Parkinson's disease mouse model by reducing neuroinflammation. Mol. Neurodegener. 11:25. doi: 10.1186/s13024-016-0090-7
    • (2016) Mol. Neurodegener , vol.11 , pp. 25
    • Pinto, M.1    Nissanka, N.2    Peralta, S.3    Brambilla, R.4    Diaz, F.5    Moraes, C.T.6
  • 96
    • 78650550580 scopus 로고    scopus 로고
    • Association of metallothionein-III with oligodendroglial cytoplasmic inclusions in multiple system atrophy
    • Pountney, D. L., Dickson, T. C., Power, J. H. T., Vickers, J. C., West, A. J., and Gai, W. P. (2011). Association of metallothionein-III with oligodendroglial cytoplasmic inclusions in multiple system atrophy. Neurotox. Res. 19, 115-122. doi: 10.1007/s12640-009-9146-6
    • (2011) Neurotox. Res , vol.19 , pp. 115-122
    • Pountney, D.L.1    Dickson, T.C.2    Power, J.H.T.3    Vickers, J.C.4    West, A.J.5    Gai, W.P.6
  • 98
    • 84876226920 scopus 로고    scopus 로고
    • A novel a-synuclein missense mutation in Parkinson disease
    • Proukakis, C., Dudzik, C. G., Brier, T., MacKay, D. S., Cooper, J. M., Millhauser, G. L., et al. (2013). A novel a-synuclein missense mutation in Parkinson disease. Neurology 80, 1062-1064. doi: 10.1212/WNL.0b013e31828727ba
    • (2013) Neurology , vol.80 , pp. 1062-1064
    • Proukakis, C.1    Dudzik, C.G.2    Brier, T.3    MacKay, D.S.4    Cooper, J.M.5    Millhauser, G.L.6
  • 99
    • 84883761227 scopus 로고    scopus 로고
    • Aging results in copper accumulations in glial fibrillary acidic protein-positive cells in the subventricular zone
    • Pushkar, Y., Robison, G., Sullivan, B., Fu, S. X., Kohne, M., Jiang, W., et al. (2013). Aging results in copper accumulations in glial fibrillary acidic protein-positive cells in the subventricular zone. Aging Cell 12, 823-832. doi: 10.1111/acel.12112
    • (2013) Aging Cell , vol.12 , pp. 823-832
    • Pushkar, Y.1    Robison, G.2    Sullivan, B.3    Fu, S.X.4    Kohne, M.5    Jiang, W.6
  • 100
    • 0023022781 scopus 로고
    • Glucocorticoid regulation of metallothionein during murine development
    • Quaife, C., Hammer, R. E., Mottet, N. K., and Palmiter, R. D. (1986). Glucocorticoid regulation of metallothionein during murine development. Dev. Biol. 118, 549-555. doi: 10.1016/0012-1606(86)90025-4
    • (1986) Dev. Biol , vol.118 , pp. 549-555
    • Quaife, C.1    Hammer, R.E.2    Mottet, N.K.3    Palmiter, R.D.4
  • 101
    • 84924237720 scopus 로고    scopus 로고
    • 'Neurodegenerative aspects of multiple system atrophy,'
    • ed. R. M. Kostrzewa (New York, NY: Springer Science+Business Media)
    • Radford, R., Wong, M. B., and Pountney, D. L. (2014). "Neurodegenerative aspects of multiple system atrophy," in Handbook of Neurotoxicity, Vol. 110, ed R. M. Kostrzewa (New York, NY: Springer Science+Business Media), 2157-2180
    • (2014) Handbook of Neurotoxicity , vol.110 , pp. 2157-2180
    • Radford, R.1    Wong, M.B.2    Pountney, D.L.3
  • 103
    • 0021173920 scopus 로고
    • Structural and functional analysis of the human metallothionein-IA gene: differential induction by metal ions and glucocorticoids
    • Richards, R. I., Heguy, A., and Karin, M. (1984). Structural and functional analysis of the human metallothionein-IA gene: differential induction by metal ions and glucocorticoids. Cell 37, 263-272. doi: 10.1016/0092-8674(84)90322-2
    • (1984) Cell , vol.37 , pp. 263-272
    • Richards, R.I.1    Heguy, A.2    Karin, M.3
  • 104
    • 0026458199 scopus 로고
    • Changes in plasma zinc, copper, iron, and hepatic metallothionein in adjuvant-induced arthritis treated with cyclosporin
    • Rofe, A. M., Philcox, J. C., Haynes, D. R., Whitehouse, M. W., and Coyle, P. (1992). Changes in plasma zinc, copper, iron, and hepatic metallothionein in adjuvant-induced arthritis treated with cyclosporin. Biol. Trace Elem. Res. 34, 237-248. doi: 10.1007/BF02783679
    • (1992) Biol. Trace Elem. Res , vol.34 , pp. 237-248
    • Rofe, A.M.1    Philcox, J.C.2    Haynes, D.R.3    Whitehouse, M.W.4    Coyle, P.5
  • 105
    • 84860174383 scopus 로고    scopus 로고
    • Mechanism of copper(II)-induced misfolding of Parkinson's disease protein
    • Rose, F., Hodak, M., and Bernholc, J. (2011). Mechanism of copper(II)-induced misfolding of Parkinson's disease protein. Sci. Rep. 1:11. doi: 10.1038/srep00011
    • (2011) Sci. Rep , vol.1 , pp. 11
    • Rose, F.1    Hodak, M.2    Bernholc, J.3
  • 106
    • 0024331811 scopus 로고
    • Metal-specific posttranscriptional control of human metallothionein genes
    • Sadhu, C., and Gedamu, L. (1989). Metal-specific posttranscriptional control of human metallothionein genes. Mol. Cell. Biol. 9, 5738-5741. doi: 10.1128/MCB.9.12.5738
    • (1989) Mol. Cell. Biol , vol.9 , pp. 5738-5741
    • Sadhu, C.1    Gedamu, L.2
  • 107
    • 34249788738 scopus 로고    scopus 로고
    • Mitochondria, metabolic disturbances, oxidative stress and the kynurenine system, with focus on neurodegenerative disorders
    • Sas, K., Robotka, H., Toldi, J., and Vécsei, L. (2007). Mitochondria, metabolic disturbances, oxidative stress and the kynurenine system, with focus on neurodegenerative disorders. J. Neurol. Sci. 257, 221-239. doi: 10.1016/j.jns.2007.01.033
    • (2007) J. Neurol. Sci , vol.257 , pp. 221-239
    • Sas, K.1    Robotka, H.2    Toldi, J.3    Vécsei, L.4
  • 108
    • 12144290630 scopus 로고    scopus 로고
    • Proteasome mediates dopaminergic neuronal degeneration, and its inhibition causes a-synuclein inclusions
    • Sawada, H., Kohno, R., Kihara, T., Izumi, Y., Sakka, N., Ibi, M., et al. (2004). Proteasome mediates dopaminergic neuronal degeneration, and its inhibition causes a-synuclein inclusions. J. Biol. Chem. 279, 10710-10719. doi: 10.1074/jbc.M308434200
    • (2004) J. Biol. Chem , vol.279 , pp. 10710-10719
    • Sawada, H.1    Kohno, R.2    Kihara, T.3    Izumi, Y.4    Sakka, N.5    Ibi, M.6
  • 109
    • 84893088967 scopus 로고    scopus 로고
    • Significance of metallothioneins in aging brain
    • Sharma, S., and Ebadi, M. (2014a). Significance of metallothioneins in aging brain. Neurochem. Int. 65, 40-48. doi: 10.1016/j.neuint.2013.12.009
    • (2014) Neurochem. Int , vol.65 , pp. 40-48
    • Sharma, S.1    Ebadi, M.2
  • 110
    • 84908228095 scopus 로고    scopus 로고
    • The Charnoly body as a universal biomarker of cell injury
    • Sharma, S., and Ebadi, M. (2014b). The Charnoly body as a universal biomarker of cell injury. Biomarkers Genomic Med. 6, 89-98. doi: 10.1016/j.bgm.2014.03.004
    • (2014) Biomarkers Genomic Med , vol.6 , pp. 89-98
    • Sharma, S.1    Ebadi, M.2
  • 111
    • 84884883519 scopus 로고    scopus 로고
    • Biomarkers in Parkinson's disease (recent update)
    • Sharma, S., Moon, C. S., Khogali, A., Haidous, A., Chabenne, A., Ojo, C., et al. (2013a). Biomarkers in Parkinson's disease (recent update). Neurochem. Int. 63, 201-229. doi: 10.1016/j.neuint.2013.06.005
    • (2013) Neurochem. Int , vol.63 , pp. 201-229
    • Sharma, S.1    Moon, C.S.2    Khogali, A.3    Haidous, A.4    Chabenne, A.5    Ojo, C.6
  • 112
    • 84876495193 scopus 로고    scopus 로고
    • Clinical significance of metallothioneins in cell therapy and nanomedicine
    • Sharma, S., Rais, A., Sandhu, R., Nel, W., and Ebadi, P. M. (2013b). Clinical significance of metallothioneins in cell therapy and nanomedicine. Int. J. Nanomed. 8, 1477-1488. doi: 10.2147/IJN.S42019
    • (2013) Int. J. Nanomed , vol.8 , pp. 1477-1488
    • Sharma, S.1    Rais, A.2    Sandhu, R.3    Nel, W.4    Ebadi, P.M.5
  • 113
    • 84880174102 scopus 로고    scopus 로고
    • Innate immunity and neuroinflammation
    • Shastri, A., Bonifati, D. M., and Kishore, U. (2013). Innate immunity and neuroinflammation. Mediators Inflamm. 2013:342931. doi: 10.1155/2013/342931
    • (2013) Mediators Inflamm , vol.2013
    • Shastri, A.1    Bonifati, D.M.2    Kishore, U.3
  • 114
    • 70349798566 scopus 로고    scopus 로고
    • Snapshot: pathogenesis of Parkinson's Disease
    • Shin, J. H., Dawson, V. L., and Dawson, T. M. (2009). Snapshot: pathogenesis of Parkinson's Disease. Cell 139, 440.e1-440.e2. doi: 10.1016/j.cell.2009.09.026
    • (2009) Cell , vol.139
    • Shin, J.H.1    Dawson, V.L.2    Dawson, T.M.3
  • 115
    • 0027428818 scopus 로고
    • The effects of 6-hydroxydopamine and oxidative stress on the level of brain metallothionein
    • Shiraga, H., Pfeiffer, R. F., and Ebadi, M. (1993). The effects of 6-hydroxydopamine and oxidative stress on the level of brain metallothionein. Neurochem. Int. 23, 561-566. doi: 10.1016/0197-0186(93)90104-D
    • (1993) Neurochem. Int , vol.23 , pp. 561-566
    • Shiraga, H.1    Pfeiffer, R.F.2    Ebadi, M.3
  • 116
    • 84968756394 scopus 로고    scopus 로고
    • Detrimental effects of oxidative losses in parkin activity in a model of sporadic Parkinson's disease are attenuated by restoration of PGC1alpha
    • Siddiqui, A., Rane, A., Rajagopalan, S., Chinta, S. J., and Andersen, J. K. (2016). Detrimental effects of oxidative losses in parkin activity in a model of sporadic Parkinson's disease are attenuated by restoration of PGC1alpha. Neurobiol. Dis. 93, 115-120. doi: 10.1016/j.nbd.2016.05.009
    • (2016) Neurobiol. Dis , vol.93 , pp. 115-120
    • Siddiqui, A.1    Rane, A.2    Rajagopalan, S.3    Chinta, S.J.4    Andersen, J.K.5
  • 117
    • 1842454976 scopus 로고    scopus 로고
    • Does alpha-synuclein modulate dopaminergic synaptic content and tone at the synapse?
    • Sidhu, A., Wersinger, C., and Vernier, P. (2004). Does alpha-synuclein modulate dopaminergic synaptic content and tone at the synapse? FASEB J. 18, 637-647. doi: 10.1096/fj.03-1112rev
    • (2004) FASEB J , vol.18 , pp. 637-647
    • Sidhu, A.1    Wersinger, C.2    Vernier, P.3
  • 118
    • 0034531475 scopus 로고    scopus 로고
    • The alpha-synucleinopathies: Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy
    • Spillantini, M. G., and Goedert, M. (2000). The alpha-synucleinopathies: Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. Ann. N. Y. Acad. Sci. 920, 16-27. doi: 10.1111/j.1749-6632.2000.tb06900.x
    • (2000) Ann. N. Y. Acad. Sci , vol.920 , pp. 16-27
    • Spillantini, M.G.1    Goedert, M.2
  • 119
    • 84988328409 scopus 로고    scopus 로고
    • Non-ceruloplasmin bound copper and ATP7B gene variants in Alzheimer's disease
    • Squitti, R., Siotto, M., Arciello, M., and Rossi, L. (2016). Non-ceruloplasmin bound copper and ATP7B gene variants in Alzheimer's disease. Metallomics 8, 863-873. doi: 10.1039/c6mt00101g
    • (2016) Metallomics , vol.8 , pp. 863-873
    • Squitti, R.1    Siotto, M.2    Arciello, M.3    Rossi, L.4
  • 120
    • 84866702836 scopus 로고    scopus 로고
    • a-Synuclein in Parkinson's disease
    • Stefanis, L. L. (2012). a-Synuclein in Parkinson's disease. Cold Spring Harb. Perspect. Med. 2:9399. doi: 10.1101/cshperspect.a009399
    • (2012) Cold Spring Harb. Perspect. Med , vol.2 , pp. 9399
    • Stefanis, L.L.1
  • 121
    • 4243094853 scopus 로고    scopus 로고
    • Long term motor complications of levodpa: clinical features, mechanisms, and management strategies
    • Thanvi, B. R., and Lo, T. C. (2004). Long term motor complications of levodpa: clinical features, mechanisms, and management strategies. Postgrad. Med. J. 80, 452-458. doi: 10.1136/pgmj.2003.013912
    • (2004) Postgrad. Med. J , vol.80 , pp. 452-458
    • Thanvi, B.R.1    Lo, T.C.2
  • 122
    • 84939943500 scopus 로고    scopus 로고
    • Regulation of intracellular copper by induction of endogenous metallothioneins improves the disease course in a mouse model of amyotrophic lateral sclerosis
    • Tokuda, E., Watanabe, S., Okawa, E., and Ono, S. I. (2015). Regulation of intracellular copper by induction of endogenous metallothioneins improves the disease course in a mouse model of amyotrophic lateral sclerosis. Neurotherapeutics 12, 461-476. doi: 10.1007/s13311-015-0346-x
    • (2015) Neurotherapeutics , vol.12 , pp. 461-476
    • Tokuda, E.1    Watanabe, S.2    Okawa, E.3    Ono, S.I.4
  • 123
    • 77954685035 scopus 로고    scopus 로고
    • Molecular mechanisms of regeneration in Alzheimer's disease brain
    • Uchida, Y. (2010). Molecular mechanisms of regeneration in Alzheimer's disease brain. Geriatr. Gerontol. Int. 10(Suppl. 1), S158-S168. doi: 10.1111/j.1447-0594.2010.00607.x
    • (2010) Geriatr. Gerontol. Int , vol.10 , pp. S158-S168
    • Uchida, Y.1
  • 125
    • 84964636321 scopus 로고    scopus 로고
    • Coordination and redox properties of copper interaction with a-synuclein
    • Valensin, D., Dell'Acqua, S., Kozlowski, H., and Casella, L. (2016). Coordination and redox properties of copper interaction with a-synuclein. J. Inorg. Biochem. 163, 292-300. doi: 10.1016/j.jinorgbio.2016.04.012
    • (2016) J. Inorg. Biochem , vol.163 , pp. 292-300
    • Valensin, D.1    Dell'Acqua, S.2    Kozlowski, H.3    Casella, L.4
  • 127
    • 77954511375 scopus 로고    scopus 로고
    • New evidence on iron, copper accumulation and zinc depletion and its correlation with DNA integrity in aging human brain regions
    • Vasudevaraju, P., Jyothsna, T., Shamasundar, N. M., Rao, S. K., Balaraj, B. M., Rao, K. S. J., et al. (2010). New evidence on iron, copper accumulation and zinc depletion and its correlation with DNA integrity in aging human brain regions. Indian J. Psychiatry 52, 140. doi: 10.4103/0019-5545.64590
    • (2010) Indian J. Psychiatry , vol.52 , pp. 140
    • Vasudevaraju, P.1    Jyothsna, T.2    Shamasundar, N.M.3    Rao, S.K.4    Balaraj, B.M.5    Rao, K.S.J.6
  • 130
    • 84947587748 scopus 로고    scopus 로고
    • Neuroinflammation in multiple system atrophy: response to and cause of a-synuclein aggregation
    • Vieira, B. D., Radford, R. A., Chung, R. S., Guillemin, G. J., and Pountney, D. L. (2015). Neuroinflammation in multiple system atrophy: response to and cause of a-synuclein aggregation. Front. Cell. Neurosci. 9:437. doi: 10.3389/fncel.2015.00437
    • (2015) Front. Cell. Neurosci , vol.9 , pp. 437
    • Vieira, B.D.1    Radford, R.A.2    Chung, R.S.3    Guillemin, G.J.4    Pountney, D.L.5
  • 131
    • 68949170348 scopus 로고    scopus 로고
    • Metalloproteins and metal sensing
    • 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
  • 132
    • 84862188904 scopus 로고    scopus 로고
    • The role of alpha-synuclein oligomerization and aggregation in cellular and animal models of Parkinson's disease
    • Wan, O. W., and Chung, K. K. (2012). The role of alpha-synuclein oligomerization and aggregation in cellular and animal models of Parkinson's disease. PLoS ONE 7:e38545. doi: 10.1371/journal.pone.0038545
    • (2012) PLoS ONE , vol.7
    • Wan, O.W.1    Chung, K.K.2
  • 133
    • 44649152946 scopus 로고    scopus 로고
    • Metallothionein in the central nervous system: roles in protection, regeneration and cognition
    • West, A. K., Hidalgo, J., Eddins, D., Levin, E. D., and Aschner, M. (2008). Metallothionein in the central nervous system: roles in protection, regeneration and cognition. Neurotoxicology 29, 489-503. doi: 10.1016/j.neuro.2007.12.006
    • (2008) Neurotoxicology , vol.29 , pp. 489-503
    • West, A.K.1    Hidalgo, J.2    Eddins, D.3    Levin, E.D.4    Aschner, M.5
  • 134
    • 0025222043 scopus 로고
    • Human metallothionein genes: structure of the functional locus at 16q13
    • West, A. K., Stallings, R., Hildebrand, C. E., Chiu, R., Karin, M., and Richards, R. I. (1990). Human metallothionein genes: structure of the functional locus at 16q13. Genomics 8, 513-518. doi: 10.1016/0888-7543(90)90038-v
    • (1990) Genomics , vol.8 , pp. 513-518
    • West, A.K.1    Stallings, R.2    Hildebrand, C.E.3    Chiu, R.4    Karin, M.5    Richards, R.I.6
  • 135
    • 79959728747 scopus 로고    scopus 로고
    • Epidemiology and etiology of Parkinson's disease: a review of the evidence
    • Wirdefeldt, K., Adami, H., Cole, P., Trichopoulos, D., and Mandel, J. (2011). Epidemiology and etiology of Parkinson's disease: a review of the evidence. Eur. J. Epidemiol. 26:1. doi: 10.1007/s10654-011-9581-6
    • (2011) Eur. J. Epidemiol , vol.26 , pp. 1
    • Wirdefeldt, K.1    Adami, H.2    Cole, P.3    Trichopoulos, D.4    Mandel, J.5
  • 136
    • 85011818934 scopus 로고    scopus 로고
    • a-synuclein toxicity in neurodegeneration: mechanism and therapeutic strategies
    • Wong, Y. C., and Krainc, D. (2017). a-synuclein toxicity in neurodegeneration: mechanism and therapeutic strategies. Nat. Med. 23, 1-13. doi: 10.1038/nm.4269
    • (2017) Nat. Med , vol.23 , pp. 1-13
    • Wong, Y.C.1    Krainc, D.2
  • 137
    • 80052961534 scopus 로고    scopus 로고
    • Neurodegenerative disease: a-synuclein gets a new look
    • Yates, D. (2011). Neurodegenerative disease: a-synuclein gets a new look. Nat. Rev. Neurosci. 12, 550. doi: 10.1038/nrn3106
    • (2011) Nat. Rev. Neurosci , vol.12 , pp. 550
    • Yates, D.1
  • 138
    • 10944243102 scopus 로고    scopus 로고
    • Role of a-synuclein in presynaptic dopamine recruitment
    • Yavich, L., Tanila, H., Vepsäläinen, S., and Jäkälä, P. (2004). Role of a-synuclein in presynaptic dopamine recruitment. J. Neurosci. 24, 11165-11170. doi: 10.1523/JNEUROSCI.2559-04.2004
    • (2004) J. Neurosci , vol.24 , pp. 11165-11170
    • Yavich, L.1    Tanila, H.2    Vepsäläinen, S.3    Jäkälä, P.4
  • 139
    • 46749123426 scopus 로고    scopus 로고
    • Accumulation of copper and other metal ions, and metallothionein I/II expression in the bovine brain as a function of aging
    • Zatta, P., Drago, D., Zambenedetti, P., Bolognin, S., Nogara, E., Peruffo, A., et al. (2008). Accumulation of copper and other metal ions, and metallothionein I/II expression in the bovine brain as a function of aging. J. Chem. Neuroanat. 36, 1-5. doi: 10.1016/j.jchemneu.2008.02.008
    • (2008) J. Chem. Neuroanat , vol.36 , pp. 1-5
    • Zatta, P.1    Drago, D.2    Zambenedetti, P.3    Bolognin, S.4    Nogara, E.5    Peruffo, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.