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Volumn 72, Issue , 2014, Pages 176-190

Hsp27 suppresses the Cu2+-induced amyloidogenicity, redox activity, and cytotoxicity of α-synuclein by metal ion stripping

Author keywords

Amyloid fibril; Free radicals; Hsp27; Reactive oxygen species; Synuclein

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; AMYLOID BETA PROTEIN[1-40]; AMYLOID PROTEIN; ASCORBIC ACID; CUPRIC ION; HEAT SHOCK PROTEIN 27; REACTIVE OXYGEN METABOLITE; SUPEROXIDE; AMYLOID BETA PROTEIN; COPPER;

EID: 84900499674     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2014.04.012     Document Type: Article
Times cited : (18)

References (64)
  • 1
    • 33745726690 scopus 로고    scopus 로고
    • Copper homeostasis and neurodegenerative disorders (Alzheimer's, prion, and Parkinson's diseases and amyotrophic lateral sclerosis)
    • E. Gaggelli, H. Kozlowski, D. Valensin, and G. Valensin Copper homeostasis and neurodegenerative disorders (Alzheimer's, prion, and Parkinson's diseases and amyotrophic lateral sclerosis) Chem. Rev. 106 2006 1995 2044
    • (2006) Chem. Rev. , vol.106 , pp. 1995-2044
    • Gaggelli, E.1    Kozlowski, H.2    Valensin, D.3    Valensin, G.4
  • 4
    • 0035872487 scopus 로고    scopus 로고
    • Copper in disorders with neurological symptoms: Alzheimer's, Menkes, and Wilson diseases
    • D. Strausak, J.F. Mercer, H.H. Dieter, W. Stremmel, and G. Multhaup Copper in disorders with neurological symptoms: Alzheimer's, Menkes, and Wilson diseases Brain Res. Bull. 55 2001 175 185
    • (2001) Brain Res. Bull. , vol.55 , pp. 175-185
    • Strausak, D.1    Mercer, J.F.2    Dieter, H.H.3    Stremmel, W.4    Multhaup, G.5
  • 5
    • 34447103789 scopus 로고    scopus 로고
    • Trafficking of the copper-ATPases, ATP7A and ATP7B: Role in copper homeostasis
    • F.S. La, and J.F. Mercer Trafficking of the copper-ATPases, ATP7A and ATP7B: role in copper homeostasis Arch. Biochem. Biophys. 463 2007 149 167
    • (2007) Arch. Biochem. Biophys. , vol.463 , pp. 149-167
    • La, F.S.1    Mercer, J.F.2
  • 7
    • 29044438902 scopus 로고    scopus 로고
    • The crucial role of metal ions in neurodegeneration: The basis for a promising therapeutic strategy
    • A. Gaeta, and R.C. Hider The crucial role of metal ions in neurodegeneration: the basis for a promising therapeutic strategy Br. J. Pharmacol. 146 2005 1041 1059
    • (2005) Br. J. Pharmacol. , vol.146 , pp. 1041-1059
    • Gaeta, A.1    Hider, R.C.2
  • 8
    • 0034035616 scopus 로고    scopus 로고
    • Metals and neuroscience
    • A.I. Bush Metals and neuroscience Curr. Opin. Chem. Biol. 4 2000 184 191
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 184-191
    • Bush, A.I.1
  • 9
    • 51749108879 scopus 로고    scopus 로고
    • Role of copper in human neurological disorders
    • V. Desai, and S.G. Kaler Role of copper in human neurological disorders Am. J. Clin. Nutr. 88 2008 855S 858S
    • (2008) Am. J. Clin. Nutr. , vol.88
    • Desai, V.1    Kaler, S.G.2
  • 11
    • 2942729775 scopus 로고    scopus 로고
    • Metals in our minds: Therapeutic implications for neurodegenerative disorders
    • P.M. Doraiswamy, and A.E. Finefrock Metals in our minds: therapeutic implications for neurodegenerative disorders Lancet Neurol. 3 2004 431 434
    • (2004) Lancet Neurol. , vol.3 , pp. 431-434
    • Doraiswamy, P.M.1    Finefrock, A.E.2
  • 14
    • 79952117485 scopus 로고    scopus 로고
    • Metal emissions and urban incident Parkinson disease: A community health study of Medicare beneficiaries by using geographic information systems
    • A.W. Willis, B.A. Evanoff, M. Lian, A. Galarza, A. Wegrzyn, M. Schootman, and B.A. Racette Metal emissions and urban incident Parkinson disease: a community health study of Medicare beneficiaries by using geographic information systems Am. J. Epidemiol. 172 2010 1357 1363
    • (2010) Am. J. Epidemiol. , vol.172 , pp. 1357-1363
    • Willis, A.W.1    Evanoff, B.A.2    Lian, M.3    Galarza, A.4    Wegrzyn, A.5    Schootman, M.6    Racette, B.A.7
  • 17
    • 0037308515 scopus 로고    scopus 로고
    • Activation of metallothioneins and alpha-crystallin/sHSPs in human lens epithelial cells by specific metals and the metal content of aging clear human lenses
    • J.R. Hawse, J.R. Cumming, B. Oppermann, N.L. Sheets, V.N. Reddy, and M. Kantorow Activation of metallothioneins and alpha-crystallin/sHSPs in human lens epithelial cells by specific metals and the metal content of aging clear human lenses Invest. Ophthalmol. Visual Sci. 44 2003 672 679
    • (2003) Invest. Ophthalmol. Visual Sci. , vol.44 , pp. 672-679
    • Hawse, J.R.1    Cumming, J.R.2    Oppermann, B.3    Sheets, N.L.4    Reddy, V.N.5    Kantorow, M.6
  • 19
    • 0029004307 scopus 로고
    • Induction of the synthesis of hsp27 and alpha B crystallin in tissues of heat-stressed rats and its suppression by ethanol or an alpha 1-adrenergic antagonist
    • Y. Inaguma, K. Hasegawa, S. Goto, H. Ito, and K. Kato Induction of the synthesis of hsp27 and alpha B crystallin in tissues of heat-stressed rats and its suppression by ethanol or an alpha 1-adrenergic antagonist J. Biochem. 117 1995 1238 1243
    • (1995) J. Biochem. , vol.117 , pp. 1238-1243
    • Inaguma, Y.1    Hasegawa, K.2    Goto, S.3    Ito, H.4    Kato, K.5
  • 20
    • 0034960562 scopus 로고    scopus 로고
    • Regulation of the levels of small heat-shock proteins during differentiation of C2C12 cells
    • H. Ito, K. Kamei, I. Iwamoto, Y. Inaguma, and K. Kato Regulation of the levels of small heat-shock proteins during differentiation of C2C12 cells Exp. Cell Res. 266 2001 213 221
    • (2001) Exp. Cell Res. , vol.266 , pp. 213-221
    • Ito, H.1    Kamei, K.2    Iwamoto, I.3    Inaguma, Y.4    Kato, K.5
  • 21
    • 0033796051 scopus 로고    scopus 로고
    • Inhibition of Daxx-mediated apoptosis by heat shock protein 27
    • S.J. Charette, J.N. Lavoie, H. Lambert, and J. Landry Inhibition of Daxx-mediated apoptosis by heat shock protein 27 Mol. Cell. Biol. 20 2000 7602 7612
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7602-7612
    • Charette, S.J.1    Lavoie, J.N.2    Lambert, H.3    Landry, J.4
  • 22
    • 0031454881 scopus 로고    scopus 로고
    • Hsp27 as a switch between differentiation and apoptosis in murine embryonic stem cells
    • P. Mehlen, A. Mehlen, J. Godet, and A.P. Arrigo Hsp27 as a switch between differentiation and apoptosis in murine embryonic stem cells J. Biol. Chem. 272 1997 31657 31665
    • (1997) J. Biol. Chem. , vol.272 , pp. 31657-31665
    • Mehlen, P.1    Mehlen, A.2    Godet, J.3    Arrigo, A.P.4
  • 24
    • 0007404243 scopus 로고    scopus 로고
    • Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFα in NIH-3T3-ras cells
    • P. Mehlen, E. Hickey, L.A. Weber, and A.P. Arrigo Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFα in NIH-3T3-ras cells Biochem. Biophys. Res. Commun. 241 1997 187 192
    • (1997) Biochem. Biophys. Res. Commun. , vol.241 , pp. 187-192
    • Mehlen, P.1    Hickey, E.2    Weber, L.A.3    Arrigo, A.P.4
  • 25
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • P.J. Muchowski, and J.L. Wacker Modulation of neurodegeneration by molecular chaperones Nat. Rev. Neurosci. 6 2005 11 22
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 27
    • 39149131353 scopus 로고    scopus 로고
    • Infection of metallothionein 1+2 knockout mice with Rocky Mountain Laboratory scrapie
    • E. Vidal, R. Tortosa, M. Marquez, A. Serafin, J. Hidalgo, and M. Pumarola Infection of metallothionein 1+2 knockout mice with Rocky Mountain Laboratory scrapie Brain Res. 1196 2008 140 150
    • (2008) Brain Res. , vol.1196 , pp. 140-150
    • Vidal, E.1    Tortosa, R.2    Marquez, M.3    Serafin, A.4    Hidalgo, J.5    Pumarola, M.6
  • 28
    • 33847421747 scopus 로고    scopus 로고
    • 2+ and acute thermal stress induce protective events via the p38-MAPK signalling pathway in the perfused Rana ridibunda heart
    • 2+ and acute thermal stress induce protective events via the p38-MAPK signalling pathway in the perfused Rana ridibunda heart J. Exp. Biol. 210 2007 438 446
    • (2007) J. Exp. Biol. , vol.210 , pp. 438-446
    • Gaitanaki, C.1    Pliatska, M.2    Stathopoulou, K.3    Beis, I.4
  • 29
    • 33751115774 scopus 로고    scopus 로고
    • Fibrillogenic and non-fibrillogenic ensembles of SDS-bound human alpha-synuclein
    • M.F. Ahmad, T. Ramakrishna, B. Raman, and C. Rao Fibrillogenic and non-fibrillogenic ensembles of SDS-bound human alpha-synuclein J. Mol. Biol. 364 2006 1061 1072
    • (2006) J. Mol. Biol. , vol.364 , pp. 1061-1072
    • Ahmad, M.F.1    Ramakrishna, T.2    Raman, B.3    Rao, C.4
  • 31
    • 18144374793 scopus 로고    scopus 로고
    • Metal ion-dependent effects of clioquinol on the fibril growth of an amyloid {beta} peptide
    • B. Raman, T. Ban, K. Yamaguchi, M. Sakai, T. Kawai, H. Naiki, and Y. Goto Metal ion-dependent effects of clioquinol on the fibril growth of an amyloid {beta} peptide J. Biol. Chem. 280 2005 16157 16162
    • (2005) J. Biol. Chem. , vol.280 , pp. 16157-16162
    • Raman, B.1    Ban, T.2    Yamaguchi, K.3    Sakai, M.4    Kawai, T.5    Naiki, H.6    Goto, Y.7
  • 32
    • 30044443305 scopus 로고    scopus 로고
    • High affinity binding between copper and full-length prion protein identified by two different techniques
    • A.R. Thompsett, S.R. Abdelraheim, M. Daniels, and D.R. Brown High affinity binding between copper and full-length prion protein identified by two different techniques J. Biol. Chem. 280 2005 42750 42758
    • (2005) J. Biol. Chem. , vol.280 , pp. 42750-42758
    • Thompsett, A.R.1    Abdelraheim, S.R.2    Daniels, M.3    Brown, D.R.4
  • 33
    • 72049122126 scopus 로고    scopus 로고
    • A spectrophotometric method for the determination of zinc, copper, and cobalt ions in metalloproteins using Zincon
    • C.E. Sabel, J.M. Neureuther, and S. Siemann A spectrophotometric method for the determination of zinc, copper, and cobalt ions in metalloproteins using Zincon Anal. Biochem. 397 2010 218 226
    • (2010) Anal. Biochem. , vol.397 , pp. 218-226
    • Sabel, C.E.1    Neureuther, J.M.2    Siemann, S.3
  • 34
    • 0014190736 scopus 로고
    • Metal ion and metal chelate catalyzed oxidation of ascorbic acid by molecular oxygen. I. Cupric and ferric ion catalyzed oxidation
    • M.M. Khan, and A.E. Martell Metal ion and metal chelate catalyzed oxidation of ascorbic acid by molecular oxygen. I. Cupric and ferric ion catalyzed oxidation J. Am. Chem. Soc. 89 1967 4176 4185
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 4176-4185
    • Khan, M.M.1    Martell, A.E.2
  • 35
    • 0030680226 scopus 로고    scopus 로고
    • Coumarin-3-carboxylic acid as a detector for hydroxyl radicals generated chemically and by gamma radiation
    • Y. Manevich, K.D. Held, and J.E. Biaglow Coumarin-3-carboxylic acid as a detector for hydroxyl radicals generated chemically and by gamma radiation Radiat. Res. 148 1997 580 591
    • (1997) Radiat. Res. , vol.148 , pp. 580-591
    • Manevich, Y.1    Held, K.D.2    Biaglow, J.E.3
  • 37
    • 0242362596 scopus 로고    scopus 로고
    • Beta-amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH
    • G.M. Klug, D. Losic, S.S. Subasinghe, M.I. Aguilar, L.L. Martin, and D.H. Small Beta-amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH Eur. J. Biochem. 270 2003 4282 4293
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4282-4293
    • Klug, G.M.1    Losic, D.2    Subasinghe, S.S.3    Aguilar, M.I.4    Martin, L.L.5    Small, D.H.6
  • 38
    • 84873355284 scopus 로고    scopus 로고
    • Cu(II) affinity for the Alzheimer's peptide: Tyrosine fluorescence studies revisited
    • B. Alies, E. Renaglia, M. RoÍzga, W. Bal, P. Faller, and C Hureau Cu(II) affinity for the Alzheimer's peptide: tyrosine fluorescence studies revisited Anal. Chem 8 2013 1501 1508
    • (2013) Anal. Chem , vol.8 , pp. 1501-1508
    • Alies, B.1    Renaglia, E.2    Roízga, M.3    Bal, W.4    Faller, P.5    Hureau, C.6
  • 40
    • 0024509805 scopus 로고
    • Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1
    • H. Naiki, K. Higuchi, M. Hosokawa, and T. Takeda Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1 Anal. Biochem. 177 1989 244 249
    • (1989) Anal. Biochem. , vol.177 , pp. 244-249
    • Naiki, H.1    Higuchi, K.2    Hosokawa, M.3    Takeda, T.4
  • 42
    • 0343131929 scopus 로고    scopus 로고
    • Differential compartmentalization of brain ascorbate and glutathione between neurons and glia
    • M.E. Rice, and I. Russo-Menna Differential compartmentalization of brain ascorbate and glutathione between neurons and glia Neuroscience 82 1998 1213 1223
    • (1998) Neuroscience , vol.82 , pp. 1213-1223
    • Rice, M.E.1    Russo-Menna, I.2
  • 43
    • 77956216847 scopus 로고    scopus 로고
    • Mitochondrial and cell death mechanisms in neurodegenerative diseases
    • L.J. Martin Mitochondrial and cell death mechanisms in neurodegenerative diseases Pharmaceuticals (Basel) 3 2010 839 915
    • (2010) Pharmaceuticals (Basel) , vol.3 , pp. 839-915
    • Martin, L.J.1
  • 44
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • U. Jakob, M. Gaestel, K. Engel, and J. Buchner Small heat shock proteins are molecular chaperones J. Biol. Chem. 268 1993 1517 1520
    • (1993) J. Biol. Chem. , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 46
    • 33845913216 scopus 로고    scopus 로고
    • Intracellular and extracellular functions of heat shock proteins: Repercussions in cancer therapy
    • E. Schmitt, M. Gehrmann, M. Brunet, G. Multhoff, and C. Garrido Intracellular and extracellular functions of heat shock proteins: repercussions in cancer therapy J. Leukocyte Biol. 81 2007 15 27
    • (2007) J. Leukocyte Biol. , vol.81 , pp. 15-27
    • Schmitt, E.1    Gehrmann, M.2    Brunet, M.3    Multhoff, G.4    Garrido, C.5
  • 47
    • 33646857038 scopus 로고    scopus 로고
    • Small heat shock proteins inhibit amyloid-beta protein aggregation and cerebrovascular amyloid-beta protein toxicity
    • M.M. Wilhelmus, W.C. Boelens, I. Otte-Holler, B. Kamps, R.M. de Waal, and M.M. Verbeek Small heat shock proteins inhibit amyloid-beta protein aggregation and cerebrovascular amyloid-beta protein toxicity Brain Res. 1089 2006 67 78
    • (2006) Brain Res. , vol.1089 , pp. 67-78
    • Wilhelmus, M.M.1    Boelens, W.C.2    Otte-Holler, I.3    Kamps, B.4    De Waal, R.M.5    Verbeek, M.M.6
  • 51
    • 79959362400 scopus 로고
    • AlphaB-crystallin, a small heat shock protein, modulates NF-kappaB activity in a phosphorylation-dependent manner and protects muscle myoblasts from TNF-alpha induced cytotoxicity
    • A.S. Adhikari, B.N. Singh, K.S. Rao, and C. Rao AlphaB-crystallin, a small heat shock protein, modulates NF-kappaB activity in a phosphorylation- dependent manner and protects muscle myoblasts from TNF-alpha induced cytotoxicity Biochim. Biophys. Acta 1532-1542 1813 2011
    • (1813) Biochim. Biophys. Acta , vol.1532-1542 , pp. 2011
    • Adhikari, A.S.1    Singh, B.N.2    Rao, K.S.3    Rao, C.4
  • 52
    • 78650761784 scopus 로고    scopus 로고
    • Compact conformations of alpha-synuclein induced by alcohols and copper
    • A. Natalello, F. Benetti, S.M. Doglia, G. Legname, and R. Grandori Compact conformations of alpha-synuclein induced by alcohols and copper Proteins 79 2011 611 621
    • (2011) Proteins , vol.79 , pp. 611-621
    • Natalello, A.1    Benetti, F.2    Doglia, S.M.3    Legname, G.4    Grandori, R.5
  • 53
    • 68849102707 scopus 로고    scopus 로고
    • Unique copper-induced oligomers mediate alpha-synuclein toxicity
    • J.A. Wright, X. Wang, and D.R. Brown Unique copper-induced oligomers mediate alpha-synuclein toxicity FASEB J 23 2009 2384 2393
    • (2009) FASEB J , vol.23 , pp. 2384-2393
    • Wright, J.A.1    Wang, X.2    Brown, D.R.3
  • 55
    • 84856293829 scopus 로고    scopus 로고
    • The molecular pathology of Alzheimer's disease
    • C.R. Harrington The molecular pathology of Alzheimer's disease Neuroimaging Clin. North Am 22 2012 11 22
    • (2012) Neuroimaging Clin. North Am , vol.22 , pp. 11-22
    • Harrington, C.R.1
  • 56
    • 0141613892 scopus 로고    scopus 로고
    • Clinical overview of the synucleinopathies
    • M.J. Marti, E. Tolosa, and J. Campdelacreu Clinical overview of the synucleinopathies Mov. Disord 18 Suppl. 6 2003 S21 S27
    • (2003) Mov. Disord , vol.18 , Issue.SUPPL. 6
    • Marti, M.J.1    Tolosa, E.2    Campdelacreu, J.3
  • 57
    • 84886877884 scopus 로고    scopus 로고
    • Impaired glutathione synthesis in neurodegeneration
    • K. Aoyama, and T. Nakaki Impaired glutathione synthesis in neurodegeneration Int. J. Mol. Sci 14 2013 21021 21044
    • (2013) Int. J. Mol. Sci , vol.14 , pp. 21021-21044
    • Aoyama, K.1    Nakaki, T.2
  • 58
    • 50149109874 scopus 로고    scopus 로고
    • 2+ binding, redox silencing, and cytoprotective effects of the small heat shock proteins alphaA- and alphaB-crystallin
    • 2+ binding, redox silencing, and cytoprotective effects of the small heat shock proteins alphaA- and alphaB-crystallin J. Mol. Biol. 382 2008 812 824
    • (2008) J. Mol. Biol. , vol.382 , pp. 812-824
    • Ahmad, M.F.1    Singh, D.2    Taiyab, A.3    Ramakrishna, T.4    Raman, B.5    Rao, C.6
  • 59
    • 79960023569 scopus 로고    scopus 로고
    • 2+-mediated generation of reactive oxygen species by the small heat shock protein αb-crystallin: The relative contributions of the N- and C-terminal domains
    • 2+-mediated generation of reactive oxygen species by the small heat shock protein αB-crystallin: the relative contributions of the N- and C-terminal domains Free Radic. Biol. Med. 51 2011 755 762
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 755-762
    • Prabhu, S.1    Srinivas, V.2    Ramakrishna, T.3    Raman, B.4    Rao, C.5
  • 60
    • 84855478926 scopus 로고    scopus 로고
    • Structural and mechanistic implications of metal binding in the small heat-shock protein alphaB-crystallin
    • A. Mainz, B. Bardiaux, F. Kuppler, G. Multhaup, I.C. Felli, R. Pierattelli, and B. Reif Structural and mechanistic implications of metal binding in the small heat-shock protein alphaB-crystallin J. Biol. Chem. 287 2012 1128 1138
    • (2012) J. Biol. Chem. , vol.287 , pp. 1128-1138
    • Mainz, A.1    Bardiaux, B.2    Kuppler, F.3    Multhaup, G.4    Felli, I.C.5    Pierattelli, R.6    Reif, B.7
  • 61
    • 79955471279 scopus 로고    scopus 로고
    • Identification and characterization of a copper-binding site in αa-crystallin
    • M. Raju, P. Santhoshkumar, T.M. Henzl, and K.K. Sharma Identification and characterization of a copper-binding site in αA-crystallin Free Radic. Biol. Med. 50 2011 1429 1436
    • (2011) Free Radic. Biol. Med. , vol.50 , pp. 1429-1436
    • Raju, M.1    Santhoshkumar, P.2    Henzl, T.M.3    Sharma, K.K.4
  • 62
    • 17644383748 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar species
    • M.M. Dedmon, J. Christodoulou, M.R. Wilson, and C.M. Dobson Heat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar species J. Biol. Chem. 280 2005 14733 14740
    • (2005) J. Biol. Chem. , vol.280 , pp. 14733-14740
    • Dedmon, M.M.1    Christodoulou, J.2    Wilson, M.R.3    Dobson, C.M.4
  • 63
    • 73949105506 scopus 로고    scopus 로고
    • Heat shock protein 27 protects against atherogenesis via an estrogen-dependent mechanism: Role of selective estrogen receptor beta modulation
    • K. Rayner, J. Sun, Y.X. Chen, M. McNulty, T. Simard, X. Zhao, D.J. Wells, B.J. de, and E.R. O'Brien Heat shock protein 27 protects against atherogenesis via an estrogen-dependent mechanism: role of selective estrogen receptor beta modulation Arterioscler. Thromb. Vasc. Biol. 29 2009 1751 1756
    • (2009) Arterioscler. Thromb. Vasc. Biol. , vol.29 , pp. 1751-1756
    • Rayner, K.1    Sun, J.2    Chen, Y.X.3    McNulty, M.4    Simard, T.5    Zhao, X.6    Wells, D.J.7    De, B.J.8    O'Brien, E.R.9
  • 64
    • 33748750998 scopus 로고    scopus 로고
    • Dual effects of antioxidants in neurodegeneration: Direct neuroprotection against oxidative stress and indirect protection via suppression of glia-mediated inflammation
    • J.Y. Wang, L.L. Wen, Y.N. Huang, Y.T. Chen, and M.C. Ku Dual effects of antioxidants in neurodegeneration: direct neuroprotection against oxidative stress and indirect protection via suppression of glia-mediated inflammation Curr. Pharm. Des 12 2006 3521 3533
    • (2006) Curr. Pharm. des , vol.12 , pp. 3521-3533
    • Wang, J.Y.1    Wen, L.L.2    Huang, Y.N.3    Chen, Y.T.4    Ku, M.C.5


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