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Volumn 314, Issue 10, 2008, Pages 2076-2089

Mitochondrial translocation of α-synuclein is promoted by intracellular acidification

Author keywords

Metabolic dysfunction; Mitochondria; Oxidative stress; Parkinson's disease; pH; Synuclein

Indexed keywords

ALPHA SYNUCLEIN; CARDIOLIPIN;

EID: 44749085250     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2008.03.012     Document Type: Article
Times cited : (162)

References (70)
  • 1
    • 33644543761 scopus 로고    scopus 로고
    • Expanding insights of mitochondrial dysfunction in Parkinson's disease
    • Abou-Sleiman P.M., Muqit M.M., and Wood N.W. Expanding insights of mitochondrial dysfunction in Parkinson's disease. Nat. Rev. Neurosci. 7 (2006) 207-219
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 207-219
    • Abou-Sleiman, P.M.1    Muqit, M.M.2    Wood, N.W.3
  • 2
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin M.T., and Beal M.F. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443 (2006) 787-795
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 4
    • 10244222286 scopus 로고    scopus 로고
    • MPTP as a mitochondrial neurotoxic model of Parkinson's disease
    • Przedborski S., Tieu K., Perier C., and Vila M. MPTP as a mitochondrial neurotoxic model of Parkinson's disease. J. Bioenerg. Biomembr. 36 (2004) 375-379
    • (2004) J. Bioenerg. Biomembr. , vol.36 , pp. 375-379
    • Przedborski, S.1    Tieu, K.2    Perier, C.3    Vila, M.4
  • 6
    • 0041430614 scopus 로고    scopus 로고
    • Dysfunction of mitochondrial complex I and the proteasome: interactions between two biochemical deficits in a cellular model of Parkinson's disease
    • Hoglinger G.U., Carrard G., Michel P.P., Medja F., Lombes A., Ruberg M., Friguet B., and Hirsch E.C. Dysfunction of mitochondrial complex I and the proteasome: interactions between two biochemical deficits in a cellular model of Parkinson's disease. J. Neurochem. 86 (2003) 1297-1307
    • (2003) J. Neurochem. , vol.86 , pp. 1297-1307
    • Hoglinger, G.U.1    Carrard, G.2    Michel, P.P.3    Medja, F.4    Lombes, A.5    Ruberg, M.6    Friguet, B.7    Hirsch, E.C.8
  • 16
    • 0035109909 scopus 로고    scopus 로고
    • Effect of the overexpression of wild-type or mutant alpha-synuclein on cell susceptibility to insult
    • Lee M., Hyun D., Halliwell B., and Jenner P. Effect of the overexpression of wild-type or mutant alpha-synuclein on cell susceptibility to insult. J. Neurochem. 76 (2001) 998-1009
    • (2001) J. Neurochem. , vol.76 , pp. 998-1009
    • Lee, M.1    Hyun, D.2    Halliwell, B.3    Jenner, P.4
  • 17
    • 20744445814 scopus 로고    scopus 로고
    • Antiapoptotic property of human alpha-synuclein in neuronal cell lines is associated with the inhibition of caspase-3 but not caspase-9 activity
    • Li W., and Lee M.K. Antiapoptotic property of human alpha-synuclein in neuronal cell lines is associated with the inhibition of caspase-3 but not caspase-9 activity. J. Neurochem. 93 (2005) 1542-1550
    • (2005) J. Neurochem. , vol.93 , pp. 1542-1550
    • Li, W.1    Lee, M.K.2
  • 19
    • 34548523836 scopus 로고    scopus 로고
    • Parkinson's disease genetic mutations increase cell susceptibility to stress: Mutant alpha-synuclein enhances H(2)O(2)- and Sin-1-induced cell death
    • Jiang H., Wu Y.C., Nakamura M., Liang Y., Tanaka Y., Holmes S., Dawson V.L., Dawson T.M., Ross C.A., and Smith W.W. Parkinson's disease genetic mutations increase cell susceptibility to stress: Mutant alpha-synuclein enhances H(2)O(2)- and Sin-1-induced cell death. Neurobiol. Aging. 28 (2006) 1709-1717
    • (2006) Neurobiol. Aging. , vol.28 , pp. 1709-1717
    • Jiang, H.1    Wu, Y.C.2    Nakamura, M.3    Liang, Y.4    Tanaka, Y.5    Holmes, S.6    Dawson, V.L.7    Dawson, T.M.8    Ross, C.A.9    Smith, W.W.10
  • 22
    • 29644434199 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity
    • Smith W.W., Jiang H., Pei Z., Tanaka Y., Morita H., Sawa A., Dawson V.L., Dawson T.M., and Ross C.A. Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity. Hum. Mol. Genet. 14 (2005) 3801-3811
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 3801-3811
    • Smith, W.W.1    Jiang, H.2    Pei, Z.3    Tanaka, Y.4    Morita, H.5    Sawa, A.6    Dawson, V.L.7    Dawson, T.M.8    Ross, C.A.9
  • 23
    • 1542617769 scopus 로고    scopus 로고
    • Enhanced substantia nigra mitochondrial pathology in human alpha-synuclein transgenic mice after treatment with MPTP
    • Song D.D., Shults C.W., Sisk A., Rockenstein E., and Masliah E. Enhanced substantia nigra mitochondrial pathology in human alpha-synuclein transgenic mice after treatment with MPTP. Exp. Neurol. 186 (2004) 158-172
    • (2004) Exp. Neurol. , vol.186 , pp. 158-172
    • Song, D.D.1    Shults, C.W.2    Sisk, A.3    Rockenstein, E.4    Masliah, E.5
  • 24
    • 0037155197 scopus 로고    scopus 로고
    • Lipid droplet binding and oligomerization properties of the Parkinson's disease protein alpha-synuclein
    • Cole N.B., Murphy D.D., Grider T., Rueter S., Brasaemle D., and Nussbaum R.L. Lipid droplet binding and oligomerization properties of the Parkinson's disease protein alpha-synuclein. J. Biol. Chem. 277 (2002) 6344-6352
    • (2002) J. Biol. Chem. , vol.277 , pp. 6344-6352
    • Cole, N.B.1    Murphy, D.D.2    Grider, T.3    Rueter, S.4    Brasaemle, D.5    Nussbaum, R.L.6
  • 25
    • 15744402739 scopus 로고    scopus 로고
    • Metal-catalyzed oxidation of alpha-synuclein: helping to define the relationship between oligomers, protofibrils, and filaments
    • Cole N.B., Murphy D.D., Lebowitz J., Di Noto L., Levine R.L., and Nussbaum R.L. Metal-catalyzed oxidation of alpha-synuclein: helping to define the relationship between oligomers, protofibrils, and filaments. J. Biol. Chem. 280 (2005) 9678-9690
    • (2005) J. Biol. Chem. , vol.280 , pp. 9678-9690
    • Cole, N.B.1    Murphy, D.D.2    Lebowitz, J.3    Di Noto, L.4    Levine, R.L.5    Nussbaum, R.L.6
  • 26
    • 3242836174 scopus 로고    scopus 로고
    • Subcellular localization of SV2 and other secretory vesicle components in PC12 cells by an efficient method of preembedding EM immunocytochemistry for cell cultures
    • Tanner V.A., Ploug T., and Tao-Cheng J.H. Subcellular localization of SV2 and other secretory vesicle components in PC12 cells by an efficient method of preembedding EM immunocytochemistry for cell cultures. J. Histochem. Cytochem. 44 (1996) 1481-1488
    • (1996) J. Histochem. Cytochem. , vol.44 , pp. 1481-1488
    • Tanner, V.A.1    Ploug, T.2    Tao-Cheng, J.H.3
  • 27
    • 11244344046 scopus 로고    scopus 로고
    • Concurrent measurements of the free cytosolic concentrations of H+ and Na+ ions with fluorescent indicators
    • Sheldon C., Cheng Y.M., and Church J. Concurrent measurements of the free cytosolic concentrations of H+ and Na+ ions with fluorescent indicators. Pflugers Arch. 449 (2004) 307-318
    • (2004) Pflugers Arch. , vol.449 , pp. 307-318
    • Sheldon, C.1    Cheng, Y.M.2    Church, J.3
  • 29
    • 0018128226 scopus 로고
    • Lipid extraction of tissues with a low-toxicity solvent
    • Hara A., and Radin N.S. Lipid extraction of tissues with a low-toxicity solvent. Anal. Biochem. 90 (1978) 420-426
    • (1978) Anal. Biochem. , vol.90 , pp. 420-426
    • Hara, A.1    Radin, N.S.2
  • 30
    • 0034193996 scopus 로고    scopus 로고
    • The biosynthesis and functional role of cardiolipin
    • Schlame M., Rua D., and Greenberg M.L. The biosynthesis and functional role of cardiolipin. Prog. Lipid Res. 39 (2000) 257-288
    • (2000) Prog. Lipid Res. , vol.39 , pp. 257-288
    • Schlame, M.1    Rua, D.2    Greenberg, M.L.3
  • 31
    • 0021914401 scopus 로고
    • Aldehyde fixatives: quantification of acid-producing reactions
    • Johnson T.J. Aldehyde fixatives: quantification of acid-producing reactions. J. Electron. Microsc. Tech. 2 (1985) 129-138
    • (1985) J. Electron. Microsc. Tech. , vol.2 , pp. 129-138
    • Johnson, T.J.1
  • 33
    • 0031881028 scopus 로고    scopus 로고
    • Molecular order and dynamics in bilayers consisting of highly polyunsaturated phospholipids
    • Mitchell D.C., and Litman B.J. Molecular order and dynamics in bilayers consisting of highly polyunsaturated phospholipids. Biophys. J. 74 (1998) 879-891
    • (1998) Biophys. J. , vol.74 , pp. 879-891
    • Mitchell, D.C.1    Litman, B.J.2
  • 36
    • 0036083038 scopus 로고    scopus 로고
    • Intracellular pH response to anoxia in acutely dissociated adult rat hippocampal CA1 neurons
    • Sheldon C., and Church J. Intracellular pH response to anoxia in acutely dissociated adult rat hippocampal CA1 neurons. J. Neurophysiol. 87 (2002) 2209-2224
    • (2002) J. Neurophysiol. , vol.87 , pp. 2209-2224
    • Sheldon, C.1    Church, J.2
  • 37
    • 0029024751 scopus 로고
    • Dithionite increases radical formation and decreases vasoconstriction in the lung. Evidence that dithionite does not mimic alveolar hypoxia
    • Archer S.L., Hampl V., Nelson D.P., Sidney E., Peterson D.A., and Weir E.K. Dithionite increases radical formation and decreases vasoconstriction in the lung. Evidence that dithionite does not mimic alveolar hypoxia. Circ. Res. 77 (1995) 174-181
    • (1995) Circ. Res. , vol.77 , pp. 174-181
    • Archer, S.L.1    Hampl, V.2    Nelson, D.P.3    Sidney, E.4    Peterson, D.A.5    Weir, E.K.6
  • 38
    • 32644467781 scopus 로고    scopus 로고
    • Oxidative stress induces nuclear translocation of C-terminus of alpha-synuclein in dopaminergic cells
    • Xu S., Zhou M., Yu S., Cai Y., Zhang A., Ueda K., and Chan P. Oxidative stress induces nuclear translocation of C-terminus of alpha-synuclein in dopaminergic cells. Biochem. Biophys. Res. Commun. 342 (2006) 330-335
    • (2006) Biochem. Biophys. Res. Commun. , vol.342 , pp. 330-335
    • Xu, S.1    Zhou, M.2    Yu, S.3    Cai, Y.4    Zhang, A.5    Ueda, K.6    Chan, P.7
  • 39
    • 0024504126 scopus 로고
    • Intracellular pH during "chemical hypoxia" in cultured rat hepatocytes. Protection by intracellular acidosis against the onset of cell death
    • Gores G.J., Nieminen A.L., Wray B.E., Herman B., and Lemasters J.J. Intracellular pH during "chemical hypoxia" in cultured rat hepatocytes. Protection by intracellular acidosis against the onset of cell death. J. Clin. Invest. 83 (1989) 386-396
    • (1989) J. Clin. Invest. , vol.83 , pp. 386-396
    • Gores, G.J.1    Nieminen, A.L.2    Wray, B.E.3    Herman, B.4    Lemasters, J.J.5
  • 40
    • 7444223594 scopus 로고    scopus 로고
    • Hydrogen peroxide-mediated cytosolic acidification is a signal for mitochondrial translocation of Bax during drug-induced apoptosis of tumor cells
    • Ahmad K.A., Iskandar K.B., Hirpara J.L., Clement M.V., and Pervaiz S. Hydrogen peroxide-mediated cytosolic acidification is a signal for mitochondrial translocation of Bax during drug-induced apoptosis of tumor cells. Cancer Res. 64 (2004) 7867-7878
    • (2004) Cancer Res. , vol.64 , pp. 7867-7878
    • Ahmad, K.A.1    Iskandar, K.B.2    Hirpara, J.L.3    Clement, M.V.4    Pervaiz, S.5
  • 41
    • 33847119787 scopus 로고    scopus 로고
    • Growth and trophic factors, pH and the Na+/H+ exchanger in Alzheimer's disease, other neurodegenerative diseases and cancer: new therapeutic possibilities and potential dangers
    • Harguindey S., Reshkin S.J., Orive G., Arranz J.L., and Anitua E. Growth and trophic factors, pH and the Na+/H+ exchanger in Alzheimer's disease, other neurodegenerative diseases and cancer: new therapeutic possibilities and potential dangers. Curr. Alzheimer Res. 4 (2007) 53-65
    • (2007) Curr. Alzheimer Res. , vol.4 , pp. 53-65
    • Harguindey, S.1    Reshkin, S.J.2    Orive, G.3    Arranz, J.L.4    Anitua, E.5
  • 42
    • 4544246352 scopus 로고    scopus 로고
    • Alterations of intracellular pH homeostasis in apoptosis: origins and roles
    • Lagadic-Gossmann D., Huc L., and Lecureur V. Alterations of intracellular pH homeostasis in apoptosis: origins and roles. Cell Death Differ. 11 (2004) 953-961
    • (2004) Cell Death Differ. , vol.11 , pp. 953-961
    • Lagadic-Gossmann, D.1    Huc, L.2    Lecureur, V.3
  • 43
    • 33745821268 scopus 로고    scopus 로고
    • Cytosolic acidification and lysosomal alkalinization during TNF-alpha induced apoptosis in U937 cells
    • Nilsson C., Johansson U., Johansson A.C., Kagedal K., and Ollinger K. Cytosolic acidification and lysosomal alkalinization during TNF-alpha induced apoptosis in U937 cells. Apoptosis 11 (2006) 1149-1159
    • (2006) Apoptosis , vol.11 , pp. 1149-1159
    • Nilsson, C.1    Johansson, U.2    Johansson, A.C.3    Kagedal, K.4    Ollinger, K.5
  • 44
    • 0030862703 scopus 로고    scopus 로고
    • Mechanism of oxidative stress-induced intracellular acidosis in rat cerebellar astrocytes and C6 glioma cells
    • Tsai K.L., Wang S.M., Chen C.C., Fong T.H., and Wu M.L. Mechanism of oxidative stress-induced intracellular acidosis in rat cerebellar astrocytes and C6 glioma cells. J. Physiol. 502 Pt 1 (1997) 161-174
    • (1997) J. Physiol. , vol.502 , Issue.PART 1 , pp. 161-174
    • Tsai, K.L.1    Wang, S.M.2    Chen, C.C.3    Fong, T.H.4    Wu, M.L.5
  • 45
    • 0034672314 scopus 로고    scopus 로고
    • Metabolic effects of 1-methyl-4-phenylpyridinium (MPP(+)) in primary neuron cultures
    • Marini A.M., and Nowak Jr. T.S. Metabolic effects of 1-methyl-4-phenylpyridinium (MPP(+)) in primary neuron cultures. J. Neurosci. Res. 62 (2000) 814-820
    • (2000) J. Neurosci. Res. , vol.62 , pp. 814-820
    • Marini, A.M.1    Nowak Jr., T.S.2
  • 46
    • 0023111890 scopus 로고
    • Microinjection of ras p21 induces a rapid rise in intracellular pH
    • Hagag N., Lacal J.C., Graber M., Aaronson S., and Viola M.V. Microinjection of ras p21 induces a rapid rise in intracellular pH. Mol. Cell. Biol. 7 (1987) 1984-1988
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 1984-1988
    • Hagag, N.1    Lacal, J.C.2    Graber, M.3    Aaronson, S.4    Viola, M.V.5
  • 47
    • 33749656530 scopus 로고    scopus 로고
    • The lysosomal-mitochondrial axis theory of postmitotic aging and cell death
    • Terman A., Gustafsson B., and Brunk U.T. The lysosomal-mitochondrial axis theory of postmitotic aging and cell death. Chem. Biol. Interact. 163 (2006) 29-37
    • (2006) Chem. Biol. Interact. , vol.163 , pp. 29-37
    • Terman, A.1    Gustafsson, B.2    Brunk, U.T.3
  • 48
    • 0018764575 scopus 로고
    • Intracellular pH measurements in Ehrlich ascites tumor cells utilizing spectroscopic probes generated in situ
    • Thomas J.A., Buchsbaum R.N., Zimniak A., and Racker E. Intracellular pH measurements in Ehrlich ascites tumor cells utilizing spectroscopic probes generated in situ. Biochemistry 18 (1979) 2210-2218
    • (1979) Biochemistry , vol.18 , pp. 2210-2218
    • Thomas, J.A.1    Buchsbaum, R.N.2    Zimniak, A.3    Racker, E.4
  • 49
  • 50
    • 33745279409 scopus 로고    scopus 로고
    • A novel mechanism of interaction between alpha-synuclein and biological membranes
    • Kim Y.S., Laurine E., Woods W., and Lee S.J. A novel mechanism of interaction between alpha-synuclein and biological membranes. J. Mol. Biol. 360 (2006) 386-397
    • (2006) J. Mol. Biol. , vol.360 , pp. 386-397
    • Kim, Y.S.1    Laurine, E.2    Woods, W.3    Lee, S.J.4
  • 51
    • 33744788870 scopus 로고    scopus 로고
    • Quantification of alpha-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy
    • Rhoades E., Ramlall T.F., Webb W.W., and Eliezer D. Quantification of alpha-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy. Biophys. J. 90 (2006) 4692-4700
    • (2006) Biophys. J. , vol.90 , pp. 4692-4700
    • Rhoades, E.1    Ramlall, T.F.2    Webb, W.W.3    Eliezer, D.4
  • 52
    • 0021804591 scopus 로고
    • Lipids of mitochondria
    • Daum G. Lipids of mitochondria. Biochim. Biophys. Acta. 822 (1985) 1-42
    • (1985) Biochim. Biophys. Acta. , vol.822 , pp. 1-42
    • Daum, G.1
  • 53
    • 33846272138 scopus 로고    scopus 로고
    • Role of cardiolipin alterations in mitochondrial dysfunction and disease
    • Chicco A.J., and Sparagna G.C. Role of cardiolipin alterations in mitochondrial dysfunction and disease. Am. J. Physiol., Cell. Physiol. 292 (2007) C33-C44
    • (2007) Am. J. Physiol., Cell. Physiol. , vol.292
    • Chicco, A.J.1    Sparagna, G.C.2
  • 55
    • 3042723249 scopus 로고    scopus 로고
    • Bid-cardiolipin interaction at mitochondrial contact site contributes to mitochondrial cristae reorganization and cytochrome C release
    • Kim T.H., Zhao Y., Ding W.X., Shin J.N., He X., Seo Y.W., Chen J., Rabinowich H., Amoscato A.A., and Yin X.M. Bid-cardiolipin interaction at mitochondrial contact site contributes to mitochondrial cristae reorganization and cytochrome C release. Mol. Biol. Cell. 15 (2004) 3061-3072
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 3061-3072
    • Kim, T.H.1    Zhao, Y.2    Ding, W.X.3    Shin, J.N.4    He, X.5    Seo, Y.W.6    Chen, J.7    Rabinowich, H.8    Amoscato, A.A.9    Yin, X.M.10
  • 57
    • 0028230245 scopus 로고
    • Direct analysis and significance of cardiolipin transverse distribution in mitochondrial inner membranes
    • Petit J.M., Huet O., Gallet P.F., Maftah A., Ratinaud M.H., and Julien R. Direct analysis and significance of cardiolipin transverse distribution in mitochondrial inner membranes. Eur. J. Biochem. 220 (1994) 871-879
    • (1994) Eur. J. Biochem. , vol.220 , pp. 871-879
    • Petit, J.M.1    Huet, O.2    Gallet, P.F.3    Maftah, A.4    Ratinaud, M.H.5    Julien, R.6
  • 58
    • 0020039867 scopus 로고
    • Polypeptide and phospholipid composition of the membrane of rat liver peroxisomes: comparison with endoplasmic reticulum and mitochondrial membranes
    • Fujiki Y., Fowler S., Shio H., Hubbard A.L., and Lazarow P.B. Polypeptide and phospholipid composition of the membrane of rat liver peroxisomes: comparison with endoplasmic reticulum and mitochondrial membranes. J. Cell Biol. 93 (1982) 103-110
    • (1982) J. Cell Biol. , vol.93 , pp. 103-110
    • Fujiki, Y.1    Fowler, S.2    Shio, H.3    Hubbard, A.L.4    Lazarow, P.B.5
  • 59
    • 23044512955 scopus 로고    scopus 로고
    • Binding of 10-N-nonyl acridine orange to cardiolipin-deficient yeast cells: implications for assay of cardiolipin
    • Gohil V.M., Gvozdenovic-Jeremic J., Schlame M., and Greenberg M.L. Binding of 10-N-nonyl acridine orange to cardiolipin-deficient yeast cells: implications for assay of cardiolipin. Anal. Biochem. 343 (2005) 350-352
    • (2005) Anal. Biochem. , vol.343 , pp. 350-352
    • Gohil, V.M.1    Gvozdenovic-Jeremic, J.2    Schlame, M.3    Greenberg, M.L.4
  • 61
    • 20344369560 scopus 로고    scopus 로고
    • Increased glutathione S-transferase activity rescues dopaminergic neuron loss in a Drosophila model of Parkinson's disease
    • Whitworth A.J., Theodore D.A., Greene J.C., Benes H., Wes P.D., and Pallanck L.J. Increased glutathione S-transferase activity rescues dopaminergic neuron loss in a Drosophila model of Parkinson's disease. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 8024-8029
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 8024-8029
    • Whitworth, A.J.1    Theodore, D.A.2    Greene, J.C.3    Benes, H.4    Wes, P.D.5    Pallanck, L.J.6
  • 62
    • 33745589773 scopus 로고    scopus 로고
    • Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
    • Clark I.E., Dodson M.W., Jiang C., Cao J.H., Huh J.R., Seol J.H., Yoo S.J., Hay B.A., and Guo M. Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 441 (2006) 1162-1166
    • (2006) Nature , vol.441 , pp. 1162-1166
    • Clark, I.E.1    Dodson, M.W.2    Jiang, C.3    Cao, J.H.4    Huh, J.R.5    Seol, J.H.6    Yoo, S.J.7    Hay, B.A.8    Guo, M.9
  • 64
    • 33746080412 scopus 로고    scopus 로고
    • Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin
    • Yang Y., Gehrke S., Imai Y., Huang Z., Ouyang Y., Wang J.W., Yang L., Beal M.F., Vogel H., and Lu B. Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 10793-10798
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 10793-10798
    • Yang, Y.1    Gehrke, S.2    Imai, Y.3    Huang, Z.4    Ouyang, Y.5    Wang, J.W.6    Yang, L.7    Beal, M.F.8    Vogel, H.9    Lu, B.10
  • 65
    • 33750052885 scopus 로고    scopus 로고
    • DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2
    • Clements C.M., McNally R.S., Conti B.J., Mak T.W., and Ting J.P. DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 15091-15096
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 15091-15096
    • Clements, C.M.1    McNally, R.S.2    Conti, B.J.3    Mak, T.W.4    Ting, J.P.5
  • 67
    • 0023280509 scopus 로고
    • Myocardial contractile function during ischemia and hypoxia
    • Allen D.G., and Orchard C.H. Myocardial contractile function during ischemia and hypoxia. Circ. Res. 60 (1987) 153-168
    • (1987) Circ. Res. , vol.60 , pp. 153-168
    • Allen, D.G.1    Orchard, C.H.2
  • 69
    • 44049099669 scopus 로고    scopus 로고
    • Mitochondrial import and accumulation of alpha -synuclein impairs complex I in human dopaminergic neuronal cultures and Parkinson's disease brain
    • Devi L., Raghavendran V., Prabhu B.M., Avadhani N.G., and Anandatheerthavarada H.K. Mitochondrial import and accumulation of alpha -synuclein impairs complex I in human dopaminergic neuronal cultures and Parkinson's disease brain. J. Biol. Chem. 283 (2008) 9089-9100
    • (2008) J. Biol. Chem. , vol.283 , pp. 9089-9100
    • Devi, L.1    Raghavendran, V.2    Prabhu, B.M.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5


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