메뉴 건너뛰기




Volumn 16, Issue R2, 2007, Pages

Parkinson's disease

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; LRRK2 PROTEIN, HUMAN; ONCOPROTEIN; PARK7 PROTEIN, HUMAN; PARKIN; PROTEIN KINASE; PROTEIN SERINE THREONINE KINASE; PTEN INDUCED PUTATIVE KINASE; PTEN-INDUCED PUTATIVE KINASE; SIGNAL PEPTIDE; SNCA PROTEIN, HUMAN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 37349004102     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddm159     Document Type: Review
Times cited : (714)

References (158)
  • 1
    • 0029981526 scopus 로고    scopus 로고
    • Neuropathology of Parkinson's disease
    • Forno, L.S. (1996) Neuropathology of Parkinson's disease. J. Neuropathol. Exp. Neurol., 55, 259-272.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 259-272
    • Forno, L.S.1
  • 5
    • 10944243102 scopus 로고    scopus 로고
    • Role of alpha-synuclein in presynaptic dopamine recruitment
    • Yavich, L., Tanila, H., Vepsalainen, S. and Jakala, P. (2004) Role of alpha-synuclein in presynaptic dopamine recruitment. J. Neurosci., 24, 11165-11170.
    • (2004) J. Neurosci. , vol.24 , pp. 11165-11170
    • Yavich, L.1    Tanila, H.2    Vepsalainen, S.3    Jakala, P.4
  • 6
    • 33750041624 scopus 로고    scopus 로고
    • Abnormal compartmentalization of norepinephrine in mouse dentate gyrus in alpha-synuclein knockout and A30P transgenic mice
    • Yavich, L., Jakala, P. and Tanila, H. (2006) Abnormal compartmentalization of norepinephrine in mouse dentate gyrus in alpha-synuclein knockout and A30P transgenic mice. J. Neurochem., 99, 724-732.
    • (2006) J. Neurochem. , vol.99 , pp. 724-732
    • Yavich, L.1    Jakala, P.2    Tanila, H.3
  • 11
    • 0032568534 scopus 로고    scopus 로고
    • a-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies
    • Spillantini, M.G., Crowther, R.A., Jakes, R., Hasegawa, M. and Goedert, M. (1998) a-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies. Proc. Natl Acad. Sci. USA, 95, 6469-6473.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6469-6473
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Hasegawa, M.4    Goedert, M.5
  • 13
    • 33646097224 scopus 로고    scopus 로고
    • Pathological changes in dopaminergic nerve cells of the substantia nigra and olfactory bulb in mice transgenic for truncated human alpha-synuclein(1-120): implications for Lewy body disorders
    • Tofaris, G.K., Garcia Reitbock, P., Humby, T., Lambourne, S.L., O'Connell, M., Ghetti, B., Gossage, H., Emson, P.C., Wilkinson, L.S., Goedert, M. et al. (2006) Pathological changes in dopaminergic nerve cells of the substantia nigra and olfactory bulb in mice transgenic for truncated human alpha-synuclein(1-120): implications for Lewy body disorders. J. Neurosci., 26, 3942-3950.
    • (2006) J. Neurosci. , vol.26 , pp. 3942-3950
    • Tofaris, G.K.1    Garcia Reitbock, P.2    Humby, T.3    Lambourne, S.L.4    O'Connell, M.5    Ghetti, B.6    Gossage, H.7    Emson, P.C.8    Wilkinson, L.S.9    Goedert, M.10
  • 14
    • 13844320376 scopus 로고    scopus 로고
    • Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations
    • Li, W., West, N., Colla, E., Pletnikova, O., Troncoso, J.C., Marsh, L., Dawson, T.M., Jakala, P., Hartmann, T., Price, D.L. et al. (2005) Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations. Proc. Natl Acad. Sci. USA, 102, 2162-2167.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 2162-2167
    • Li, W.1    West, N.2    Colla, E.3    Pletnikova, O.4    Troncoso, J.C.5    Marsh, L.6    Dawson, T.M.7    Jakala, P.8    Hartmann, T.9    Price, D.L.10
  • 18
    • 33846817344 scopus 로고    scopus 로고
    • Sept4, a component of presynaptic Scaffold and Lewy bodies, is required for the suppression of alpha-synuclein neurotoxicity
    • Ihara, M., Yamasaki, N., Hagiwara, A., Tanigaki, A., Kitano, A., Hikawa, R., Tomimoto, H., Noda, M., Takanashi, M., Mori, H. et al. (2007) Sept4, a component of presynaptic Scaffold and Lewy bodies, is required for the suppression of alpha-synuclein neurotoxicity. Neuron, 53, 519-533.
    • (2007) Neuron , vol.53 , pp. 519-533
    • Ihara, M.1    Yamasaki, N.2    Hagiwara, A.3    Tanigaki, A.4    Kitano, A.5    Hikawa, R.6    Tomimoto, H.7    Noda, M.8    Takanashi, M.9    Mori, H.10
  • 19
    • 33746897702 scopus 로고    scopus 로고
    • a-Synuclein from platelets is not phosphorylated at serine 129 in Parkinson's disease and multiple system atrophy
    • Shults, C.W., Barrett, J.M. and Fontaine, D. (2006) a-Synuclein from platelets is not phosphorylated at serine 129 in Parkinson's disease and multiple system atrophy. Neurosci. Lett., 405, 223-225.
    • (2006) Neurosci. Lett. , vol.405 , pp. 223-225
    • Shults, C.W.1    Barrett, J.M.2    Fontaine, D.3
  • 21
    • 33846997878 scopus 로고    scopus 로고
    • Presynaptic alpha-synuclein aggregates, not Lewy bodies, cause neurodegeneration in dementia with Lewy bodies
    • Kramer, M.L. and Schulz-Schaeffer, W.J. (2007) Presynaptic alpha-synuclein aggregates, not Lewy bodies, cause neurodegeneration in dementia with Lewy bodies. J. Neurosci., 27, 1405-1410.
    • (2007) J. Neurosci. , vol.27 , pp. 1405-1410
    • Kramer, M.L.1    Schulz-Schaeffer, W.J.2
  • 23
    • 34249946941 scopus 로고    scopus 로고
    • Mono- and double-mutant mouse models of Parkinson's disease display severe mitochondrial damage
    • doi 10.1093/hmg/ddm083
    • Stichel, C.C., Zhu, X.R., Bader, V., Linnartz, B., Schmidt, S. and Lubbert, H. (2007) Mono- and double-mutant mouse models of Parkinson's disease display severe mitochondrial damage. Hum. Mol. Genet., doi 10.1093/hmg/ddm083.
    • (2007) Hum. Mol. Genet
    • Stichel, C.C.1    Zhu, X.R.2    Bader, V.3    Linnartz, B.4    Schmidt, S.5    Lubbert, H.6
  • 24
    • 30644471051 scopus 로고    scopus 로고
    • Parkinson's disease alpha-synuclein transgenic mice develop neuronal mitochondrial degeneration and cell death
    • Martin, L.J., Pan, Y., Price, A.C., Sterling, W., Copeland, N.G., Jenkins, N.A., Price, D.L. and Lee, M.K. (2006) Parkinson's disease alpha-synuclein transgenic mice develop neuronal mitochondrial degeneration and cell death. J. Neurosci., 26, 41-50.
    • (2006) J. Neurosci. , vol.26 , pp. 41-50
    • Martin, L.J.1    Pan, Y.2    Price, A.C.3    Sterling, W.4    Copeland, N.G.5    Jenkins, N.A.6    Price, D.L.7    Lee, M.K.8
  • 27
    • 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. (2004) Enhanced substantia nigra mitochondrial pathology in human alpha-synuclein transgenic mice after treatment with MPTP. Exp. Neurol., 186, 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
  • 32
    • 33645244513 scopus 로고    scopus 로고
    • Alpha-synuclein facilitates the toxicity of oxidized catechol metabolites: implications for selective neurodegeneration in Parkinson's disease
    • Hasegawa, T., Matsuzaki-Kobayashi, M., Takeda, A., Sugeno, N., Kikuchi, A., Furukawa, K., Perry, G., Smith, M.A. and Itoyama, Y. (2006) Alpha-synuclein facilitates the toxicity of oxidized catechol metabolites: implications for selective neurodegeneration in Parkinson's disease. FEBS Lett., 580, 2147-2152.
    • (2006) FEBS Lett , vol.580 , pp. 2147-2152
    • Hasegawa, T.1    Matsuzaki-Kobayashi, M.2    Takeda, A.3    Sugeno, N.4    Kikuchi, A.5    Furukawa, K.6    Perry, G.7    Smith, M.A.8    Itoyama, Y.9
  • 33
    • 40849118624 scopus 로고    scopus 로고
    • alpha-Synuclein activates stress signaling protein kinases in THP-1 cells and microglia
    • doi:10.1016/j.neurobiolaging.2006.11.013
    • Klegeris, A., Pelech, S., Giasson, B.I., Maguire, J., Zhang, H., McGeer, E.G. and McGeer, P.L. (2006) alpha-Synuclein activates stress signaling protein kinases in THP-1 cells and microglia. Neurobiol. Aging, doi:10.1016/j.neurobiolaging.2006.11.013.
    • (2006) Neurobiol. Aging
    • Klegeris, A.1    Pelech, S.2    Giasson, B.I.3    Maguire, J.4    Zhang, H.5    McGeer, E.G.6    McGeer, P.L.7
  • 35
    • 33845656077 scopus 로고    scopus 로고
    • Impairment of microtubule-dependent trafficking by overexpression of alpha-synuclein
    • Lee, H.J., Khoshaghideh, F., Lee, S. and Lee, S.J. (2006) Impairment of microtubule-dependent trafficking by overexpression of alpha-synuclein. Eur. J. Neurosci., 24, 3153-3162.
    • (2006) Eur. J. Neurosci. , vol.24 , pp. 3153-3162
    • Lee, H.J.1    Khoshaghideh, F.2    Lee, S.3    Lee, S.J.4
  • 36
    • 33947605407 scopus 로고    scopus 로고
    • alpha-Synuclein overexpression reduces gap junctional intercellular communication in dopaminergic neuroblastoma cells
    • Sung, J.Y., Lee, H.J., Jeong, E.I., Oh, Y., Park, J., Kang, K.S. and Chung, K.C. (2007) alpha-Synuclein overexpression reduces gap junctional intercellular communication in dopaminergic neuroblastoma cells. Neurosci. Lett., 416, 289-293.
    • (2007) Neurosci. Lett. , vol.416 , pp. 289-293
    • Sung, J.Y.1    Lee, H.J.2    Jeong, E.I.3    Oh, Y.4    Park, J.5    Kang, K.S.6    Chung, K.C.7
  • 37
    • 33749583553 scopus 로고    scopus 로고
    • Alpha-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity
    • Kontopoulos, E., Parvin, J.D. and Feany, M.B. (2006) Alpha-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity. Hum. Mol. Genet., 15, 3012-3023.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 3012-3023
    • Kontopoulos, E.1    Parvin, J.D.2    Feany, M.B.3
  • 38
    • 0034700158 scopus 로고    scopus 로고
    • Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein
    • Zhang, Y., Gao, J., Chung, K.K., Huang, H., Dawson, V.L. and Dawson, T.M. (2000) Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proc. Natl Acad. Sci. USA, 97, 13354-13359.
    • (2000) CDCrel-1. Proc. Natl Acad. Sci. USA , vol.97 , pp. 13354-13359
    • Zhang, Y.1    Gao, J.2    Chung, K.K.3    Huang, H.4    Dawson, V.L.5    Dawson, T.M.6
  • 41
    • 33750354046 scopus 로고    scopus 로고
    • Parkin and defective ubiquitination in Parkinson's disease
    • Dawson, T.M. (2006) Parkin and defective ubiquitination in Parkinson's disease. J. Neural Transm. Suppl., 70, 209-213.
    • (2006) J. Neural Transm. Suppl. , vol.70 , pp. 209-213
    • Dawson, T.M.1
  • 45
    • 33846898753 scopus 로고    scopus 로고
    • The Drosophila parkin homologue is required for normal mitochondrial dynamics during spermiogenesis
    • Riparbelli, M.G. and Callaini, G. (2007) The Drosophila parkin homologue is required for normal mitochondrial dynamics during spermiogenesis. Dev. Biol., 303, 108-120.
    • (2007) Dev. Biol. , vol.303 , pp. 108-120
    • Riparbelli, M.G.1    Callaini, G.2
  • 47
    • 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. (2006) Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin. Proc. Natl Acad. Sci. USA, 103, 10793-10798.
    • (2006) Proc. Natl Acad. Sci. USA , 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
  • 48
    • 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. (2006) Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature, 441, 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
  • 49
    • 33745602748 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
    • Park, J., Lee, S.B., Lee, S., Kim, Y., Song, S., Kim, S., Bae, E., Kim, J., Shong, M., Kim, J.M. et al. (2006) Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature, 441, 1157-1161.
    • (2006) Nature , vol.441 , pp. 1157-1161
    • Park, J.1    Lee, S.B.2    Lee, S.3    Kim, Y.4    Song, S.5    Kim, S.6    Bae, E.7    Kim, J.8    Shong, M.9    Kim, J.M.10
  • 52
    • 2542534741 scopus 로고    scopus 로고
    • S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function
    • Chung, K.K., Thomas, B., Li, X., Pletnikova, O., Troncoso, J.C., Marsh, L., Dawson, V.L. and Dawson, T.M. (2004) S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function. Science, 304, 1328-1331.
    • (2004) Science , vol.304 , pp. 1328-1331
    • Chung, K.K.1    Thomas, B.2    Li, X.3    Pletnikova, O.4    Troncoso, J.C.5    Marsh, L.6    Dawson, V.L.7    Dawson, T.M.8
  • 54
    • 34250344611 scopus 로고    scopus 로고
    • Phosphorylation of parkin by the cyclin-dependent kinase 5 at the linker region modulates its ubiquitin-ligase activity and aggregation
    • Avraham, E., Rott, R., Liani, E., Szargel, R. and Engelender, S. (2007) Phosphorylation of parkin by the cyclin-dependent kinase 5 at the linker region modulates its ubiquitin-ligase activity and aggregation. J. Biol. Chem., 282, 12842-12850.
    • (2007) J. Biol. Chem. , vol.282 , pp. 12842-12850
    • Avraham, E.1    Rott, R.2    Liani, E.3    Szargel, R.4    Engelender, S.5
  • 55
    • 29644448325 scopus 로고    scopus 로고
    • Stress-induced alterations in parkin solubility promote parkin aggregation and compromise parkin's protective function
    • Wang, C., Ko, H.S., Thomas, B., Tsang, F., Chew, K.C., Tay, S.P., Ho, M.W., Lim, T.M., Soong, T.W., Pletnikova, O. et al. (2005) Stress-induced alterations in parkin solubility promote parkin aggregation and compromise parkin's protective function. Hum. Mol. Genet., 14, 3885-3897.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 3885-3897
    • Wang, C.1    Ko, H.S.2    Thomas, B.3    Tsang, F.4    Chew, K.C.5    Tay, S.P.6    Ho, M.W.7    Lim, T.M.8    Soong, T.W.9    Pletnikova, O.10
  • 57
    • 33846804056 scopus 로고    scopus 로고
    • A Drosophila model of mutant human parkin-induced toxicity demonstrates selective loss of dopaminergic neurons and dependence on cellular dopamine
    • Sang, T.K., Chang, H.Y., Lawless, G.M., Ratnaparkhi, A., Mee, L., Ackerson, L.C., Maidment, N.T., Krantz, D.E. and Jackson, G.R. (2007) A Drosophila model of mutant human parkin-induced toxicity demonstrates selective loss of dopaminergic neurons and dependence on cellular dopamine. J. Neurosci., 27, 981-992.
    • (2007) J. Neurosci. , vol.27 , pp. 981-992
    • Sang, T.K.1    Chang, H.Y.2    Lawless, G.M.3    Ratnaparkhi, A.4    Mee, L.5    Ackerson, L.C.6    Maidment, N.T.7    Krantz, D.E.8    Jackson, G.R.9
  • 60
    • 30344450813 scopus 로고    scopus 로고
    • Parkin-deficient mice are not more sensitive to 6-hydroxydopamine or methamphetamine neurotoxicity
    • Perez, F.A., Curtis, W.R. and Palmiter, R.D. (2005) Parkin-deficient mice are not more sensitive to 6-hydroxydopamine or methamphetamine neurotoxicity. BMC Neurosci., 6, 71.
    • (2005) BMC Neurosci , vol.6 , pp. 71
    • Perez, F.A.1    Curtis, W.R.2    Palmiter, R.D.3
  • 69
    • 33947282153 scopus 로고    scopus 로고
    • DJ-1 and Parkin modulate dopamine-dependent behavior and inhibit MPTP-induced nigral dopamine neuron loss in mice
    • Paterna, J.C., Leng, A., Weber, E., Feldon, J. and Bueler, H. (2007) DJ-1 and Parkin modulate dopamine-dependent behavior and inhibit MPTP-induced nigral dopamine neuron loss in mice. Mol. Ther., 15, 698-704.
    • (2007) Mol. Ther. , vol.15 , pp. 698-704
    • Paterna, J.C.1    Leng, A.2    Weber, E.3    Feldon, J.4    Bueler, H.5
  • 71
    • 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. (2006) DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2. Proc. Natl Acad. Sci. USA, 103, 15091-15096.
    • (2006) Proc. Natl Acad. Sci. USA , 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
  • 72
    • 30044449754 scopus 로고    scopus 로고
    • DJ-1 up-regulates glutathione synthesis during oxidative stress and inhibits A53T alpha-synuclein toxicity
    • Zhou, W. and Freed, C.R. (2005) DJ-1 up-regulates glutathione synthesis during oxidative stress and inhibits A53T alpha-synuclein toxicity. J. Biol. Chem., 280, 43150-43158.
    • (2005) J. Biol. Chem. , vol.280 , pp. 43150-43158
    • Zhou, W.1    Freed, C.R.2
  • 73
    • 13944267769 scopus 로고    scopus 로고
    • DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation
    • Shendelman, S., Jonason, A., Martinat, C., Leete, T. and Abeliovich, A. (2004) DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation. PLoS Biol., 2, e362.
    • (2004) PLoS Biol , vol.2
    • Shendelman, S.1    Jonason, A.2    Martinat, C.3    Leete, T.4    Abeliovich, A.5
  • 74
    • 31344464179 scopus 로고    scopus 로고
    • The oxidation state of DJ-1 regulates its chaperone activity toward alpha-synuclein
    • Zhou, W., Zhu, M., Wilson, M.A., Petsko, G.A. and Fink, A.L. (2006) The oxidation state of DJ-1 regulates its chaperone activity toward alpha-synuclein. J. Mol. Biol., 356, 1036-1048.
    • (2006) J. Mol. Biol. , vol.356 , pp. 1036-1048
    • Zhou, W.1    Zhu, M.2    Wilson, M.A.3    Petsko, G.A.4    Fink, A.L.5
  • 76
    • 34250361915 scopus 로고    scopus 로고
    • Structural determinants of the C-terminal helix-kink-helix motif essential for protein stability and survival promoting activity of DJ-1
    • Gorner, K., Holtorf, E., Waak, J., Pham, T.T., Vogt-Weisenhorn, D.M., Wurst, W., Haass, C. and Kahle, P.J. (2007) Structural determinants of the C-terminal helix-kink-helix motif essential for protein stability and survival promoting activity of DJ-1. J. Biol. Chem., 282, 13680-13691.
    • (2007) J. Biol. Chem. , vol.282 , pp. 13680-13691
    • Gorner, K.1    Holtorf, E.2    Waak, J.3    Pham, T.T.4    Vogt-Weisenhorn, D.M.5    Wurst, W.6    Haass, C.7    Kahle, P.J.8
  • 77
    • 34248585862 scopus 로고    scopus 로고
    • Destabilization of DJ-1 by familial substitution and oxidative modifications: implications for Parkinson's disease
    • Hulleman, J.D., Mirzaei, H., Guigard, E., Taylor, K.L., Ray, S.S., Kay, C.M., Regnier, F.E. and Rochet, J.C. (2007) Destabilization of DJ-1 by familial substitution and oxidative modifications: implications for Parkinson's disease. Biochemistry, 46, 5776-5789.
    • (2007) Biochemistry , vol.46 , pp. 5776-5789
    • Hulleman, J.D.1    Mirzaei, H.2    Guigard, E.3    Taylor, K.L.4    Ray, S.S.5    Kay, C.M.6    Regnier, F.E.7    Rochet, J.C.8
  • 83
    • 33847723997 scopus 로고    scopus 로고
    • p53-dependent neuronal cell death in a DJ-1-deficient zebrafish model of Parkinson's disease
    • Bretaud, S., Allen, C., Ingham, P.W. and Bandmann, O. (2007) p53-dependent neuronal cell death in a DJ-1-deficient zebrafish model of Parkinson's disease. J. Neurochem., 100, 1626-1635.
    • (2007) J. Neurochem. , vol.100 , pp. 1626-1635
    • Bretaud, S.1    Allen, C.2    Ingham, P.W.3    Bandmann, O.4
  • 84
    • 33745163261 scopus 로고    scopus 로고
    • Enhanced sensitivity of DJ-1-deficient dopaminergic neurons to energy metabolism impairment: role of Na {thorn} /K{thorn} ATPase
    • Pisani, A., Martella, G., Tscherter, A., Costa, C., Mercuri, N.B., Bernardi, G., Shen, J. and Calabresi, P. (2006) Enhanced sensitivity of DJ-1-deficient dopaminergic neurons to energy metabolism impairment: role of Na {thorn} /K{thorn} ATPase. Neurobiol. Dis., 23, 54-60.
    • (2006) Neurobiol. Dis. , vol.23 , pp. 54-60
    • Pisani, A.1    Martella, G.2    Tscherter, A.3    Costa, C.4    Mercuri, N.B.5    Bernardi, G.6    Shen, J.7    Calabresi, P.8
  • 85
    • 26444489693 scopus 로고    scopus 로고
    • Inactivation of Drosophila DJ-1 leads to impairments of oxidative stress response and phosphatidylinositol 3-kinase/Akt signaling
    • Yang, Y., Gehrke, S., Haque, M.E., Imai, Y., Kosek, J., Yang, L., Beal, M.F., Nishimura, I., Wakamatsu, K., Ito, S. et al. (2005) Inactivation of Drosophila DJ-1 leads to impairments of oxidative stress response and phosphatidylinositol 3-kinase/Akt signaling. Proc. Natl Acad. Sci. USA, 102, 13670-13675.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 13670-13675
    • Yang, Y.1    Gehrke, S.2    Haque, M.E.3    Imai, Y.4    Kosek, J.5    Yang, L.6    Beal, M.F.7    Nishimura, I.8    Wakamatsu, K.9    Ito, S.10
  • 86
    • 22144465488 scopus 로고    scopus 로고
    • Interaction of DJ-1 with Daxx inhibits apoptosis signal-regulating kinase 1 activity and cell death
    • Junn, E., Taniguchi, H., Jeong, B.S., Zhao, X., Ichijo, H. and Mouradian, M.M. (2005) Interaction of DJ-1 with Daxx inhibits apoptosis signal-regulating kinase 1 activity and cell death. Proc. Natl Acad. Sci. USA, 102, 9691-9696.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 9691-9696
    • Junn, E.1    Taniguchi, H.2    Jeong, B.S.3    Zhao, X.4    Ichijo, H.5    Mouradian, M.M.6
  • 87
    • 33746355607 scopus 로고    scopus 로고
    • DJ-1 transcriptionally up-regulates the human tyrosine hydroxylase by inhibiting the sumoylation of pyrimidine tract-binding protein-associated splicing factor
    • Zhong, N., Kim, C.Y., Rizzu, P., Geula, C., Porter, D.R., Pothos, E.N., Squitieri, F., Heutink, P. and Xu, J. (2006) DJ-1 transcriptionally up-regulates the human tyrosine hydroxylase by inhibiting the sumoylation of pyrimidine tract-binding protein-associated splicing factor. J. Biol. Chem., 281, 20940-20948.
    • (2006) J. Biol. Chem. , vol.281 , pp. 20940-20948
    • Zhong, N.1    Kim, C.Y.2    Rizzu, P.3    Geula, C.4    Porter, D.R.5    Pothos, E.N.6    Squitieri, F.7    Heutink, P.8    Xu, J.9
  • 89
    • 33646098921 scopus 로고    scopus 로고
    • Early-onset parkinsonism associated with PINK1 mutations: frequency, genotypes, and phenotypes
    • author reply 1129-1130
    • Klein, C., Grunewald, A. and Hedrich, K. (2006) Early-onset parkinsonism associated with PINK1 mutations: frequency, genotypes, and phenotypes. Neurology, 66, 1129-1130. author reply 1129-1130.
    • (2006) Neurology , vol.66 , pp. 1129-1130
    • Klein, C.1    Grunewald, A.2    Hedrich, K.3
  • 92
    • 17644365438 scopus 로고    scopus 로고
    • Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability
    • Beilina, A., Van Der Brug, M., Ahmad, R., Kesavapany, S., Miller, D.W., Petsko, G.A. and Cookson, M.R. (2005) Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability. Proc. Natl Acad. Sci. USA, 102, 5703-5708.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 5703-5708
    • Beilina, A.1    Van Der Brug, M.2    Ahmad, R.3    Kesavapany, S.4    Miller, D.W.5    Petsko, G.A.6    Cookson, M.R.7
  • 94
    • 33750220194 scopus 로고    scopus 로고
    • C-terminal truncation and Parkinson's disease-associated mutations down-regulate the protein serine/threonine kinase activity of PTEN-induced kinase-1
    • Sim, C.H., Lio, D.S., Mok, S.S., Masters, C.L., Hill, A.F., Culvenor, J.G. and Cheng, H.C. (2006) C-terminal truncation and Parkinson's disease-associated mutations down-regulate the protein serine/threonine kinase activity of PTEN-induced kinase-1. Hum. Mol. Genet., 15, 3251-3262.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 3251-3262
    • Sim, C.H.1    Lio, D.S.2    Mok, S.S.3    Masters, C.L.4    Hill, A.F.5    Culvenor, J.G.6    Cheng, H.C.7
  • 96
    • 26644440926 scopus 로고    scopus 로고
    • Wild-type PINK1 prevents basal and induced neuronal apoptosis, a protective effect abrogated by Parkinson disease-related mutations
    • Petit, A., Kawarai, T., Paitel, E., Sanjo, N., Maj, M., Scheid, M., Chen, F., Gu, Y., Hasegawa, H., Salehi-Rad, S. et al. (2005) Wild-type PINK1 prevents basal and induced neuronal apoptosis, a protective effect abrogated by Parkinson disease-related mutations. J. Biol. Chem., 280, 34025-34032.
    • (2005) J. Biol. Chem. , vol.280 , pp. 34025-34032
    • Petit, A.1    Kawarai, T.2    Paitel, E.3    Sanjo, N.4    Maj, M.5    Scheid, M.6    Chen, F.7    Gu, Y.8    Hasegawa, H.9    Salehi-Rad, S.10
  • 97
    • 27144469287 scopus 로고    scopus 로고
    • Small interfering RNA targeting the PINK1 induces apoptosis in dopaminergic cells SH-SY5Y
    • Deng, H., Jankovic, J., Guo, Y., Xie, W. and Le, W. (2005) Small interfering RNA targeting the PINK1 induces apoptosis in dopaminergic cells SH-SY5Y. Biochem. Biophys. Res. Commun., 337, 1133-1138.
    • (2005) Biochem. Biophys. Res. Commun. , vol.337 , pp. 1133-1138
    • Deng, H.1    Jankovic, J.2    Guo, Y.3    Xie, W.4    Le, W.5
  • 98
    • 33744760852 scopus 로고    scopus 로고
    • Association of PINK1 and DJ-1 confers digenic inheritance of early-onset Parkinson's disease
    • Tang, B., Xiong, H., Sun, P., Zhang, Y., Wang, D., Hu, Z., Zhu, Z., Ma, H., Pan, Q., Xia, J.H. et al. (2006) Association of PINK1 and DJ-1 confers digenic inheritance of early-onset Parkinson's disease. Hum. Mol. Genet., 15, 1816-1825.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1816-1825
    • Tang, B.1    Xiong, H.2    Sun, P.3    Zhang, Y.4    Wang, D.5    Hu, Z.6    Zhu, Z.7    Ma, H.8    Pan, Q.9    Xia, J.H.10
  • 107
    • 33845796537 scopus 로고    scopus 로고
    • Expression and localization of Parkinson's disease-associated leucine-rich repeat kinase 2 in the mouse brain
    • Higashi, S., Moore, D.J., Colebrooke, R.E., Biskup, S., Dawson, V.L., Arai, H., Dawson, T.M. and Emson, P.C. (2007) Expression and localization of Parkinson's disease-associated leucine-rich repeat kinase 2 in the mouse brain. J. Neurochem., 100, 368-381.
    • (2007) J. Neurochem. , vol.100 , pp. 368-381
    • Higashi, S.1    Moore, D.J.2    Colebrooke, R.E.3    Biskup, S.4    Dawson, V.L.5    Arai, H.6    Dawson, T.M.7    Emson, P.C.8
  • 109
    • 33745917404 scopus 로고    scopus 로고
    • Distribution of PINK1 and LRRK2 in rat and mouse brain
    • Taymans, J.M., Van den Haute, C. and Baekelandt, V. (2006) Distribution of PINK1 and LRRK2 in rat and mouse brain. J. Neurochem., 98, 951-961.
    • (2006) J. Neurochem. , vol.98 , pp. 951-961
    • Taymans, J.M.1    Van den Haute, C.2    Baekelandt, V.3
  • 110
  • 111
    • 33947663512 scopus 로고    scopus 로고
    • LRK-1, a C. elegans PARK8-related kinase, regulates axonal-dendritic polarity of SV proteins
    • Sakaguchi-Nakashima, A., Meir, J.Y., Jin, Y., Matsumoto, K. and Hisamoto, N. (2007) LRK-1, a C. elegans PARK8-related kinase, regulates axonal-dendritic polarity of SV proteins. Curr. Biol., 17, 592-598.
    • (2007) Curr. Biol. , vol.17 , pp. 592-598
    • Sakaguchi-Nakashima, A.1    Meir, J.Y.2    Jin, Y.3    Matsumoto, K.4    Hisamoto, N.5
  • 113
    • 33750317653 scopus 로고    scopus 로고
    • LRRK2 protein is a component of Lewy bodies
    • author reply 618-619
    • Zhu, X., Siedlak, S.L., Smith, M.A., Perry, G. and Chen, S.G. (2006) LRRK2 protein is a component of Lewy bodies. Ann. Neurol., 60, 617-618. author reply 618-619.
    • (2006) Ann. Neurol. , vol.60 , pp. 617-618
    • Zhu, X.1    Siedlak, S.L.2    Smith, M.A.3    Perry, G.4    Chen, S.G.5
  • 114
    • 33751256567 scopus 로고    scopus 로고
    • The familial Parkinsonism gene LRRK2 regulates neurite process morphology
    • MacLeod, D., Dowman, J., Hammond, R., Leete, T., Inoue, K. and Abeliovich, A. (2006) The familial Parkinsonism gene LRRK2 regulates neurite process morphology. Neuron, 52, 587-593.
    • (2006) Neuron , vol.52 , pp. 587-593
    • MacLeod, D.1    Dowman, J.2    Hammond, R.3    Leete, T.4    Inoue, K.5    Abeliovich, A.6
  • 115
    • 28044464937 scopus 로고    scopus 로고
    • a new player with a familiar theme for Parkinson's disease pathogenesis
    • Leucine-rich repeat kinase 2
    • Li, C. and Beal, M.F. (2005) Leucine-rich repeat kinase 2: a new player with a familiar theme for Parkinson's disease pathogenesis. Proc. Natl Acad. Sci. USA, 102, 16535-16536.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 16535-16536
    • Li, C.1    Beal, M.F.2
  • 116
    • 33751227461 scopus 로고    scopus 로고
    • Genetic analysis of LRRK2 mutations in patients with Parkinson disease
    • Deng, H., Le, W., Guo, Y., Hunter, C.B., Xie, W., Huang, M. and Jankovic, J. (2006) Genetic analysis of LRRK2 mutations in patients with Parkinson disease. J. Neurol. Sci., 251, 102-106.
    • (2006) J. Neurol. Sci. , vol.251 , pp. 102-106
    • Deng, H.1    Le, W.2    Guo, Y.3    Hunter, C.B.4    Xie, W.5    Huang, M.6    Jankovic, J.7
  • 122
    • 33846818834 scopus 로고    scopus 로고
    • GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease
    • Ito, G., Okai, T., Fujino, G., Takeda, K., Ichijo, H., Katada, T. and Iwatsubo, T. (2007) GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease. Biochemistry, 46, 1380-1388.
    • (2007) Biochemistry , vol.46 , pp. 1380-1388
    • Ito, G.1    Okai, T.2    Fujino, G.3    Takeda, K.4    Ichijo, H.5    Katada, T.6    Iwatsubo, T.7
  • 123
    • 34250192244 scopus 로고    scopus 로고
    • Mutations in LRRK2/dardarin associated with Parkinson disease are more toxic than equivalent mutations in the homologous kinase LRRK1
    • doi:10.1111/j.1471-4159.2007.04523.x
    • Greggio, E., Lewis, P.A., van der Brug, M.P., Ahmad, R., Kaganovich, A., Ding, J., Beilina, A., Baker, A.K. and Cookson, M.R. (2007) Mutations in LRRK2/dardarin associated with Parkinson disease are more toxic than equivalent mutations in the homologous kinase LRRK1. J. Neurochem., doi:10.1111/j.1471-4159.2007.04523.x.
    • (2007) J. Neurochem
    • Greggio, E.1    Lewis, P.A.2    van der Brug, M.P.3    Ahmad, R.4    Kaganovich, A.5    Ding, J.6    Beilina, A.7    Baker, A.K.8    Cookson, M.R.9
  • 127
  • 128
    • 33646948530 scopus 로고    scopus 로고
    • Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled
    • Keeney, P.M., Xie, J., Capaldi, R.A. and Bennett, J.P., Jr (2006) Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled. J. Neurosci., 26, 5256-5264.
    • (2006) J. Neurosci. , vol.26 , pp. 5256-5264
    • Keeney, P.M.1    Xie, J.2    Capaldi, R.A.3    Bennett Jr., J.P.4
  • 129
    • 25444474703 scopus 로고    scopus 로고
    • Mitochondria take center stage in aging and neurodegeneration
    • Beal, M.F. (2005) Mitochondria take center stage in aging and neurodegeneration. Ann. Neurol., 58, 495-505.
    • (2005) Ann. Neurol. , vol.58 , pp. 495-505
    • Beal, M.F.1
  • 131
    • 0031843721 scopus 로고    scopus 로고
    • The risk of Parkinson's disease with exposure to pesticides, farming, well water, and rural living
    • Gorell, J.M., Johnson, C.C., Rybicki, B.A., Peterson, E.L. and Richardson, R.J. (1998) The risk of Parkinson's disease with exposure to pesticides, farming, well water, and rural living. Neurology, 50, 1346-1350.
    • (1998) Neurology , vol.50 , pp. 1346-1350
    • Gorell, J.M.1    Johnson, C.C.2    Rybicki, B.A.3    Peterson, E.L.4    Richardson, R.J.5
  • 132
    • 0020680904 scopus 로고
    • Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis
    • Langston, J.W., Ballard, P., Tetrud, J.W. and Irwin, I. (1983) Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis. Science, 219, 979-980.
    • (1983) Science , vol.219 , pp. 979-980
    • Langston, J.W.1    Ballard, P.2    Tetrud, J.W.3    Irwin, I.4
  • 134
    • 0034671469 scopus 로고    scopus 로고
    • The nigrostriatal dopaminergic system as a preferential target of repeated exposures to combined paraquat and maneb: implications for Parkinson's disease
    • Thiruchelvam, M., Richfield, E.K., Baggs, R.B., Tank, A.W. and Cory-Slechta, D.A. (2000) The nigrostriatal dopaminergic system as a preferential target of repeated exposures to combined paraquat and maneb: implications for Parkinson's disease. J. Neurosci., 20, 9207-9214.
    • (2000) J. Neurosci. , vol.20 , pp. 9207-9214
    • Thiruchelvam, M.1    Richfield, E.K.2    Baggs, R.B.3    Tank, A.W.4    Cory-Slechta, D.A.5
  • 135
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin, M.T. and Beal, M.F. (2006) Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature, 443, 787-795.
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 137
    • 33646351299 scopus 로고    scopus 로고
    • Mitochondrial DNA deletions are abundant and cause functional impairment in aged human substantia nigra neurons
    • Kraytsberg, Y., Kudryavtseva, E., McKee, A.C., Geula, C., Kowall, N.W. and Khrapko, K. (2006) Mitochondrial DNA deletions are abundant and cause functional impairment in aged human substantia nigra neurons. Nat. Genet., 38, 518-520.
    • (2006) Nat. Genet. , vol.38 , pp. 518-520
    • Kraytsberg, Y.1    Kudryavtseva, E.2    McKee, A.C.3    Geula, C.4    Kowall, N.W.5    Khrapko, K.6
  • 139
    • 33846460819 scopus 로고    scopus 로고
    • Mitochondria mass is low in mouse substantia nigra dopamine neurons: implications for Parkinson's disease
    • Liang, C.L., Wang, T.T., Luby-Phelps, K. and German, D.C. (2007) Mitochondria mass is low in mouse substantia nigra dopamine neurons: implications for Parkinson's disease. Exp. Neurol., 203, 370-380.
    • (2007) Exp. Neurol. , vol.203 , pp. 370-380
    • Liang, C.L.1    Wang, T.T.2    Luby-Phelps, K.3    German, D.C.4
  • 141
    • 33749047253 scopus 로고    scopus 로고
    • Reversible inhibition of mitochondrial complex I activity following chronic dopaminergic glutathione depletion in vitro: implications for Parkinson's disease
    • Chinta, S.J. and Andersen, J.K. (2006) Reversible inhibition of mitochondrial complex I activity following chronic dopaminergic glutathione depletion in vitro: implications for Parkinson's disease. Free Radic. Biol. Med., 41, 1442-1448.
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 1442-1448
    • Chinta, S.J.1    Andersen, J.K.2
  • 142
  • 143
    • 33750462349 scopus 로고    scopus 로고
    • PGC-1alpha, a new therapeutic target in Huntington's disease? Cell
    • McGill, J.K. and Beal, M.F. (2006) PGC-1alpha, a new therapeutic target in Huntington's disease? Cell, 127, 465-468.
    • (2006) , vol.127 , pp. 465-468
    • McGill, J.K.1    Beal, M.F.2
  • 145
    • 2342514015 scopus 로고    scopus 로고
    • An important role of Nrf2-ARE pathway in the cellular defense mechanism
    • Lee, J.M. and Johnson, J.A. (2004) An important role of Nrf2-ARE pathway in the cellular defense mechanism. J. Biochem. Mol. Biol., 37, 139-143.
    • (2004) J. Biochem. Mol. Biol. , vol.37 , pp. 139-143
    • Lee, J.M.1    Johnson, J.A.2
  • 146
    • 33344469643 scopus 로고    scopus 로고
    • Oxidative and electrophilic stresses activate Nrf2 through inhibition of ubiquitination activity of Keap1
    • Kobayashi, A., Kang, M.I., Watai, Y., Tong, K.I., Shibata, T., Uchida, K. and Yamamoto, M. (2006) Oxidative and electrophilic stresses activate Nrf2 through inhibition of ubiquitination activity of Keap1. Mol. Cell. Biol., 26, 221-229.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 221-229
    • Kobayashi, A.1    Kang, M.I.2    Watai, Y.3    Tong, K.I.4    Shibata, T.5    Uchida, K.6    Yamamoto, M.7
  • 147
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarashi, K., Engel, J.D. and Yamamoto, M. (1999) Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev., 13, 76-86.
    • (1999) Genes Dev , vol.13 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 149
    • 33751503096 scopus 로고    scopus 로고
    • In vivo modulation of the Parkinsonian phenotype by Nrf2
    • Burton, N.C., Kensler, T.W. and Guilarte, T.R. (2006) In vivo modulation of the Parkinsonian phenotype by Nrf2. Neurotoxicology, 27, 1094-1100.
    • (2006) Neurotoxicology , vol.27 , pp. 1094-1100
    • Burton, N.C.1    Kensler, T.W.2    Guilarte, T.R.3
  • 150
    • 20744440945 scopus 로고    scopus 로고
    • Induction of the Nrf2-driven antioxidant response confers neuroprotection during mitochondrial stress in vivo
    • Shih, A.Y., Imbeault, S., Barakauskas, V., Erb, H., Jiang, L., Li, P. and Murphy, T.H. (2005) Induction of the Nrf2-driven antioxidant response confers neuroprotection during mitochondrial stress in vivo. J. Biol. Chem., 280, 22925-22936.
    • (2005) J. Biol. Chem. , vol.280 , pp. 22925-22936
    • Shih, A.Y.1    Imbeault, S.2    Barakauskas, V.3    Erb, H.4    Jiang, L.5    Li, P.6    Murphy, T.H.7
  • 151
    • 11844253848 scopus 로고    scopus 로고
    • Protection from mitochondrial complex II inhibition in vitro and in vivo by Nrf2-mediated transcription
    • Calkins, M.J., Jakel, R.J., Johnson, D.A., Chan, K., Kan, Y.W. and Johnson, J.A. (2005) Protection from mitochondrial complex II inhibition in vitro and in vivo by Nrf2-mediated transcription. Proc. Natl Acad. Sci. USA, 102, 244-249.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 244-249
    • Calkins, M.J.1    Jakel, R.J.2    Johnson, D.A.3    Chan, K.4    Kan, Y.W.5    Johnson, J.A.6
  • 155
  • 158
    • 33747611218 scopus 로고    scopus 로고
    • Mutational analysis of DJ-1 in Drosophila implicates functional inactivation by oxidative damage and aging
    • Meulener, M.C., Xu, K., Thomson, L., Ischiropoulos, H. and Bonini, N.M. (2006) Mutational analysis of DJ-1 in Drosophila implicates functional inactivation by oxidative damage and aging. Proc. Natl Acad. Sci. USA, 103, 12517-12522.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 12517-12522
    • Meulener, M.C.1    Xu, K.2    Thomson, L.3    Ischiropoulos, H.4    Bonini, N.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.