메뉴 건너뛰기




Volumn 11, Issue 4, 2012, Pages 419-429

Redox sensitivity of tyrosine Hydroxylase activity and expression in dopaminergic dysfunction

Author keywords

Dopamine; Neurodegenaration; Parkinson's disease; Reactive oxygen species; Tyrosine hydroxylase

Indexed keywords

3 NITROTYROSINE; CYSTEINE; DISULFIDE; DOPAMINE; LEVODOPA; PEROXYNITRITE; TYROSINE 3 MONOOXYGENASE; ZINC FINGER PROTEIN;

EID: 84862563824     PISSN: 18715273     EISSN: 19963181     Source Type: Journal    
DOI: 10.2174/187152712800792938     Document Type: Review
Times cited : (18)

References (123)
  • 1
    • 0034545719 scopus 로고    scopus 로고
    • Quantification and significance of protein oxidation in biological samples
    • Shacter, E. Quantification and significance of protein oxidation in biological samples. Drug Metab. Rev., 2000, 32(3/4), 307-326.
    • (2000) Drug Metab. Rev , vol.32 , Issue.3-4 , pp. 307-326
    • Shacter, E.1
  • 2
    • 9444243245 scopus 로고    scopus 로고
    • Cysteine/cystine couple is a newly recognized node in the circuitry for biologic redox signaling and control
    • Jones, D.P.; Go, Y.M.; Anderson, C.L.; Ziegler, T.R.; Kinkade, J.M., Jr.; Kirlin, W.G. Cysteine/cystine couple is a newly recognized node in the circuitry for biologic redox signaling and control. FASEB J., 2004, 18(11), 1246-1248.
    • (2004) FASEB J , vol.18 , Issue.11 , pp. 1246-1248
    • Jones, D.P.1    Go, Y.M.2    Anderson, C.L.3    Ziegler, T.R.4    Kinkade Jr., J.M.5    Kirlin, W.G.6
  • 3
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Schafer, F.Q.; Buettner, G.R. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic. Biol. Med., 2001, 30(11), 1191-1212.
    • (2001) Free Radic. Biol. Med , vol.30 , Issue.11 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 4
    • 0033597878 scopus 로고    scopus 로고
    • Oxidative protein folding is driven by the electron transport system
    • Bader, M.; Muse, W.; Ballou, D.P.; Gassner, C.; Bardwell, J.C. Oxidative protein folding is driven by the electron transport system. Cell, 1999, 98(2), 217-227.
    • (1999) Cell , vol.98 , Issue.2 , pp. 217-227
    • Bader, M.1    Muse, W.2    Ballou, D.P.3    Gassner, C.4    Bardwell, J.C.5
  • 5
    • 0141492988 scopus 로고    scopus 로고
    • Thiol-based regulatory switches
    • Paget, M.S.; Buttner, M.J. Thiol-based regulatory switches. Ann. Rev. Genet., 2003, 37, 91-121.
    • (2003) Ann. Rev. Genet , vol.37 , pp. 91-121
    • Paget, M.S.1    Buttner, M.J.2
  • 6
    • 0035039021 scopus 로고    scopus 로고
    • Protein oxidation in aging and age-related diseases
    • Stadtman, E.R. Protein oxidation in aging and age-related diseases. Ann. NY Acad. Sci., 2001, 928, 22-38.
    • (2001) Ann. NY Acad. Sci , vol.928 , pp. 22-38
    • Stadtman, E.R.1
  • 7
    • 37349055140 scopus 로고    scopus 로고
    • Effect of lipid peroxidation on the properties of lipid bilayers: A molecular dynamics study
    • Wong-Ekkabut, J.; Xu, Z.; Triampo, W.; Tang, I.M.; Tieleman, D.P.; Monticelli, L. Effect of lipid peroxidation on the properties of lipid bilayers: a molecular dynamics study. Biophys. J., 2007, 93(12), 4225-4236.
    • (2007) Biophys. J , vol.93 , Issue.12 , pp. 4225-4236
    • Wong-Ekkabut, J.1    Xu, Z.2    Triampo, W.3    Tang, I.M.4    Tieleman, D.P.5    Monticelli, L.6
  • 8
    • 0032823769 scopus 로고    scopus 로고
    • Antioxidant defence mechanisms: From the beginning to the end (of the beginning)
    • Halliwell, B. Antioxidant defence mechanisms: from the beginning to the end (of the beginning). Free Radic. Res., 1999, 31(4), 261-272.
    • (1999) Free Radic. Res , vol.31 , Issue.4 , pp. 261-272
    • Halliwell, B.1
  • 10
    • 0142010013 scopus 로고    scopus 로고
    • General aspects of neurodegeneration
    • Jellinger, K.A. General aspects of neurodegeneration. J. Neural Transm. Suppl., 2003, 65, 101-144.
    • (2003) J. Neural Transm. Suppl , vol.65 , pp. 101-144
    • Jellinger, K.A.1
  • 11
    • 13644253800 scopus 로고    scopus 로고
    • Searching for the role and the most suitable biomarkers of oxidative stress in Alzheimer's disease and in other neurodegenerative diseases
    • Migliore, L.; Fontana, I.; Colognato, R.; Coppede, F.; Siciliano, G.; Murri, L. Searching for the role and the most suitable biomarkers of oxidative stress in Alzheimer's disease and in other neurodegenerative diseases. Neurobiol. Aging, 2005, 26(5), 587-595.
    • (2005) Neurobiol. Aging , vol.26 , Issue.5 , pp. 587-595
    • Migliore, L.1    Fontana, I.2    Colognato, R.3    Coppede, F.4    Siciliano, G.5    Murri, L.6
  • 13
    • 34548459050 scopus 로고    scopus 로고
    • A probable causative factor for an old problem: Selenium and glutathione peroxidase appear to play important roles in epilepsy pathogenesis
    • Ashrafi, M.R.; Shams, S.; Nouri, M.; Mohseni, M.; Shabanian, R.; Yekaninejad, M.S.; Chegini, N.; Khodadad, A.; Safaralizadeh, R. A probable causative factor for an old problem: selenium and glutathione peroxidase appear to play important roles in epilepsy pathogenesis. Epilepsia, 2007, 48(9), 1750-1755.
    • (2007) Epilepsia , vol.48 , Issue.9 , pp. 1750-1755
    • Ashrafi, M.R.1    Shams, S.2    Nouri, M.3    Mohseni, M.4    Shabanian, R.5    Yekaninejad, M.S.6    Chegini, N.7    Khodadad, A.8    Safaralizadeh, R.9
  • 14
    • 79954628371 scopus 로고    scopus 로고
    • Pilocapine alters NMDA receptor expression and function in hippocampal neurons: NADPH oxidase and ERK1/2 mechanisms
    • Di Maio, R.; Mastroberardino, P.G.; Hu, X.; Montero, L.; Greenamyre, J.T. Pilocapine alters NMDA receptor expression and function in hippocampal neurons: NADPH oxidase and ERK1/2 mechanisms. Neurobiol. Dis., 2011, 42(3), 482-495.
    • (2011) Neurobiol. Dis , vol.42 , Issue.3 , pp. 482-495
    • Di Maio, R.1    Mastroberardino, P.G.2    Hu, X.3    Montero, L.4    Greenamyre, J.T.5
  • 15
    • 34250365299 scopus 로고    scopus 로고
    • Death in the substantia nigra: A motor tragedy. Expert
    • Esposito, E.; Di Matteo, V.; Di Giovanni, G. Death in the substantia nigra: a motor tragedy. Expert Rev. Neurother., 2007, 7(6), 677-697.
    • (2007) Rev. Neurother , vol.7 , Issue.6 , pp. 677-697
    • Esposito, E.1    Di Matteo, V.2    Di Giovanni, G.3
  • 16
    • 0027420895 scopus 로고
    • Nigral degeneration in Parkinson's disease
    • Rinne, J.O. Nigral degeneration in Parkinson's disease. Mov. Disord. 1993, 8(Suppl 1), S31-S35.
    • (1993) Mov. Disord , vol.8 , Issue.SUPPL. 1
    • Rinne, J.O.1
  • 17
    • 34247469020 scopus 로고    scopus 로고
    • Dopamine neuron systems in the brain: An update
    • Bjorklund, A.; Dunnett, S.B. Dopamine neuron systems in the brain: an update. Trends Neurosci., 2007, 30(5), 194-202.
    • (2007) Trends Neurosci , vol.30 , Issue.5 , pp. 194-202
    • Bjorklund, A.1    Dunnett, S.B.2
  • 18
    • 0032171185 scopus 로고    scopus 로고
    • L-Type calcium channels mediate a slow excitatory synaptic transmission in rat midbrain dopaminergic neurons
    • Bonci, A.; Grillner, P.; Mercuri, N.B.; Bernardi, G. L-Type calcium channels mediate a slow excitatory synaptic transmission in rat midbrain dopaminergic neurons. J. Neurosci., 1998, 18(17), 6693-6703.
    • (1998) J. Neurosci , vol.18 , Issue.17 , pp. 6693-6703
    • Bonci, A.1    Grillner, P.2    Mercuri, N.B.3    Bernardi, G.4
  • 19
    • 0027236205 scopus 로고
    • Nifedipine- and omegaconotoxin- sensitive Ca2+ conductances in guinea-pig substantia nigra pars compacta neurones
    • Nedergaard, S.; Flatman, J.A.; Engberg, I. Nifedipine- and omegaconotoxin- sensitive Ca2+ conductances in guinea-pig substantia nigra pars compacta neurones. J. Physiol., 1993, 466, 727-747.
    • (1993) J. Physiol , vol.466 , pp. 727-747
    • Nedergaard, S.1    Flatman, J.A.2    Engberg, I.3
  • 20
    • 33846453291 scopus 로고    scopus 로고
    • Roles of subthreshold calcium current and sodium current in spontaneous firing of mouse midbrain dopamine neurons
    • Puopolo, M.; Raviola, E.; Bean, B.P. Roles of subthreshold calcium current and sodium current in spontaneous firing of mouse midbrain dopamine neurons. J. Neurosci., 2007, 27(3), 645-656.
    • (2007) J. Neurosci , vol.27 , Issue.3 , pp. 645-656
    • Puopolo, M.1    Raviola, E.2    Bean, B.P.3
  • 21
    • 77953447144 scopus 로고    scopus 로고
    • A molecular basis for the increased vulnerability of substantia nigra dopamine neurons in aging and Parkinson's disease
    • Chan, C.S.; Gertler, T.S.; Surmeier, D.J. A molecular basis for the increased vulnerability of substantia nigra dopamine neurons in aging and Parkinson's disease. Mov. Disord., 2010, 25(Suppl 1), S63-S70.
    • (2010) Mov. Disord , vol.25 , Issue.SUPPL. 1
    • Chan, C.S.1    Gertler, T.S.2    Surmeier, D.J.3
  • 23
    • 0029751104 scopus 로고    scopus 로고
    • Oxidative stress and the pathogenesis of Parkinson's disease
    • Jenner, P.; Olanow, C.W. Oxidative stress and the pathogenesis of Parkinson's disease. Neurology, 1996, 47(6 Suppl 3), S161-170.
    • (1996) Neurology , vol.47 , Issue.6 SUPPL. 3 , pp. 161-170
    • Jenner, P.1    Olanow, C.W.2
  • 25
    • 0036075892 scopus 로고    scopus 로고
    • Environmental risk factors and Parkinson's disease: Selective degeneration of nigral dopaminergic neurons caused by the herbicide paraquat
    • McCormack, A.L.; Thiruchelvam, M.; Manning-Bog, A.B.; Thiffault, C.; Langston, J.W.; Cory-Slechta, D.A.; Di Monte, D.A. Environmental risk factors and Parkinson's disease: selective degeneration of nigral dopaminergic neurons caused by the herbicide paraquat. Neurobiol. Dis., 2002, 10(2), 119-127.
    • (2002) Neurobiol. Dis , vol.10 , Issue.2 , pp. 119-127
    • McCormack, A.L.1    Thiruchelvam, M.2    Manning-Bog, A.B.3    Thiffault, C.4    Langston, J.W.5    Cory-Slechta, D.A.6    Di Monte, D.A.7
  • 26
    • 33745057405 scopus 로고    scopus 로고
    • Aspirin protects striatal dopaminergic neurons from neurotoxin-induced degeneration: An in vivo microdialysis study
    • Di Matteo, V.; Pierucci, M.; Di Giovanni, G.; Di Santo, A.; Poggi, A.; Benigno, A.; Esposito, E. Aspirin protects striatal dopaminergic neurons from neurotoxin-induced degeneration: an in vivo microdialysis study. Brain Res., 2006, 1095(1), 167-177.
    • (2006) Brain Res , vol.1095 , Issue.1 , pp. 167-177
    • Di Matteo, V.1    Pierucci, M.2    Di Giovanni, G.3    Di Santo, A.4    Poggi, A.5    Benigno, A.6    Esposito, E.7
  • 27
    • 0024582213 scopus 로고
    • Acute regulation of tyrosine hydroxylase by nerve activity and by neurotransmitters via phosphorylation
    • Zigmond, R.E.; Schwarzschild, M.A.; Rittenhouse, A.R. Acute regulation of tyrosine hydroxylase by nerve activity and by neurotransmitters via phosphorylation. Ann. Rev. Neurosci., 1989, 12, 415-461.
    • (1989) Ann. Rev. Neurosci , vol.12 , pp. 415-461
    • Zigmond, R.E.1    Schwarzschild, M.A.2    Rittenhouse, A.R.3
  • 28
    • 0025353854 scopus 로고
    • Phosphorylation of tyrosine hydroxylase in situ at serine 8, 19, 31, and 40
    • Haycock, J.W. Phosphorylation of tyrosine hydroxylase in situ at serine 8, 19, 31, and 40. J. Biol. Chem., 1990, 265(20), 11682-11691.
    • (1990) J. Biol. Chem , vol.265 , Issue.20 , pp. 11682-11691
    • Haycock, J.W.1
  • 29
    • 0032852842 scopus 로고    scopus 로고
    • Tetrahydropterin-dependent amino acid hydroxylases
    • Fitzpatrick, P.F. Tetrahydropterin-dependent amino acid hydroxylases. Ann. Rev., Biochem., 1999, 68, 355-381.
    • (1999) Ann. Rev., Biochem , vol.68 , pp. 355-381
    • Fitzpatrick, P.F.1
  • 30
    • 0030017489 scopus 로고    scopus 로고
    • Intricate regulation of tyrosine hydroxylase activity and gene expression
    • Kumer, S.C.; Vrana, K.E. Intricate regulation of tyrosine hydroxylase activity and gene expression. J. Neurochem., 1996, 67(2), 443-462.
    • (1996) J. Neurochem , vol.67 , Issue.2 , pp. 443-462
    • Kumer, S.C.1    Vrana, K.E.2
  • 31
    • 0038731081 scopus 로고    scopus 로고
    • Biological selectivity and functional aspects of protein tyrosine nitration
    • Ischiropoulos, H. Biological selectivity and functional aspects of protein tyrosine nitration. Biochem. Biophys. Res. Commun., 2003, 305(3), 776-783.
    • (2003) Biochem. Biophys. Res. Commun , vol.305 , Issue.3 , pp. 776-783
    • Ischiropoulos, H.1
  • 34
    • 0032560486 scopus 로고    scopus 로고
    • Ischiropoulos, H. Inactivation of tyrosine hydroxylase by nitration following exposure to peroxynitrite and 1- methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)
    • Ara, J.; Przedborski, S.; Naini, A.B.; Jackson-Lewis, V.; Trifiletti, R.R.; Horwitz, J.; Ischiropoulos, H. Inactivation of tyrosine hydroxylase by nitration following exposure to peroxynitrite and 1- methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). Proc. Natl. Acad. Sci. USA, 1998, 95(13), 7659-7663.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.13 , pp. 7659-7663
    • Ara, J.1    Przedborski, S.2    Naini, A.B.3    Jackson-Lewis, V.4    Trifiletti, R.R.5    Horwitz, J.6
  • 36
    • 22044436241 scopus 로고    scopus 로고
    • S-thiolation of tyrosine hydroxylase by reactive nitrogen species in the presence of cysteine or glutathione
    • Sadidi, M.; Geddes, T.J.; Kuhn, D.M. S-thiolation of tyrosine hydroxylase by reactive nitrogen species in the presence of cysteine or glutathione. Antioxid. Redox Signal., 2005, 7(7-8), 863-869.
    • (2005) Antioxid. Redox Signal , vol.7 , Issue.7-8 , pp. 863-869
    • Sadidi, M.1    Geddes, T.J.2    Kuhn, D.M.3
  • 38
    • 57149133830 scopus 로고    scopus 로고
    • Protection against cell death and sustained tyrosine hydroxylase phosphorylation in hydrogen peroxide- and MPP-treated human neuroblastoma cells with melatonin
    • Chetsawang, B.; Chetsawang, J.; Govitrapong, P. Protection against cell death and sustained tyrosine hydroxylase phosphorylation in hydrogen peroxide- and MPP-treated human neuroblastoma cells with melatonin. J. Pineal Res., 2009, 46(1), 36-42.
    • (2009) J. Pineal Res , vol.46 , Issue.1 , pp. 36-42
    • Chetsawang, B.1    Chetsawang, J.2    Govitrapong, P.3
  • 39
    • 43049165779 scopus 로고    scopus 로고
    • Melatonin inhibits amphetamine-induced increase in alpha-synuclein and decrease in phosphorylated tyrosine hydroxylase in SK-N-SH cells
    • Klongpanichapak, S.; Phansuwan-Pujito, P.; Ebadi, M.; Govitrapong, P. Melatonin inhibits amphetamine-induced increase in alpha-synuclein and decrease in phosphorylated tyrosine hydroxylase in SK-N-SH cells. Neurosci. Lett., 2008, 436(3), 309-313.
    • (2008) Neurosci. Lett , vol.436 , Issue.3 , pp. 309-313
    • Klongpanichapak, S.1    Phansuwan-Pujito, P.2    Ebadi, M.3    Govitrapong, P.4
  • 40
    • 80052693652 scopus 로고    scopus 로고
    • Oxidative stress in zinc-induced dopaminergic neurodegeneration: Implications of superoxide dismutase and heme oxygenase-1
    • Singh, B.K.; Kumar, A.; Ahmad, I.; Kumar, V.; Patel, D.K.; Jain, S.K.; Singh, C. Oxidative stress in zinc-induced dopaminergic neurodegeneration: implications of superoxide dismutase and heme oxygenase-1. Free Radic. Res., 2011, 45(10), 1207-1222.
    • (2011) Free Radic. Res , vol.45 , Issue.10 , pp. 1207-1222
    • Singh, B.K.1    Kumar, A.2    Ahmad, I.3    Kumar, V.4    Patel, D.K.5    Jain, S.K.6    Singh, C.7
  • 41
    • 70350399505 scopus 로고    scopus 로고
    • Oxidative status of DJ-1-dependent activation of dopamine synthesis through interaction of tyrosine hydroxylase and 4-dihydroxy-L-phenylalanine (L-DOPA) decarboxylase with DJ-1
    • Ishikawa, S.; Taira, T.; Niki, T.; Takahashi-Niki, K.; Maita, C.; Maita, H.; Ariga, H.; Iguchi-Ariga, S.M. Oxidative status of DJ-1-dependent activation of dopamine synthesis through interaction of tyrosine hydroxylase and 4-dihydroxy-L-phenylalanine (L-DOPA) decarboxylase with DJ-1. J. Biol. Chem., 2009, 284(42), 28832-28844.
    • (2009) J. Biol. Chem , vol.284 , Issue.42 , pp. 28832-28844
    • Ishikawa, S.1    Taira, T.2    Niki, T.3    Takahashi-Niki, K.4    Maita, C.5    Maita, H.6    Ariga, H.7    Iguchi-Ariga, S.M.8
  • 43
    • 0037378026 scopus 로고    scopus 로고
    • Oxidative stress in Parkinson's disease
    • discussion S36-S38
    • Jenner, P. Oxidative stress in Parkinson's disease. Ann. Neurol., 2003, 53(Suppl 3), S26-S36; discussion S36-S38.
    • (2003) Ann. Neurol , vol.53 , Issue.SUPPL. 3
    • Jenner, P.1
  • 45
    • 76149095657 scopus 로고    scopus 로고
    • Intracellular redox state alters NMDA receptor response during aging through Ca2+/calmodulin-dependent protein kinase II
    • Bodhinathan, K.; Kumar, A.; Foster, T.C. Intracellular redox state alters NMDA receptor response during aging through Ca2+/calmodulin-dependent protein kinase II. J. Neurosci., 2010, 30(5), 1914-1924.
    • (2010) J. Neurosci , vol.30 , Issue.5 , pp. 1914-1924
    • Bodhinathan, K.1    Kumar, A.2    Foster, T.C.3
  • 46
    • 67349255336 scopus 로고    scopus 로고
    • Oxidation of a potassium channel causes progressive sensory function loss during aging
    • Cai, S.Q.; Sesti, F. Oxidation of a potassium channel causes progressive sensory function loss during aging. Nat. Neurosci., 2009, 12(5), 611-617.
    • (2009) Nat. Neurosci , vol.12 , Issue.5 , pp. 611-617
    • Cai, S.Q.1    Sesti, F.2
  • 47
    • 33750219924 scopus 로고    scopus 로고
    • Oxidative modification of M-type K(+) channels as a mechanism of cytoprotective neuronal silencing
    • Gamper, N.; Zaika, O.; Li, Y.; Martin, P.; Hernandez, C.C.; Perez, M.R.; Wang, A.Y.; Jaffe, D.B.; Shapiro, M.S. Oxidative modification of M-type K(+) channels as a mechanism of cytoprotective neuronal silencing. EMBO J., 2006, 25(20), 4996-5004.
    • (2006) EMBO J , vol.25 , Issue.20 , pp. 4996-5004
    • Gamper, N.1    Zaika, O.2    Li, Y.3    Martin, P.4    Hernandez, C.C.5    Perez, M.R.6    Wang, A.Y.7    Jaffe, D.B.8    Shapiro, M.S.9
  • 48
    • 0030042987 scopus 로고    scopus 로고
    • Physical and functional sensitivity of zinc finger transcription factors to redox change
    • Wu, X.; Bishopric, N.H.; Discher, D.J.; Murphy, B.J.; Webster, K.A. Physical and functional sensitivity of zinc finger transcription factors to redox change. Mol. Cell Biol., 1996, 16(3), 1035-1046.
    • (1996) Mol. Cell Biol , vol.16 , Issue.3 , pp. 1035-1046
    • Wu, X.1    Bishopric, N.H.2    Discher, D.J.3    Murphy, B.J.4    Webster, K.A.5
  • 50
    • 77954935933 scopus 로고    scopus 로고
    • A model of redox kinetics implicates the thiol proteome in cellular hydrogen peroxide responses
    • Adimora, N.J.; Jones, D.P.; Kemp, M.L. A model of redox kinetics implicates the thiol proteome in cellular hydrogen peroxide responses. Antioxid. Redox Signal., 2010, 13(6), 731-743.
    • (2010) Antioxid. Redox Signal , vol.13 , Issue.6 , pp. 731-743
    • Adimora, N.J.1    Jones, D.P.2    Kemp, M.L.3
  • 51
    • 39949085437 scopus 로고    scopus 로고
    • Nonequilibrium thermodynamics of thiol/disulfide redox systems: A perspective on redox systems biology
    • Kemp, M.; Go, Y.M.; Jones, D.P. Nonequilibrium thermodynamics of thiol/disulfide redox systems: a perspective on redox systems biology. Free Radic. Biol. Med., 2008, 44(6), 921-937.
    • (2008) Free Radic. Biol. Med , vol.44 , Issue.6 , pp. 921-937
    • Kemp, M.1    Go, Y.M.2    Jones, D.P.3
  • 52
    • 28844448703 scopus 로고    scopus 로고
    • The bipyridyl herbicide paraquat produces oxidative stress-mediated toxicity in human neuroblastoma SH-SY5Y cells: Relevance to the dopaminergic pathogenesis
    • Yang, W.; Tiffany-Castiglioni, E. The bipyridyl herbicide paraquat produces oxidative stress-mediated toxicity in human neuroblastoma SH-SY5Y cells: relevance to the dopaminergic pathogenesis. J. Toxicol. Environ. Health A, 2005, 68(22), 1939-1961.
    • (2005) J. Toxicol. Environ. Health A , vol.68 , Issue.22 , pp. 1939-1961
    • Yang, W.1    Tiffany-Castiglioni, E.2
  • 54
    • 0035795180 scopus 로고    scopus 로고
    • Generation and propagation of radical reactions on proteins
    • Hawkins, C.L.; Davies, M.J. Generation and propagation of radical reactions on proteins. Biochim. Biophys. Acta, 2001, 1504(2/3), 196-219.
    • (2001) Biochim. Biophys. Acta , vol.1504 , Issue.2-3 , pp. 196-219
    • Hawkins, C.L.1    Davies, M.J.2
  • 55
    • 0031010333 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman, E.R.; Berlett, B.S. Reactive oxygen-mediated protein oxidation in aging and disease. Chem. Res. Toxicol., 1997, 10(5), 485-494.
    • (1997) Chem. Res. Toxicol , vol.10 , Issue.5 , pp. 485-494
    • Stadtman, E.R.1    Berlett, B.S.2
  • 56
    • 0025911829 scopus 로고
    • Metal-catalyzed oxidation of proteins. Physiological consequences
    • Stadtman, E.R.; Oliver, C.N. Metal-catalyzed oxidation of proteins. Physiological consequences. J. Biol. Chem., 1991, 266(4), 2005-2008.
    • (1991) J. Biol. Chem , vol.266 , Issue.4 , pp. 2005-2008
    • Stadtman, E.R.1    Oliver, C.N.2
  • 57
    • 0141767129 scopus 로고    scopus 로고
    • Role of nitric oxide in rotenone-induced nigro-striatal injury
    • He, Y.; Imam, S.Z.; Dong, Z.; Jankovic, J.; Ali, S.F.; Appel, S.H.; Le, W. Role of nitric oxide in rotenone-induced nigro-striatal injury. J. Neurochem., 2003, 86(6), 1338-1345.
    • (2003) J. Neurochem , vol.86 , Issue.6 , pp. 1338-1345
    • He, Y.1    Imam, S.Z.2    Dong, Z.3    Jankovic, J.4    Ali, S.F.5    Appel, S.H.6    Le, W.7
  • 58
    • 0023430333 scopus 로고
    • Isolation and characterization of tetrahydropterin oxidation products generated in the tyrosine 3- monooxygenase (tyrosine hydroxylase) reaction
    • Haavik, J.; Flatmark, T. Isolation and characterization of tetrahydropterin oxidation products generated in the tyrosine 3- monooxygenase (tyrosine hydroxylase) reaction. Eur. J. Biochem., 1987, 168(1), 21-26.
    • (1987) Eur. J. Biochem , vol.168 , Issue.1 , pp. 21-26
    • Haavik, J.1    Flatmark, T.2
  • 59
    • 0032560609 scopus 로고    scopus 로고
    • Effects of phosphorylation of serine 40 of tyrosine hydroxylase on binding of catecholamines: Evidence for a novel regulatory mechanism
    • Ramsey, A.J.; Fitzpatrick, P.F. Effects of phosphorylation of serine 40 of tyrosine hydroxylase on binding of catecholamines: evidence for a novel regulatory mechanism. Biochemistry, 1998, 37(25), 8980-8986.
    • (1998) Biochemistry , vol.37 , Issue.25 , pp. 8980-8986
    • Ramsey, A.J.1    Fitzpatrick, P.F.2
  • 60
    • 0034141542 scopus 로고    scopus 로고
    • Effects of phosphorylation on binding of catecholamines to tyrosine hydroxylase: Specificity and thermodynamics
    • Ramsey, A.J.; Fitzpatrick, P.F. Effects of phosphorylation on binding of catecholamines to tyrosine hydroxylase: specificity and thermodynamics. Biochemistry, 2000, 39(4), 773-778.
    • (2000) Biochemistry , vol.39 , Issue.4 , pp. 773-778
    • Ramsey, A.J.1    Fitzpatrick, P.F.2
  • 61
    • 0027032792 scopus 로고
    • Parkinsonism secondary to ethylene oxide exposure: Case report
    • Barbosa, E.R.; Comerlatti, L.R.; Haddad, M.S.; Scaff, M. [Parkinsonism secondary to ethylene oxide exposure: case report. Arq. Neuropsiquiatr., 1992, 50(4), 531-533.
    • (1992) Arq. Neuropsiquiatr , vol.50 , Issue.4 , pp. 531-533
    • Barbosa, E.R.1    Comerlatti, L.R.2    Haddad, M.S.3    Scaff, M.4
  • 62
    • 0032939923 scopus 로고    scopus 로고
    • Transient severe parkinsonism after acute organophosphate poisoning
    • Muller-Vahl, K.R.; Kolbe, H.; Dengler, R. Transient severe parkinsonism after acute organophosphate poisoning. J. Neurol. Neurosurg. Psychiatry, 1999, 66(2), 253-254.
    • (1999) J. Neurol. Neurosurg. Psychiatry , vol.66 , Issue.2 , pp. 253-254
    • Muller-Vahl, K.R.1    Kolbe, H.2    Dengler, R.3
  • 64
    • 84867417361 scopus 로고    scopus 로고
    • Bioenergetic Origins of Complexity and Disease
    • Epub ahead of print
    • Wallace, D.C. Bioenergetic Origins of Complexity and Disease. Cold Spring Harb. Symp. Quant. Biol., 2011, [Epub ahead of print].
    • (2011) Cold Spring Harb. Symp. Quant. Biol
    • Wallace, D.C.1
  • 65
    • 2242477521 scopus 로고    scopus 로고
    • Dopamine biosynthesis is regulated by S-glutathionylation. Potential mechanism of tyrosine hydroxylast inhibition during oxidative stress
    • Borges, C.R.; Geddes, T.; Watson, J.T.; Kuhn, D.M. Dopamine biosynthesis is regulated by S-glutathionylation. Potential mechanism of tyrosine hydroxylast inhibition during oxidative stress. J. Biol. Chem., 2002, 277(50), 48295-48302.
    • (2002) J. Biol. Chem , vol.277 , Issue.50 , pp. 48295-48302
    • Borges, C.R.1    Geddes, T.2    Watson, J.T.3    Kuhn, D.M.4
  • 66
    • 0042206787 scopus 로고    scopus 로고
    • Dopamine prevents nitration of tyrosine hydroxylase by peroxynitrite and nitrogen dioxide: Is nitrotyrosine formation an early step in dopamine neuronal damage?
    • Park, S.; Geddes, T.J.; Javitch, J.A.; Kuhn, D.M. Dopamine prevents nitration of tyrosine hydroxylase by peroxynitrite and nitrogen dioxide: is nitrotyrosine formation an early step in dopamine neuronal damage? J. Biol. Chem., 2003, 278(31), 28736-28742.
    • (2003) J. Biol. Chem , vol.278 , Issue.31 , pp. 28736-28742
    • Park, S.1    Geddes, T.J.2    Javitch, J.A.3    Kuhn, D.M.4
  • 67
    • 0033869092 scopus 로고    scopus 로고
    • Regulation of protein function by Sglutathiolation in response to oxidative and nitrosative stress
    • Klatt, P.; Lamas, S. Regulation of protein function by Sglutathiolation in response to oxidative and nitrosative stress. Eur. J. Biochem., 2000, 267(16), 4928-4944.
    • (2000) Eur. J. Biochem , vol.267 , Issue.16 , pp. 4928-4944
    • Klatt, P.1    Lamas, S.2
  • 68
    • 0141459380 scopus 로고    scopus 로고
    • Tetrahydrobiopterin prevents nitration of tyrosine hydroxylase by peroxynitrite and nitrogen dioxide
    • Kuhn, D.M.; Geddes, T.J. Tetrahydrobiopterin prevents nitration of tyrosine hydroxylase by peroxynitrite and nitrogen dioxide. Mol. Pharmacol., 2003, 64(4), 946-953.
    • (2003) Mol. Pharmacol , vol.64 , Issue.4 , pp. 946-953
    • Kuhn, D.M.1    Geddes, T.J.2
  • 69
    • 0037066408 scopus 로고    scopus 로고
    • Reduced nicotinamide nucleotides prevent nitration of tyrosine hydroxylase by peroxynitrite
    • Kuhn, D.M.; Geddes, T.J. Reduced nicotinamide nucleotides prevent nitration of tyrosine hydroxylase by peroxynitrite. Brain Res., 2002, 933(1), 85-89.
    • (2002) Brain Res , vol.933 , Issue.1 , pp. 85-89
    • Kuhn, D.M.1    Geddes, T.J.2
  • 70
    • 2042516708 scopus 로고    scopus 로고
    • Nitrotyrosine as a marker for peroxynitrite-induced neurotoxicity: The beginning or the end of the end of dopamine neurons?
    • Kuhn, D.M.; Sakowski, S.A.; Sadidi, M.; Geddes, T.J. Nitrotyrosine as a marker for peroxynitrite-induced neurotoxicity: the beginning or the end of the end of dopamine neurons? J. Neurochem., 2004, 89(3), 529-536.
    • (2004) J. Neurochem , vol.89 , Issue.3 , pp. 529-536
    • Kuhn, D.M.1    Sakowski, S.A.2    Sadidi, M.3    Geddes, T.J.4
  • 72
    • 33847126974 scopus 로고    scopus 로고
    • Dynamics of tyrosine hydroxylase mediated regulation of dopamine synthesis
    • Kaushik, P.; Gorin, F.; Vali, S. Dynamics of tyrosine hydroxylase mediated regulation of dopamine synthesis. J. Comput. Neurosci., 2007, 22(2), 147-160.
    • (2007) J. Comput. Neurosci , vol.22 , Issue.2 , pp. 147-160
    • Kaushik, P.1    Gorin, F.2    Vali, S.3
  • 73
    • 11144247943 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 phosphorylates serine 31 of tyrosine hydroxylase and regulates its stability
    • Moy, L.Y.; Tsai, L.H. Cyclin-dependent kinase 5 phosphorylates serine 31 of tyrosine hydroxylase and regulates its stability. J. Biol. Chem., 2004, 279(52), 54487-54493.
    • (2004) J. Biol. Chem , vol.279 , Issue.52 , pp. 54487-54493
    • Moy, L.Y.1    Tsai, L.H.2
  • 74
    • 0036399655 scopus 로고    scopus 로고
    • Proteasome-driven turnover of tryptophan hydroxylase is triggered by phosphorylation in RBL2H3 cells, a serotonin producing mast cell line
    • Iida, Y.; Sawabe, K.; Kojima, M.; Oguro, K.; Nakanishi, N.; Hasegawa, H. Proteasome-driven turnover of tryptophan hydroxylase is triggered by phosphorylation in RBL2H3 cells, a serotonin producing mast cell line. Eur. J. Biochem., 2002, 269(19), 4780-4788.
    • (2002) Eur. J. Biochem , vol.269 , Issue.19 , pp. 4780-4788
    • Iida, Y.1    Sawabe, K.2    Kojima, M.3    Oguro, K.4    Nakanishi, N.5    Hasegawa, H.6
  • 75
    • 70949084763 scopus 로고    scopus 로고
    • Accumulation of phosphorylated tyrosine hydroxylase into insoluble protein aggregates by inhibition of an ubiquitin-proteasome system in PC12D cells
    • Kawahata, I.; Tokuoka, H.; Parvez, H.; Ichinose, H. Accumulation of phosphorylated tyrosine hydroxylase into insoluble protein aggregates by inhibition of an ubiquitin-proteasome system in PC12D cells. J. Neural Transm., 2009, 116(12), 1571-1578.
    • (2009) J. Neural Transm , vol.116 , Issue.12 , pp. 1571-1578
    • Kawahata, I.1    Tokuoka, H.2    Parvez, H.3    Ichinose, H.4
  • 76
    • 48449107159 scopus 로고    scopus 로고
    • Thiol chemistry and specificity in redox signaling
    • Winterbourn, C.C.; Hampton, M.B. Thiol chemistry and specificity in redox signaling. Free Radic. Biol. Med., 2008, 45(5), 549-561.
    • (2008) Free Radic. Biol. Med , vol.45 , Issue.5 , pp. 549-561
    • Winterbourn, C.C.1    Hampton, M.B.2
  • 77
    • 33750929692 scopus 로고    scopus 로고
    • Reactive oxygen intermediates and signaling through kinase pathways
    • McCubrey, J.A.; Franklin, R.A. Reactive oxygen intermediates and signaling through kinase pathways. Antioxid. Redox Signal., 2006, 8(9/10), 1745-1748.
    • (2006) Antioxid. Redox Signal , vol.8 , Issue.9-10 , pp. 1745-1748
    • McCubrey, J.A.1    Franklin, R.A.2
  • 78
    • 0021118474 scopus 로고
    • Computer-assisted morphometry and microdensitometry of transmitter- identified neurons with special reference to the mesostriatal dopamine pathway. Methodological Aspects
    • Agnati, L.F.; Fuxe, K.; Benfenati, F.; Zini, I.; Zoli, M.; Fabbri, L.; Harfstrand, A. Computer-assisted morphometry and microdensitometry of transmitter- identified neurons with special reference to the mesostriatal dopamine pathway. Methodological aspects. Acta Physiol. Scand. Suppl., 1984, 532, 5-36.
    • (1984) Acta Physiol. Scand. Suppl , vol.532 , pp. 5-36
    • Agnati, L.F.1    Fuxe, K.2    Benfenati, F.3    Zini, I.4    Zoli, M.5    Fabbri, L.6    Harfstrand, A.7
  • 79
    • 0025355643 scopus 로고
    • RNA and protein metabolism in the aging brain
    • Finch, C.E.; Morgan, D.G. RNA and protein metabolism in the aging brain. Ann. Rev. Neurosci., 1990, 13, 75-88.
    • (1990) Ann. Rev. Neurosci , vol.13 , pp. 75-88
    • Finch, C.E.1    Morgan, D.G.2
  • 80
    • 0024349454 scopus 로고
    • Changes in monoamines and their metabolite levels in substantia nigra of aged rats
    • Venero, J.L.; Machado, A.; Cano, J. Changes in monoamines and their metabolite levels in substantia nigra of aged rats. Mech. Ageing Dev., 1989, 49(3), 227-233.
    • (1989) Mech. Ageing Dev , vol.49 , Issue.3 , pp. 227-233
    • Venero, J.L.1    Machado, A.2    Cano, J.3
  • 81
    • 0025900961 scopus 로고
    • Age effects on monoamine turnover of the rat substantia nigra
    • Venero, J.L.; Machado, A.; Cano, J. Age effects on monoamine turnover of the rat substantia nigra. Brain Res., 1991, 557(1/2), 109-114.
    • (1991) Brain Res , vol.557 , Issue.1-2 , pp. 109-114
    • Venero, J.L.1    Machado, A.2    Cano, J.3
  • 82
    • 0023740773 scopus 로고
    • Rate of cell death in parkinsonism indicates active neuropathological process
    • McGeer, P.L.; Itagaki, S.; Akiyama, H.; McGeer, E.G. Rate of cell death in parkinsonism indicates active neuropathological process. Ann. Neurol., 1988, 24(4), 574-576.
    • (1988) Ann. Neurol , vol.24 , Issue.4 , pp. 574-576
    • McGeer, P.L.1    Itagaki, S.2    Akiyama, H.3    McGeer, E.G.4
  • 84
    • 78650810190 scopus 로고    scopus 로고
    • LDOPA reverses motor deficits associated with normal aging in mice
    • Allen, E.; Carlson, K.M.; Zigmond, M.J.; Cavanaugh, J.E. LDOPA reverses motor deficits associated with normal aging in mice. Neurosci. Lett., 2010, 489(1), 1-4.
    • (2010) Neurosci. Lett , vol.489 , Issue.1 , pp. 1-4
    • Allen, E.1    Carlson, K.M.2    Zigmond, M.J.3    Cavanaugh, J.E.4
  • 85
    • 84855204111 scopus 로고    scopus 로고
    • Theaflavin, a black tea polyphenol, protects nigral dopaminergic neurons against chronic MPTP/probenecid induced Parkinson's disease
    • Anandhan, A.; Tamilselvam, K.; Radhiga, T.; Rao, S.; Essa, M.M.; Manivasagam, T. Theaflavin, a black tea polyphenol, protects nigral dopaminergic neurons against chronic MPTP/probenecid induced Parkinson's disease. Brain Res., 2011, 1433, 104-113.
    • (2011) Brain Res , vol.1433 , pp. 104-113
    • Anandhan, A.1    Tamilselvam, K.2    Radhiga, T.3    Rao, S.4    Essa, M.M.5    Manivasagam, T.6
  • 86
    • 84862871811 scopus 로고    scopus 로고
    • Neuroprotective Effect of Sesame Seed Oil in 6-Hydroxydopamine Induced Neurotoxicity in Mice Model: Cellular, Biochemical and Neurochemical Evidence
    • Ahmad, S.; Khan, M.B.; Hoda, M.N.; Bhatia, K.; Haque, R.; Fazili, I.S.; Jamal, A.; Khan, J.S.; Katare, D.P. Neuroprotective Effect of Sesame Seed Oil in 6-Hydroxydopamine Induced Neurotoxicity in Mice Model: Cellular, Biochemical and Neurochemical Evidence. Neurochem. Res., 2011, 37(3), 516-526.
    • (2011) Neurochem. Res , vol.37 , Issue.3 , pp. 516-526
    • Ahmad, S.1    Khan, M.B.2    Hoda, M.N.3    Bhatia, K.4    Haque, R.5    Fazili, I.S.6    Jamal, A.7    Khan, J.S.8    Katare, D.P.9
  • 87
    • 79960501774 scopus 로고    scopus 로고
    • Ethyl pyruvate rescues nigrostriatal dopaminergic neurons by regulating glial activation in a mouse model of Parkinson's disease
    • Huh, S.H.; Chung, Y.C.; Piao, Y.; Jin, M.Y.; Son, H.J.; Yoon, N.S.; Hong, J.Y.; Pak, Y.K.; Kim, Y.S.; Hong, J.K.; Hwang, O.; Jin, B.K. Ethyl pyruvate rescues nigrostriatal dopaminergic neurons by regulating glial activation in a mouse model of Parkinson's disease. J. Immunol., 2011, 187(2), 960-969.
    • (2011) J. Immunol , vol.187 , Issue.2 , pp. 960-969
    • Huh, S.H.1    Chung, Y.C.2    Piao, Y.3    Jin, M.Y.4    Son, H.J.5    Yoon, N.S.6    Hong, J.Y.7    Pak, Y.K.8    Kim, Y.S.9    Hong, J.K.10    Hwang, O.11    Jin, B.K.12
  • 88
    • 49149102041 scopus 로고    scopus 로고
    • Rotenone-induced PC12 cell toxicity is caused by oxidative stress resulting from altered dopamine metabolism
    • Sai, Y.; Wu, Q.; Le, W.; Ye, F.; Li, Y.; Dong, Z. Rotenone-induced PC12 cell toxicity is caused by oxidative stress resulting from altered dopamine metabolism. Toxicol. In Vitro, 2008, 22(6), 1461-1468.
    • (2008) Toxicol. In Vitro , vol.22 , Issue.6 , pp. 1461-1468
    • Sai, Y.1    Wu, Q.2    Le, W.3    Ye, F.4    Li, Y.5    Dong, Z.6
  • 89
    • 79961210760 scopus 로고    scopus 로고
    • Lithium protects against oxidative stress-mediated cell death in alpha-synucleinoverexpressing in vitro and in vivo models of Parkinson's disease
    • Kim, Y.H.; Rane, A.; Lussier, S.; Andersen, J.K. Lithium protects against oxidative stress-mediated cell death in alpha-synucleinoverexpressing in vitro and in vivo models of Parkinson's disease. J. Neurosci. Res., 2011, 89(10), 1666-1675.
    • (2011) J. Neurosci. Res , vol.89 , Issue.10 , pp. 1666-1675
    • Kim, Y.H.1    Rane, A.2    Lussier, S.3    Andersen, J.K.4
  • 90
    • 84857789619 scopus 로고    scopus 로고
    • Effects of lithium therapy on Na(+)-K(+)-ATPase activity and lipid peroxidation in bipolar disorder
    • Banerjee, U.; Dasgupta, A.; Rout, J.K.; Singh, O.P. Effects of lithium therapy on Na(+)-K(+)-ATPase activity and lipid peroxidation in bipolar disorder. Prog. Neuropsychopharmacol. Biol. Psychiatry, 2012, 37(1), 56-61.
    • (2012) Prog. Neuropsychopharmacol. Biol. Psychiatry , vol.37 , Issue.1 , pp. 56-61
    • Banerjee, U.1    Dasgupta, A.2    Rout, J.K.3    Singh, O.P.4
  • 91
    • 84862584856 scopus 로고    scopus 로고
    • Mood stabilizer lithium inhibits amphetamine-increased 4- hydroxynonenal-protein adducts in rat frontal cortex
    • Epub ahead of print
    • Tan, H.; Young, L.T.; Shao, L.; Che, Y.; Honer, W.G.; Wang, J.F. Mood stabilizer lithium inhibits amphetamine-increased 4- hydroxynonenal-protein adducts in rat frontal cortex. Int. J. Neuropsychopharmacol., 2011, [Epub ahead of print]
    • (2011) Int. J. Neuropsychopharmacol
    • Tan, H.1    Young, L.T.2    Shao, L.3    Che, Y.4    Honer, W.G.5    Wang, J.F.6
  • 94
    • 33846334440 scopus 로고    scopus 로고
    • Effect of lithium and lithium withdrawal on potassium-evoked dopamine release and tyrosine hydroxylase expression in the rat
    • Ferrie, L.; Young, A.H.; McQuade, R. Effect of lithium and lithium withdrawal on potassium-evoked dopamine release and tyrosine hydroxylase expression in the rat. Int. J. Neuropsychopharmacol., 2006, 9(6), 729-735.
    • (2006) Int. J. Neuropsychopharmacol , vol.9 , Issue.6 , pp. 729-735
    • Ferrie, L.1    Young, A.H.2    McQuade, R.3
  • 95
    • 0033674209 scopus 로고    scopus 로고
    • Movement of zinc and its functional significance in the brain
    • Takeda, A. Movement of zinc and its functional significance in the brain. Brain Res. Brain Res. Rev., 2000, 34(3), 137-148.
    • (2000) Brain Res. Brain Res. Rev , vol.34 , Issue.3 , pp. 137-148
    • Takeda, A.1
  • 96
    • 77956390795 scopus 로고    scopus 로고
    • Effect of zinc and paraquat co-exposure on neurodegeneration: Modulation of oxidative stress and expression of metallothioneins, toxicant responsive and transporter genes in rats
    • Kumar, A.; Ahmad, I.; Shukla, S.; Singh, B.K.; Patel, D.K.; Pandey, H.P.; Singh, C. Effect of zinc and paraquat co-exposure on neurodegeneration: Modulation of oxidative stress and expression of metallothioneins, toxicant responsive and transporter genes in rats. Free Radic. Res., 2010, 44(8), 950-965.
    • (2010) Free Radic. Res , vol.44 , Issue.8 , pp. 950-965
    • Kumar, A.1    Ahmad, I.2    Shukla, S.3    Singh, B.K.4    Patel, D.K.5    Pandey, H.P.6    Singh, C.7
  • 97
    • 84862777684 scopus 로고    scopus 로고
    • Involvement of NADPH oxidase and glutathione in zinc-induced dopaminergic neurodegeneration in rats: Similarity with paraquat neurotoxicity
    • Kumar, A.; Singh, B.K.; Ahmad, I.; Shukla, S.; Patel, D.K.; Srivastava, G.; Kumar, V.; Pandey, H.P.; Singh, C. Involvement of NADPH oxidase and glutathione in zinc-induced dopaminergic neurodegeneration in rats: Similarity with paraquat neurotoxicity. Brain Res., 2011, 1438, 48-64.
    • (2011) Brain Res , vol.1438 , pp. 48-64
    • Kumar, A.1    Singh, B.K.2    Ahmad, I.3    Shukla, S.4    Patel, D.K.5    Srivastava, G.6    Kumar, V.7    Pandey, H.P.8    Singh, C.9
  • 98
    • 0025821265 scopus 로고
    • Alterations in the levels of iron, ferritin and other trace metals in Parkinson's disease and other neurodegenerative diseases affecting the basal ganglia
    • Dexter, D.T.; Carayon, A.; Javoy-Agid, F.; Agid, Y.; Wells, F.R.; Daniel, S.E.; Lees, A.J.; Jenner, P.; Marsden, C.D. Alterations in the levels of iron, ferritin and other trace metals in Parkinson's disease and other neurodegenerative diseases affecting the basal ganglia. Brain, 1991, 114(Pt 4), 1953-1975.
    • (1991) Brain , vol.114 , Issue.Pt 4 , pp. 1953-1975
    • Dexter, D.T.1    Carayon, A.2    Javoy-Agid, F.3    Agid, Y.4    Wells, F.R.5    Daniel, S.E.6    Lees, A.J.7    Jenner, P.8    Marsden, C.D.9
  • 99
    • 0038707360 scopus 로고    scopus 로고
    • Zincinduced apoptosis in substantia nigra of rat brain: Neuroprotection by vitamin D3
    • Lin, A.M.; Fan, S.F.; Yang, D.M.; Hsu, L.L.; Yang, C.H. Zincinduced apoptosis in substantia nigra of rat brain: neuroprotection by vitamin D3. Free Radic. Biol. Med., 2003, 34(11), 1416-1425.
    • (2003) Free Radic. Biol. Med , vol.34 , Issue.11 , pp. 1416-1425
    • Lin, A.M.1    Fan, S.F.2    Yang, D.M.3    Hsu, L.L.4    Yang, C.H.5
  • 100
    • 0027257482 scopus 로고
    • Induction and nuclear accumulation of fos and jun proto-oncogenes in hypoxic cardiac myocytes
    • Webster, K.A.; Discher, D.J.; Bishopric, N.H. Induction and nuclear accumulation of fos and jun proto-oncogenes in hypoxic cardiac myocytes. J. Biol. Chem., 1993, 268(22), 16852-16858.
    • (1993) J. Biol. Chem , vol.268 , Issue.22 , pp. 16852-16858
    • Webster, K.A.1    Discher, D.J.2    Bishopric, N.H.3
  • 101
    • 0025825989 scopus 로고
    • Redox regulation of a protein tyrosine kinase in the endoplasmic reticulum
    • Bauskin, A.R.; Alkalay, I.; Ben-Neriah, Y. Redox regulation of a protein tyrosine kinase in the endoplasmic reticulum. Cell, 1991, 66(4), 685-696.
    • (1991) Cell , vol.66 , Issue.4 , pp. 685-696
    • Bauskin, A.R.1    Alkalay, I.2    Ben-Neriah, Y.3
  • 102
    • 0026751187 scopus 로고
    • The regulation of glutathione peroxidase gene expression by oxygen tension in cultured human cardiomyocytes
    • Cowan, D.B.; Weisel, R.D.; Williams, W.G.; Mickle, D.A. The regulation of glutathione peroxidase gene expression by oxygen tension in cultured human cardiomyocytes. J. Mol. Cell Cardiol., 1992, 24(4), 423-433.
    • (1992) J. Mol. Cell Cardiol , vol.24 , Issue.4 , pp. 423-433
    • Cowan, D.B.1    Weisel, R.D.2    Williams, W.G.3    Mickle, D.A.4
  • 103
    • 0027210562 scopus 로고
    • General involvement of hypoxiainducible factor 1 in transcriptional response to hypoxia
    • Wang, G.L.; Semenza, G.L. General involvement of hypoxiainducible factor 1 in transcriptional response to hypoxia. Proc. Natl. Acad. Sci. USA, 1993, 90(9), 4304-4308.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , Issue.9 , pp. 4304-4308
    • Wang, G.L.1    Semenza, G.L.2
  • 104
    • 18144432245 scopus 로고
    • Zinc fingers
    • Rhodes, D.; Klug, A. Zinc fingers. Sci. Am., 1993, 268(2), 56-59.
    • (1993) Sci. Am , vol.268 , Issue.2 , pp. 56-59
    • Rhodes, D.1    Klug, A.2
  • 105
    • 0026497472 scopus 로고
    • Sp1 and the subfamily of zinc finger proteins with guanine-rich binding sites
    • Berg, J.M. Sp1 and the subfamily of zinc finger proteins with guanine-rich binding sites. Proc. Natl. Acad. Sci. USA, 1992, 89(23), 11109-11110.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , Issue.23 , pp. 11109-11110
    • Berg, J.M.1
  • 106
    • 0026742626 scopus 로고
    • Toward rules relating zinc finger protein sequences and DNA binding site preferences
    • Desjarlais, J.R.; Berg, J.M. Toward rules relating zinc finger protein sequences and DNA binding site preferences. Proc. Natl. Acad. Sci. USA, 1992, 89(16), 7345-7349.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , Issue.16 , pp. 7345-7349
    • Desjarlais, J.R.1    Berg, J.M.2
  • 107
    • 0023663884 scopus 로고
    • Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain
    • Kadonaga, J.T.; Carner, K.R.; Masiarz, F.R.; Tjian, R. Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain. Cell, 1987, 51(6), 1079-1090.
    • (1987) Cell , vol.51 , Issue.6 , pp. 1079-1090
    • Kadonaga, J.T.1    Carner, K.R.2    Masiarz, F.R.3    Tjian, R.4
  • 108
    • 0028036190 scopus 로고
    • A glutamine-rich hydrophobic patch in transcription factor Sp1 contacts the dTAFII110 component of the Drosophila TFIID complex and mediates transcriptional activation
    • Gill, G.; Pascal, E.; Tseng, Z.H.; Tjian, R. A glutamine-rich hydrophobic patch in transcription factor Sp1 contacts the dTAFII110 component of the Drosophila TFIID complex and mediates transcriptional activation. Proc. Natl. Acad. Sci. USA, 1994, 91(1), 192-196.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , Issue.1 , pp. 192-196
    • Gill, G.1    Pascal, E.2    Tseng, Z.H.3    Tjian, R.4
  • 109
    • 0026647971 scopus 로고
    • The retinoblastoma gene product regulates Sp1-mediated transcription
    • Kim, S.J.; Onwuta, U.S.; Lee, Y.I.; Li, R.; Botchan, M.R.; Robbins, P.D. The retinoblastoma gene product regulates Sp1-mediated transcription. Mol. Cell Biol., 1992, 12(6), 2455-2463.
    • (1992) Mol. Cell Biol , vol.12 , Issue.6 , pp. 2455-2463
    • Kim, S.J.1    Onwuta, U.S.2    Lee, Y.I.3    Li, R.4    Botchan, M.R.5    Robbins, P.D.6
  • 110
    • 0026756135 scopus 로고
    • Cloning of GT box-binding proteins: A novel Sp1 multigene family regulating T-cell receptor gene expression
    • Kingsley, C.; Winoto, A. Cloning of GT box-binding proteins: a novel Sp1 multigene family regulating T-cell receptor gene expression. Mol. Cell. Biol., 1992, 12(10), 4251-4261.
    • (1992) Mol. Cell. Biol , vol.12 , Issue.10 , pp. 4251-4261
    • Kingsley, C.1    Winoto, A.2
  • 111
    • 0027968491 scopus 로고
    • The DNAbinding efficiency of Sp1 is affected by redox changes
    • Ammendola, R.; Mesuraca, M.; Russo, T.; Cimino, F. The DNAbinding efficiency of Sp1 is affected by redox changes. Eur. J. Biochem., 1994, 225(1), 483-489.
    • (1994) Eur. J. Biochem , vol.225 , Issue.1 , pp. 483-489
    • Ammendola, R.1    Mesuraca, M.2    Russo, T.3    Cimino, F.4
  • 112
    • 0024516594 scopus 로고
    • Oxidation-reduction and the molecular mechanism of a regulatory RNA-protein interaction
    • Hentze, M.W.; Rouault, T.A.; Harford, J.B.; Klausner, R.D. Oxidation-reduction and the molecular mechanism of a regulatory RNA-protein interaction. Science, 1989, 244(4902), 357-359.
    • (1989) Science , vol.244 , Issue.4902 , pp. 357-359
    • Hentze, M.W.1    Rouault, T.A.2    Harford, J.B.3    Klausner, R.D.4
  • 113
    • 0026473086 scopus 로고
    • The helix-loop-helix/leucine repeat transcription factor USF can be functionally regulated in a redox-dependent manner
    • Pognonec, P.; Kato, H.; Roeder, R.G. The helix-loop-helix/leucine repeat transcription factor USF can be functionally regulated in a redox-dependent manner. J. Biol. Chem., 1992, 267(34), 24563-24567.
    • (1992) J. Biol. Chem , vol.267 , Issue.34 , pp. 24563-24567
    • Pognonec, P.1    Kato, H.2    Roeder, R.G.3
  • 114
    • 0037426917 scopus 로고    scopus 로고
    • Pathways to Parkinsonism
    • Cookson, M.R. Pathways to Parkinsonism. Neuron, 2003, 37(1), 7-10.
    • (2003) Neuron , vol.37 , Issue.1 , pp. 7-10
    • Cookson, M.R.1
  • 117
    • 0042232353 scopus 로고    scopus 로고
    • The role of pathogenic DJ-1 mutations in Parkinson's disease
    • Abou-Sleiman, P.M.; Healy, D.G.; Quinn, N.; Lees, A.J.; Wood, N.W. The role of pathogenic DJ-1 mutations in Parkinson's disease. Ann. Neurol., 2003, 54(3), 283-286.
    • (2003) Ann. Neurol , vol.54 , Issue.3 , pp. 283-286
    • Abou-Sleiman, P.M.1    Healy, D.G.2    Quinn, N.3    Lees, A.J.4    Wood, N.W.5
  • 123
    • 33746355607 scopus 로고    scopus 로고
    • DJ-1 transcriptionally upregulates 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.; Xu, J. DJ-1 transcriptionally upregulates the human tyrosine hydroxylase by inhibiting the sumoylation of pyrimidine tract-binding protein-associated splicing factor. J. Biol. Chem., 2006, 281(30), 20940-20948.
    • (2006) J. Biol. Chem , vol.281 , Issue.30 , 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.