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Volumn 236, Issue , 2016, Pages 148-157

Regulators of mitochondrial complex I activity: A review of literature and evaluation in postmortem prefrontal cortex from patients with bipolar disorder

Author keywords

Bipolar disorder; DJ 1; Gene expression; Microarray; Mitochondrial complex I; Mitochondrial regulators

Indexed keywords

DJ 1 PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SIRTUIN 3; STAT3 PROTEIN; IGF2BP2 PROTEIN, HUMAN; ONCOPROTEIN; PARK7 PROTEIN, HUMAN; PROTEIN DEGLYCASE DJ-1; RNA BINDING PROTEIN; SIGNAL PEPTIDE; SIRT3 PROTEIN, HUMAN; STAT3 PROTEIN, HUMAN;

EID: 84957683514     PISSN: 01651781     EISSN: 18727123     Source Type: Journal    
DOI: 10.1016/j.psychres.2015.12.015     Document Type: Article
Times cited : (8)

References (122)
  • 2
    • 84904498580 scopus 로고    scopus 로고
    • Altered dopamine homeostasis differentially affects mitochondrial voltage-dependent anion channels turnover
    • Alberio T., Mammucari C., D'Agostino G., Rizzuto R., Fasano M. Altered dopamine homeostasis differentially affects mitochondrial voltage-dependent anion channels turnover. Biochim. Biophys. Acta 2014, 1842:1816-1822.
    • (2014) Biochim. Biophys. Acta , vol.1842 , pp. 1816-1822
    • Alberio, T.1    Mammucari, C.2    D'Agostino, G.3    Rizzuto, R.4    Fasano, M.5
  • 4
    • 77950575478 scopus 로고    scopus 로고
    • Mitochondrial complex I activity and oxidative damage to mitochondrial proteins in the prefrontal cortex of patients with bipolar disorder
    • Andreazza A.C., Shao L., Wang J.F., Young L.T. Mitochondrial complex I activity and oxidative damage to mitochondrial proteins in the prefrontal cortex of patients with bipolar disorder. Arch. Gen. Psychiatry 2010, 67:360-368.
    • (2010) Arch. Gen. Psychiatry , vol.67 , pp. 360-368
    • Andreazza, A.C.1    Shao, L.2    Wang, J.F.3    Young, L.T.4
  • 5
    • 84901398313 scopus 로고    scopus 로고
    • The neurobiology of bipolar disorder: identifying targets for specific agents and synergies for combination treatment
    • Andreazza A.C., Young L.T. The neurobiology of bipolar disorder: identifying targets for specific agents and synergies for combination treatment. Int. J. Neuropsychopharmacol. 2014, 17:1039-1052.
    • (2014) Int. J. Neuropsychopharmacol. , vol.17 , pp. 1039-1052
    • Andreazza, A.C.1    Young, L.T.2
  • 7
    • 0035108147 scopus 로고    scopus 로고
    • Protein thiol oxidation by haloperidol results in inhibition of mitochondrial complex I in brain regions: comparison with atypical antipsychotics
    • Balijepalli S., Kenchappa R.S., Boyd M.R., Ravindranath V. Protein thiol oxidation by haloperidol results in inhibition of mitochondrial complex I in brain regions: comparison with atypical antipsychotics. Neurochem. Int. 2001, 38:425-435.
    • (2001) Neurochem. Int. , vol.38 , pp. 425-435
    • Balijepalli, S.1    Kenchappa, R.S.2    Boyd, M.R.3    Ravindranath, V.4
  • 9
    • 84879026707 scopus 로고    scopus 로고
    • SIRT3 regulation of mitochondrial oxidative stress
    • Bause A.S., Haigis M.C. SIRT3 regulation of mitochondrial oxidative stress. Exp. Gerontol. 2013, 48:634-639.
    • (2013) Exp. Gerontol. , vol.48 , pp. 634-639
    • Bause, A.S.1    Haigis, M.C.2
  • 10
    • 0036570159 scopus 로고    scopus 로고
    • Oxidatively modified proteins in aging and disease
    • Beal M.F. Oxidatively modified proteins in aging and disease. Free. Radic. Biol. Med. 2002, 32:797-803.
    • (2002) Free. Radic. Biol. Med. , vol.32 , pp. 797-803
    • Beal, M.F.1
  • 11
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly
    • Beckman J.S., Koppenol W.H. Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly. Am. J. Physiol. 1996, 271:C1424-C1437.
    • (1996) Am. J. Physiol. , vol.271 , pp. C1424-C1437
    • Beckman, J.S.1    Koppenol, W.H.2
  • 12
    • 9144249116 scopus 로고    scopus 로고
    • Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant DEFENSE
    • Beer S.M., Taylor E.R., Brown S.E., Dahm C.C., Costa N.J., Runswick M.J., Murphy M.P. Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant DEFENSE. J. Biol. Chem. 2004, 279:47939-47951.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47939-47951
    • Beer, S.M.1    Taylor, E.R.2    Brown, S.E.3    Dahm, C.C.4    Costa, N.J.5    Runswick, M.J.6    Murphy, M.P.7
  • 13
    • 0025980955 scopus 로고
    • The iron chelator desferrioxamine (Desferal) retards 6-hydroxydopamine-induced degeneration of nigrostriatal dopamine neurons
    • Ben-Shachar D., Eshel G., Finberg J.P., Youdim M.B. The iron chelator desferrioxamine (Desferal) retards 6-hydroxydopamine-induced degeneration of nigrostriatal dopamine neurons. J. Neurochem. 1991, 56:1441-1444.
    • (1991) J. Neurochem. , vol.56 , pp. 1441-1444
    • Ben-Shachar, D.1    Eshel, G.2    Finberg, J.P.3    Youdim, M.B.4
  • 14
    • 2342573633 scopus 로고    scopus 로고
    • Dopamine toxicity involves mitochondrial complex I inhibition: implications to dopamine-related neuropsychiatric disorders
    • Ben-Shachar D., Zuk R., Gazawi H., Ljubuncic P. Dopamine toxicity involves mitochondrial complex I inhibition: implications to dopamine-related neuropsychiatric disorders. Biochem. Pharmacol. 2004, 67:1965-1974.
    • (2004) Biochem. Pharmacol. , vol.67 , pp. 1965-1974
    • Ben-Shachar, D.1    Zuk, R.2    Gazawi, H.3    Ljubuncic, P.4
  • 16
    • 84928947027 scopus 로고    scopus 로고
    • Three paths to drug discovery in psychiatry
    • Berk M., Nierenberg A.A. Three paths to drug discovery in psychiatry. Am. J. Psychiatry 2015, 172:412-414.
    • (2015) Am. J. Psychiatry , vol.172 , pp. 412-414
    • Berk, M.1    Nierenberg, A.A.2
  • 17
    • 22044436635 scopus 로고    scopus 로고
    • Glutathione depletion in a midbrain-derived immortalized dopaminergic cell line results in limited tyrosine nitration of mitochondrial complex I subunits: implications for Parkinson's disease
    • Bharath S., Andersen J.K. Glutathione depletion in a midbrain-derived immortalized dopaminergic cell line results in limited tyrosine nitration of mitochondrial complex I subunits: implications for Parkinson's disease. Antioxid. Redox Signal 2005, 7:900-910.
    • (2005) Antioxid. Redox Signal , vol.7 , pp. 900-910
    • Bharath, S.1    Andersen, J.K.2
  • 19
    • 33745603712 scopus 로고    scopus 로고
    • S-nitrosothiol inhibition of mitochondrial complex I causes a reversible increase in mitochondrial hydrogen peroxide production
    • Borutaite V., Brown G.C. S-nitrosothiol inhibition of mitochondrial complex I causes a reversible increase in mitochondrial hydrogen peroxide production. Biochim. Biophys. Acta 2006, 1757:562-566.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 562-566
    • Borutaite, V.1    Brown, G.C.2
  • 20
    • 3543008400 scopus 로고    scopus 로고
    • Inhibition of mitochondrial respiratory complex I by nitric oxide, peroxynitrite and S-nitrosothiols
    • Brown G.C., Borutaite V. Inhibition of mitochondrial respiratory complex I by nitric oxide, peroxynitrite and S-nitrosothiols. Biochim. Biophys. Acta 2004, 1658:44-49.
    • (2004) Biochim. Biophys. Acta , vol.1658 , pp. 44-49
    • Brown, G.C.1    Borutaite, V.2
  • 21
    • 84902087370 scopus 로고    scopus 로고
    • An updated meta-analysis of oxidative stress markers in bipolar disorder
    • Brown N.C., Andreazza A.C., Young L.T. An updated meta-analysis of oxidative stress markers in bipolar disorder. Psychiatry Res. 2014, 218:61-68.
    • (2014) Psychiatry Res. , vol.218 , pp. 61-68
    • Brown, N.C.1    Andreazza, A.C.2    Young, L.T.3
  • 22
    • 84873400499 scopus 로고    scopus 로고
    • The relationship between bipolar disorder and type 2 diabetes: more than just co-morbid disorders
    • Calkin C.V., Gardner D.M., Ransom T., Alda M. The relationship between bipolar disorder and type 2 diabetes: more than just co-morbid disorders. Ann. Med. 2013, 45:171-181.
    • (2013) Ann. Med. , vol.45 , pp. 171-181
    • Calkin, C.V.1    Gardner, D.M.2    Ransom, T.3    Alda, M.4
  • 23
    • 84928954768 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in the pathophysiology of bipolar disorder: effects of pharmacotherapy
    • Callaly E., Walder K., Morris G., Maes M., Debnath M., Berk M. Mitochondrial dysfunction in the pathophysiology of bipolar disorder: effects of pharmacotherapy. Mini Rev. Med. Chem. 2015, 15:355-365.
    • (2015) Mini Rev. Med. Chem. , vol.15 , pp. 355-365
    • Callaly, E.1    Walder, K.2    Morris, G.3    Maes, M.4    Debnath, M.5    Berk, M.6
  • 24
    • 84869063791 scopus 로고    scopus 로고
    • Glucose modulates respiratory complex I activity in response to acute mitochondrial dysfunction
    • Cannino G., El-Khoury R., Pirinen M., Hutz B., Rustin P., Jacobs H.T., Dufour E. Glucose modulates respiratory complex I activity in response to acute mitochondrial dysfunction. J. Biol. Chem. 2012, 287:38729-38740.
    • (2012) J. Biol. Chem. , vol.287 , pp. 38729-38740
    • Cannino, G.1    El-Khoury, R.2    Pirinen, M.3    Hutz, B.4    Rustin, P.5    Jacobs, H.T.6    Dufour, E.7
  • 25
    • 0035010364 scopus 로고    scopus 로고
    • Chronic valproate treatment decreases the in vivo turnover of arachidonic acid in brain phospholipids: a possible common effect of mood stabilizers
    • Chang M.C., Contreras M.A., Rosenberger T.A., Rintala J.J., Bell J.M., Rapoport S.I. Chronic valproate treatment decreases the in vivo turnover of arachidonic acid in brain phospholipids: a possible common effect of mood stabilizers. J. Neurochem. 2001, 77:796-803.
    • (2001) J. Neurochem. , vol.77 , pp. 796-803
    • Chang, M.C.1    Contreras, M.A.2    Rosenberger, T.A.3    Rintala, J.J.4    Bell, J.M.5    Rapoport, S.I.6
  • 26
    • 78650126962 scopus 로고    scopus 로고
    • Nitrosylation and nitration of mitochondrial complex I in Parkinson's disease
    • Chinta S.J., Andersen J.K. Nitrosylation and nitration of mitochondrial complex I in Parkinson's disease. Free. Radic. Res. 2011, 45:53-58.
    • (2011) Free. Radic. Res. , vol.45 , pp. 53-58
    • Chinta, S.J.1    Andersen, J.K.2
  • 27
    • 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., Andersen J.K. Reversible inhibition of mitochondrial complex I activity following chronic dopaminergic glutathione depletion in vitro: implications for Parkinson's disease. Free. Radic. Biol. Med. 2006, 41:1442-1448.
    • (2006) Free. Radic. Biol. Med. , vol.41 , pp. 1442-1448
    • Chinta, S.J.1    Andersen, J.K.2
  • 28
    • 33646022514 scopus 로고    scopus 로고
    • Up-regulation of gamma-glutamyl transpeptidase activity following glutathione depletion has a compensatory rather than an inhibitory effect on mitochondrial complex I activity: implications for Parkinson's disease
    • Chinta S.J., Kumar J.M., Zhang H., Forman H.J., Andersen J.K. Up-regulation of gamma-glutamyl transpeptidase activity following glutathione depletion has a compensatory rather than an inhibitory effect on mitochondrial complex I activity: implications for Parkinson's disease. Free. Radic. Biol. Med. 2006, 40:1557-1563.
    • (2006) Free. Radic. Biol. Med. , vol.40 , pp. 1557-1563
    • Chinta, S.J.1    Kumar, J.M.2    Zhang, H.3    Forman, H.J.4    Andersen, J.K.5
  • 29
    • 38449097902 scopus 로고    scopus 로고
    • Inducible alterations of glutathione levels in adult dopaminergic midbrain neurons result in nigrostriatal degeneration
    • Chinta S.J., Kumar M.J., Hsu M., Rajagopalan S., Kaur D., Rane A., Nicholls D.G., Choi J., Andersen J.K. Inducible alterations of glutathione levels in adult dopaminergic midbrain neurons result in nigrostriatal degeneration. J. Neurosci. 2007, 27:13997-14006.
    • (2007) J. Neurosci. , vol.27 , pp. 13997-14006
    • Chinta, S.J.1    Kumar, M.J.2    Hsu, M.3    Rajagopalan, S.4    Kaur, D.5    Rane, A.6    Nicholls, D.G.7    Choi, J.8    Andersen, J.K.9
  • 32
    • 79952959359 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and pathology in bipolar disorder and schizophrenia
    • Clay H.B., Sillivan S., Konradi C. Mitochondrial dysfunction and pathology in bipolar disorder and schizophrenia. Int. J. Dev. Neurosci. 2011, 29:311-324.
    • (2011) Int. J. Dev. Neurosci. , vol.29 , pp. 311-324
    • Clay, H.B.1    Sillivan, S.2    Konradi, C.3
  • 33
    • 0032560572 scopus 로고    scopus 로고
    • Persistent inhibition of cell respiration by nitric oxide: crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione
    • Clementi E., Brown G.C., Feelisch M., Moncada S. Persistent inhibition of cell respiration by nitric oxide: crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione. Proc. Natl. Acad. Sci. U.S.A. 1998, 95:7631-7636.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 7631-7636
    • Clementi, E.1    Brown, G.C.2    Feelisch, M.3    Moncada, S.4
  • 34
    • 0344758310 scopus 로고    scopus 로고
    • Arachidonic acid interaction with the mitochondrial electron transport chain promotes reactive oxygen species generation
    • Cocco T., Di Paola M., Papa S., Lorusso M. Arachidonic acid interaction with the mitochondrial electron transport chain promotes reactive oxygen species generation. Free. Radic. Biol. Med. 1999, 27:51-59.
    • (1999) Free. Radic. Biol. Med. , vol.27 , pp. 51-59
    • Cocco, T.1    Di Paola, M.2    Papa, S.3    Lorusso, M.4
  • 35
    • 0035170284 scopus 로고    scopus 로고
    • Melatonin protects against 6-OHDA-induced neurotoxicity in rats: a role for mitochondrial complex I activity
    • Dabbeni-Sala F., Di Santo S., Franceschini D., Skaper S.D., Giusti P. Melatonin protects against 6-OHDA-induced neurotoxicity in rats: a role for mitochondrial complex I activity. FASEB J. 2001, 15:164-170.
    • (2001) FASEB J. , vol.15 , pp. 164-170
    • Dabbeni-Sala, F.1    Di Santo, S.2    Franceschini, D.3    Skaper, S.D.4    Giusti, P.5
  • 37
    • 84882309276 scopus 로고    scopus 로고
    • Assessing the roles of stimulants/stimulant-like drugs and dopamine-agonists in the treatment of bipolar depression
    • 378-013-0378-z
    • Dell'Osso B., Ketter T.A., Cremaschi L., Spagnolin G., Altamura A.C. Assessing the roles of stimulants/stimulant-like drugs and dopamine-agonists in the treatment of bipolar depression. Curr. Psychiatry Rep. 2013, 15. 378-013-0378-z.
    • (2013) Curr. Psychiatry Rep. , vol.15
    • Dell'Osso, B.1    Ketter, T.A.2    Cremaschi, L.3    Spagnolin, G.4    Altamura, A.C.5
  • 38
    • 84870375907 scopus 로고    scopus 로고
    • Reduction of STAT3 expression induces mitochondrial dysfunction and autophagy in cardiac HL-1 cells
    • Elschami M., Scherr M., Philippens B., Gerardy-Schahn R. Reduction of STAT3 expression induces mitochondrial dysfunction and autophagy in cardiac HL-1 cells. Eur. J. Cell. Biol. 2013, 92:21-29.
    • (2013) Eur. J. Cell. Biol. , vol.92 , pp. 21-29
    • Elschami, M.1    Scherr, M.2    Philippens, B.3    Gerardy-Schahn, R.4
  • 39
    • 84893129567 scopus 로고    scopus 로고
    • Sex hormones and biomarkers of neuroprotection and neurodegeneration: implications for female reproductive events in bipolar disorder
    • Frey B.N., Dias R.S. Sex hormones and biomarkers of neuroprotection and neurodegeneration: implications for female reproductive events in bipolar disorder. Bipolar Disord. 2014, 16:48-57.
    • (2014) Bipolar Disord. , vol.16 , pp. 48-57
    • Frey, B.N.1    Dias, R.S.2
  • 40
    • 84873036367 scopus 로고    scopus 로고
    • IMP2 regulates differentiation potentials of mouse neocortical neural precursor cells
    • Fujii Y., Kishi Y., Gotoh Y. IMP2 regulates differentiation potentials of mouse neocortical neural precursor cells. Genes. Cells 2013, 18:79-89.
    • (2013) Genes. Cells , vol.18 , pp. 79-89
    • Fujii, Y.1    Kishi, Y.2    Gotoh, Y.3
  • 41
    • 84866498143 scopus 로고    scopus 로고
    • DJ-1 protects dopaminergic neurons against rotenone-induced apoptosis by enhancing ERK-dependent mitophagy
    • Gao H., Yang W., Qi Z., Lu L., Duan C., Zhao C., Yang H. DJ-1 protects dopaminergic neurons against rotenone-induced apoptosis by enhancing ERK-dependent mitophagy. J. Mol. Biol. 2012, 423:232-248.
    • (2012) J. Mol. Biol. , vol.423 , pp. 232-248
    • Gao, H.1    Yang, W.2    Qi, Z.3    Lu, L.4    Duan, C.5    Zhao, C.6    Yang, H.7
  • 43
    • 0032511134 scopus 로고    scopus 로고
    • Mechanism of inhibition of mitochondrial respiratory complex I by 6-hydroxydopamine and its prevention by desferrioxamine
    • Glinka Y., Tipton K.F., Youdim M.B. Mechanism of inhibition of mitochondrial respiratory complex I by 6-hydroxydopamine and its prevention by desferrioxamine. Eur. J. Pharmacol. 1998, 351:121-129.
    • (1998) Eur. J. Pharmacol. , vol.351 , pp. 121-129
    • Glinka, Y.1    Tipton, K.F.2    Youdim, M.B.3
  • 44
    • 0029969350 scopus 로고    scopus 로고
    • Nature of inhibition of mitochondrial respiratory complex I by 6-Hydroxydopamine
    • Glinka Y., Tipton K.F., Youdim M.B. Nature of inhibition of mitochondrial respiratory complex I by 6-Hydroxydopamine. J. Neurochem. 1996, 66:2004-2010.
    • (1996) J. Neurochem. , vol.66 , pp. 2004-2010
    • Glinka, Y.1    Tipton, K.F.2    Youdim, M.B.3
  • 45
    • 0028918841 scopus 로고
    • Inhibition of mitochondrial complexes I and IV by 6-hydroxydopamine
    • Glinka Y.Y., Youdim M.B. Inhibition of mitochondrial complexes I and IV by 6-hydroxydopamine. Eur. J. Pharmacol. 1995, 292:329-332.
    • (1995) Eur. J. Pharmacol. , vol.292 , pp. 329-332
    • Glinka, Y.Y.1    Youdim, M.B.2
  • 47
    • 0018095085 scopus 로고
    • Oxidative pathways for catecholamines in the genesis of neuromelanin and cytotoxic quinones
    • Graham D.G. Oxidative pathways for catecholamines in the genesis of neuromelanin and cytotoxic quinones. Mol. Pharmacol. 1978, 14:633-643.
    • (1978) Mol. Pharmacol. , vol.14 , pp. 633-643
    • Graham, D.G.1
  • 49
    • 0026754574 scopus 로고
    • Reactive oxygen species and the central nervous system
    • Halliwell B. Reactive oxygen species and the central nervous system. J. Neurochem. 1992, 59:1609-1623.
    • (1992) J. Neurochem. , vol.59 , pp. 1609-1623
    • Halliwell, B.1
  • 50
    • 0029933450 scopus 로고    scopus 로고
    • Role of oxidation in the neurotoxic effects of intrastriatal dopamine injections
    • Hastings T.G., Lewis D.A., Zigmond M.J. Role of oxidation in the neurotoxic effects of intrastriatal dopamine injections. Proc. Natl. Acad. Sci. U.S.A. 1996, 93:1956-1961.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 1956-1961
    • Hastings, T.G.1    Lewis, D.A.2    Zigmond, M.J.3
  • 52
    • 0036175622 scopus 로고    scopus 로고
    • Impairment of brain mitochondrial function by reactive nitrogen species: the role of glutathione in dictating susceptibility
    • Heales S.J., Bolanos J.P. Impairment of brain mitochondrial function by reactive nitrogen species: the role of glutathione in dictating susceptibility. Neurochem. Int. 2002, 40:469-474.
    • (2002) Neurochem. Int. , vol.40 , pp. 469-474
    • Heales, S.J.1    Bolanos, J.P.2
  • 53
    • 84878905186 scopus 로고    scopus 로고
    • Mitochondrial complex I
    • Hirst J. Mitochondrial complex I. Annu. Rev. Biochem. 2013, 82:551-575.
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 551-575
    • Hirst, J.1
  • 54
    • 14644416354 scopus 로고    scopus 로고
    • Glutathione depletion resulting in selective mitochondrial complex I inhibition in dopaminergic cells is via an NO-mediated pathway not involving peroxynitrite: implications for Parkinson's disease
    • Hsu M., Srinivas B., Kumar J., Subramanian R., Andersen J. Glutathione depletion resulting in selective mitochondrial complex I inhibition in dopaminergic cells is via an NO-mediated pathway not involving peroxynitrite: implications for Parkinson's disease. J. Neurochem. 2005, 92:1091-1103.
    • (2005) J. Neurochem. , vol.92 , pp. 1091-1103
    • Hsu, M.1    Srinivas, B.2    Kumar, J.3    Subramanian, R.4    Andersen, J.5
  • 55
    • 84866738264 scopus 로고    scopus 로고
    • Differential toxicity of 6-hydroxydopamine in SH-SY5Y human neuroblastoma cells and rat brain mitochondria: protective role of catalase and superoxide dismutase
    • Iglesias-Gonzalez J., Sanchez-Iglesias S., Mendez-Alvarez E., Rose S., Hikima A., Jenner P., Soto-Otero R. Differential toxicity of 6-hydroxydopamine in SH-SY5Y human neuroblastoma cells and rat brain mitochondria: protective role of catalase and superoxide dismutase. Neurochem. Res. 2012, 37:2150-2160.
    • (2012) Neurochem. Res. , vol.37 , pp. 2150-2160
    • Iglesias-Gonzalez, J.1    Sanchez-Iglesias, S.2    Mendez-Alvarez, E.3    Rose, S.4    Hikima, A.5    Jenner, P.6    Soto-Otero, R.7
  • 58
    • 33847283651 scopus 로고    scopus 로고
    • Dopamine but not 3,4-dihydroxy phenylacetic acid (DOPAC) inhibits brain respiratory chain activity by autoxidation and mitochondria catalyzed oxidation to quinone products: implications in Parkinson's disease
    • Jana S., Maiti A.K., Bagh M.B., Banerjee K., Das A., Roy A., Chakrabarti S. Dopamine but not 3,4-dihydroxy phenylacetic acid (DOPAC) inhibits brain respiratory chain activity by autoxidation and mitochondria catalyzed oxidation to quinone products: implications in Parkinson's disease. Brain Res. 2007, 1139:195-200.
    • (2007) Brain Res. , vol.1139 , pp. 195-200
    • Jana, S.1    Maiti, A.K.2    Bagh, M.B.3    Banerjee, K.4    Das, A.5    Roy, A.6    Chakrabarti, S.7
  • 59
    • 79954581538 scopus 로고    scopus 로고
    • Mitochondrial dysfunction mediated by quinone oxidation products of dopamine: Implications in dopamine cytotoxicity and pathogenesis of Parkinson's disease
    • Jana S., Sinha M., Chanda D., Roy T., Banerjee K., Munshi S., Patro B.S., Chakrabarti S. Mitochondrial dysfunction mediated by quinone oxidation products of dopamine: Implications in dopamine cytotoxicity and pathogenesis of Parkinson's disease. Biochim. Biophys. Acta 2011, 1812:663-673.
    • (2011) Biochim. Biophys. Acta , vol.1812 , pp. 663-673
    • Jana, S.1    Sinha, M.2    Chanda, D.3    Roy, T.4    Banerjee, K.5    Munshi, S.6    Patro, B.S.7    Chakrabarti, S.8
  • 61
    • 0034714346 scopus 로고    scopus 로고
    • Glutathione depletion in PC12 results in selective inhibition of mitochondrial complex I activity. Implications for Parkinson's disease
    • Jha N., Jurma O., Lalli G., Liu Y., Pettus E.H., Greenamyre J.T., Liu R.M., Forman H.J., Andersen J.K. Glutathione depletion in PC12 results in selective inhibition of mitochondrial complex I activity. Implications for Parkinson's disease. J. Biol. Chem. 2000, 275:26096-26101.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26096-26101
    • Jha, N.1    Jurma, O.2    Lalli, G.3    Liu, Y.4    Pettus, E.H.5    Greenamyre, J.T.6    Liu, R.M.7    Forman, H.J.8    Andersen, J.K.9
  • 62
    • 0036829579 scopus 로고    scopus 로고
    • Redox analysis of human plasma allows separation of pro-oxidant events of aging from decline in antioxidant defenses
    • Jones D.P., Mody V.C., Carlson J.L., Lynn M.J., Sternberg P. Redox analysis of human plasma allows separation of pro-oxidant events of aging from decline in antioxidant defenses. Free. Radic. Biol. Med. 2002, 33:1290-1300.
    • (2002) Free. Radic. Biol. Med. , vol.33 , pp. 1290-1300
    • Jones, D.P.1    Mody, V.C.2    Carlson, J.L.3    Lynn, M.J.4    Sternberg, P.5
  • 63
    • 36549008295 scopus 로고    scopus 로고
    • Constitutive expression and functional characterization of mitochondrial glutaredoxin (Grx2) in mouse and human brain
    • Karunakaran S., Saeed U., Ramakrishnan S., Koumar R.C., Ravindranath V. Constitutive expression and functional characterization of mitochondrial glutaredoxin (Grx2) in mouse and human brain. Brain Res. 2007, 1185:8-17.
    • (2007) Brain Res. , vol.1185 , pp. 8-17
    • Karunakaran, S.1    Saeed, U.2    Ramakrishnan, S.3    Koumar, R.C.4    Ravindranath, V.5
  • 64
    • 0034280096 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in bipolar disorder
    • Kato T., Kato N. Mitochondrial dysfunction in bipolar disorder. Bipolar Disord. 2000, 2:180-190.
    • (2000) Bipolar Disord. , vol.2 , pp. 180-190
    • Kato, T.1    Kato, N.2
  • 65
    • 20444491283 scopus 로고    scopus 로고
    • Inhibition of rat brain mitochondrial electron transport chain activity by dopamine oxidation products during extended in vitro incubation: implications for Parkinson's disease
    • Khan F.H., Sen T., Maiti A.K., Jana S., Chatterjee U., Chakrabarti S. Inhibition of rat brain mitochondrial electron transport chain activity by dopamine oxidation products during extended in vitro incubation: implications for Parkinson's disease. Biochim. Biophys. Acta 2005, 1741:65-74.
    • (2005) Biochim. Biophys. Acta , vol.1741 , pp. 65-74
    • Khan, F.H.1    Sen, T.2    Maiti, A.K.3    Jana, S.4    Chatterjee, U.5    Chakrabarti, S.6
  • 67
    • 79961210760 scopus 로고    scopus 로고
    • Lithium protects against oxidative stress-mediated cell death in alpha-synuclein-overexpressing 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-synuclein-overexpressing in vitro and in vivo models of Parkinson's disease. J. Neurosci. Res. 2011, 89:1666-1675.
    • (2011) J. Neurosci. Res. , vol.89 , pp. 1666-1675
    • Kim, Y.H.1    Rane, A.2    Lussier, S.3    Andersen, J.K.4
  • 68
    • 77955347446 scopus 로고    scopus 로고
    • Sirtuin 3, a new target of PGC-1alpha, plays an important role in the suppression of ROS and mitochondrial biogenesis
    • Kong X., Wang R., Xue Y., Liu X., Zhang H., Chen Y., Fang F., Chang Y. Sirtuin 3, a new target of PGC-1alpha, plays an important role in the suppression of ROS and mitochondrial biogenesis. PLOS One 2010, 5:e11707.
    • (2010) PLOS One , vol.5 , pp. e11707
    • Kong, X.1    Wang, R.2    Xue, Y.3    Liu, X.4    Zhang, H.5    Chen, Y.6    Fang, F.7    Chang, Y.8
  • 73
    • 68949203453 scopus 로고    scopus 로고
    • A disruption in iron-sulfur center biogenesis via inhibition of mitochondrial dithiol glutaredoxin 2 may contribute to mitochondrial and cellular iron dysregulation in mammalian glutathione-depleted dopaminergic cells: implications for Parkinson's disease
    • Lee D.W., Kaur D., Chinta S.J., Rajagopalan S., Andersen J.K. A disruption in iron-sulfur center biogenesis via inhibition of mitochondrial dithiol glutaredoxin 2 may contribute to mitochondrial and cellular iron dysregulation in mammalian glutathione-depleted dopaminergic cells: implications for Parkinson's disease. Antioxid. Redox Signal 2009, 11:2083-2094.
    • (2009) Antioxid. Redox Signal , vol.11 , pp. 2083-2094
    • Lee, D.W.1    Kaur, D.2    Chinta, S.J.3    Rajagopalan, S.4    Andersen, J.K.5
  • 74
    • 0036256644 scopus 로고    scopus 로고
    • What does Stat3 do?
    • Levy D.E., Lee C.K. What does Stat3 do?. J. Clin. Invest 2002, 109:1143-1148.
    • (2002) J. Clin. Invest , vol.109 , pp. 1143-1148
    • Levy, D.E.1    Lee, C.K.2
  • 75
    • 84874931751 scopus 로고    scopus 로고
    • Reactive oxygen species and the free radical theory of aging
    • Liochev S.I. Reactive oxygen species and the free radical theory of aging. Free. Radic. Biol. Med. 2013, 60:1-4.
    • (2013) Free. Radic. Biol. Med. , vol.60 , pp. 1-4
    • Liochev, S.I.1
  • 76
    • 63449093494 scopus 로고    scopus 로고
    • Alpha-Synuclein is differentially expressed in mitochondria from different rat brain regions and dose-dependently down-regulates complex I activity
    • Liu G., Zhang C., Yin J., Li X., Cheng F., Li Y., Yang H., Ueda K., Chan P., Yu S. alpha-Synuclein is differentially expressed in mitochondria from different rat brain regions and dose-dependently down-regulates complex I activity. Neurosci. Lett. 2009, 454:187-192.
    • (2009) Neurosci. Lett. , vol.454 , pp. 187-192
    • Liu, G.1    Zhang, C.2    Yin, J.3    Li, X.4    Cheng, F.5    Li, Y.6    Yang, H.7    Ueda, K.8    Chan, P.9    Yu, S.10
  • 77
    • 77951239770 scopus 로고    scopus 로고
    • The transgenic overexpression of alpha-synuclein and not its related pathology associates with complex I inhibition
    • Loeb V., Yakunin E., Saada A., Sharon R. The transgenic overexpression of alpha-synuclein and not its related pathology associates with complex I inhibition. J. Biol. Chem. 2010, 285:7334-7343.
    • (2010) J. Biol. Chem. , vol.285 , pp. 7334-7343
    • Loeb, V.1    Yakunin, E.2    Saada, A.3    Sharon, R.4
  • 78
    • 0019350010 scopus 로고
    • Coupling of dopamine oxidation (monoamine oxidase activity) to glutathione oxidation via the generation of hydrogen peroxide in rat brain homogenates
    • Maker H.S., Weiss C., Silides D.J., Cohen G. Coupling of dopamine oxidation (monoamine oxidase activity) to glutathione oxidation via the generation of hydrogen peroxide in rat brain homogenates. J. Neurochem. 1981, 36:589-593.
    • (1981) J. Neurochem. , vol.36 , pp. 589-593
    • Maker, H.S.1    Weiss, C.2    Silides, D.J.3    Cohen, G.4
  • 81
    • 0031460696 scopus 로고    scopus 로고
    • Peroxynitrite rapidly permeates phospholipid membranes
    • Marla S.S., Lee J., Groves J.T. Peroxynitrite rapidly permeates phospholipid membranes. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:14243-14248.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 14243-14248
    • Marla, S.S.1    Lee, J.2    Groves, J.T.3
  • 82
    • 70349681975 scopus 로고    scopus 로고
    • Glutathione--a review on its role and significance in Parkinson's disease
    • Martin H.L., Teismann P. Glutathione--a review on its role and significance in Parkinson's disease. FASEB J. 2009, 23:3263-3272.
    • (2009) FASEB J. , vol.23 , pp. 3263-3272
    • Martin, H.L.1    Teismann, P.2
  • 83
    • 0030869160 scopus 로고    scopus 로고
    • Inhibition of complex I by neuroleptics in normal human brain cortex parallels the extrapyramidal toxicity of neuroleptics
    • Maurer I., Moller H.J. Inhibition of complex I by neuroleptics in normal human brain cortex parallels the extrapyramidal toxicity of neuroleptics. Mol. Cell. Biochem. 1997, 174:255-259.
    • (1997) Mol. Cell. Biochem. , vol.174 , pp. 255-259
    • Maurer, I.1    Moller, H.J.2
  • 85
    • 33744518169 scopus 로고    scopus 로고
    • Tamoxifen and estradiol interact with the flavin mononucleotide site of complex I leading to mitochondrial failure
    • Moreira P.I., Custodio J., Moreno A., Oliveira C.R., Santos M.S. Tamoxifen and estradiol interact with the flavin mononucleotide site of complex I leading to mitochondrial failure. J. Biol. Chem. 2006, 281:10143-10152.
    • (2006) J. Biol. Chem. , vol.281 , pp. 10143-10152
    • Moreira, P.I.1    Custodio, J.2    Moreno, A.3    Oliveira, C.R.4    Santos, M.S.5
  • 86
    • 84888206003 scopus 로고    scopus 로고
    • Coenzyme Q10 depletion in medical and neuropsychiatric disorders: potential repercussions and therapeutic implications
    • Morris G., Anderson G., Berk M., Maes M. Coenzyme Q10 depletion in medical and neuropsychiatric disorders: potential repercussions and therapeutic implications. Mol. Neurobiol. 2013, 48:883-903.
    • (2013) Mol. Neurobiol. , vol.48 , pp. 883-903
    • Morris, G.1    Anderson, G.2    Berk, M.3    Maes, M.4
  • 87
    • 84925945862 scopus 로고    scopus 로고
    • The many roads to mitochondrial dysfunction in neuroimmune and neuropsychiatric disorders
    • 68-015-0310-y
    • Morris G., Berk M. The many roads to mitochondrial dysfunction in neuroimmune and neuropsychiatric disorders. BMC Med. 2015, 13. 68-015-0310-y.
    • (2015) BMC Med. , vol.13
    • Morris, G.1    Berk, M.2
  • 91
    • 79953903691 scopus 로고    scopus 로고
    • DJ-1 deficiency in astrocytes selectively enhances mitochondrial Complex I inhibitor-induced neurotoxicity
    • Mullett S.J., Hinkle D.A. DJ-1 deficiency in astrocytes selectively enhances mitochondrial Complex I inhibitor-induced neurotoxicity. J. Neurochem. 2011, 117:375-387.
    • (2011) J. Neurochem. , vol.117 , pp. 375-387
    • Mullett, S.J.1    Hinkle, D.A.2
  • 92
    • 57449089358 scopus 로고    scopus 로고
    • DJ-1 knock-down in astrocytes impairs astrocyte-mediated neuroprotection against rotenone
    • Mullett S.J., Hinkle D.A. DJ-1 knock-down in astrocytes impairs astrocyte-mediated neuroprotection against rotenone. Neurobiol. Dis. 2009, 33:28-36.
    • (2009) Neurobiol. Dis. , vol.33 , pp. 28-36
    • Mullett, S.J.1    Hinkle, D.A.2
  • 93
    • 0141510019 scopus 로고    scopus 로고
    • Oxidative damage to mitochondrial complex I due to peroxynitrite: identification of reactive tyrosines by mass spectrometry
    • Murray J., Taylor S.W., Zhang B., Ghosh S.S., Capaldi R.A. Oxidative damage to mitochondrial complex I due to peroxynitrite: identification of reactive tyrosines by mass spectrometry. J. Biol. Chem. 2003, 278:37223-37230.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37223-37230
    • Murray, J.1    Taylor, S.W.2    Zhang, B.3    Ghosh, S.S.4    Capaldi, R.A.5
  • 96
    • 79960921750 scopus 로고    scopus 로고
    • Nitric oxide and DOPAC-induced cell death: from GSH depletion to mitochondrial energy crisis
    • Nunes C., Barbosa R.M., Almeida L., Laranjinha J. Nitric oxide and DOPAC-induced cell death: from GSH depletion to mitochondrial energy crisis. Mol. Cell. Neurosci. 2011, 48:94-103.
    • (2011) Mol. Cell. Neurosci. , vol.48 , pp. 94-103
    • Nunes, C.1    Barbosa, R.M.2    Almeida, L.3    Laranjinha, J.4
  • 97
    • 0032422401 scopus 로고    scopus 로고
    • Immunohistochemical and ELISA assays for biomarkers of oxidative stress in aging and disease
    • Onorato J.M., Thorpe S.R., Baynes J.W. Immunohistochemical and ELISA assays for biomarkers of oxidative stress in aging and disease. Ann. N. Y. Acad. Sci. 1998, 854:277-290.
    • (1998) Ann. N. Y. Acad. Sci. , vol.854 , pp. 277-290
    • Onorato, J.M.1    Thorpe, S.R.2    Baynes, J.W.3
  • 99
    • 77954927294 scopus 로고    scopus 로고
    • Stoichiometry of STAT3 and mitochondrial proteins: Implications for the regulation of oxidative phosphorylation by protein-protein interactions
    • Phillips D., Reilley M.J., Aponte A.M., Wang G., Boja E., Gucek M., Balaban R.S. Stoichiometry of STAT3 and mitochondrial proteins: Implications for the regulation of oxidative phosphorylation by protein-protein interactions. J. Biol. Chem. 2010, 285:23532-23536.
    • (2010) J. Biol. Chem. , vol.285 , pp. 23532-23536
    • Phillips, D.1    Reilley, M.J.2    Aponte, A.M.3    Wang, G.4    Boja, E.5    Gucek, M.6    Balaban, R.S.7
  • 100
    • 0033621429 scopus 로고    scopus 로고
    • The regulation of mitochondrial oxygen uptake by redox reactions involving nitric oxide and ubiquinol
    • Poderoso J.J., Lisdero C., Schopfer F., Riobo N., Carreras M.C., Cadenas E., Boveris A. The regulation of mitochondrial oxygen uptake by redox reactions involving nitric oxide and ubiquinol. J. Biol. Chem. 1999, 274:37709-37716.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37709-37716
    • Poderoso, J.J.1    Lisdero, C.2    Schopfer, F.3    Riobo, N.4    Carreras, M.C.5    Cadenas, E.6    Boveris, A.7
  • 102
    • 0346458616 scopus 로고    scopus 로고
    • Chronic exposure to nitric oxide alters the free iron pool in endothelial cells: role of mitochondrial respiratory complexes and heat shock proteins
    • Ramachandran A., Ceaser E., Darley-Usmar V.M. Chronic exposure to nitric oxide alters the free iron pool in endothelial cells: role of mitochondrial respiratory complexes and heat shock proteins. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:384-389.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 384-389
    • Ramachandran, A.1    Ceaser, E.2    Darley-Usmar, V.M.3
  • 103
    • 0036301389 scopus 로고    scopus 로고
    • Do lithium and anticonvulsants target the brain arachidonic acid cascade in bipolar disorder?
    • Rapoport S.I., Bosetti F. Do lithium and anticonvulsants target the brain arachidonic acid cascade in bipolar disorder?. Arch. Gen. Psychiatry 2002, 59:592-596.
    • (2002) Arch. Gen. Psychiatry , vol.59 , pp. 592-596
    • Rapoport, S.I.1    Bosetti, F.2
  • 104
    • 84902656355 scopus 로고    scopus 로고
    • Lithium and the other mood stabilizers effective in bipolar disorder target the rat brain arachidonic acid cascade
    • Rapoport S.I. Lithium and the other mood stabilizers effective in bipolar disorder target the rat brain arachidonic acid cascade. ACS Chem. Neurosci. 2014, 5:459-467.
    • (2014) ACS Chem. Neurosci. , vol.5 , pp. 459-467
    • Rapoport, S.I.1
  • 106
    • 0035477926 scopus 로고    scopus 로고
    • Nitric oxide inhibits mitochondrial NADH:ubiquinone reductase activity through peroxynitrite formation
    • Riobo N.A., Clementi E., Melani M., Boveris A., Cadenas E., Moncada S., Poderoso J.J. Nitric oxide inhibits mitochondrial NADH:ubiquinone reductase activity through peroxynitrite formation. Biochem. J. 2001, 359:139-145.
    • (2001) Biochem. J. , vol.359 , pp. 139-145
    • Riobo, N.A.1    Clementi, E.2    Melani, M.3    Boveris, A.4    Cadenas, E.5    Moncada, S.6    Poderoso, J.J.7
  • 107
    • 84903272169 scopus 로고    scopus 로고
    • Altered plasma glutathione levels in bipolar disorder indicates higher oxidative stress; a possible risk factor for illness onset despite normal brain-derived neurotrophic factor (BDNF) levels
    • Rosa A.R., Singh N., Whitaker E., de Brito M., Lewis A.M., Vieta E., Churchill G.C., Geddes J.R., Goodwin G.M. Altered plasma glutathione levels in bipolar disorder indicates higher oxidative stress; a possible risk factor for illness onset despite normal brain-derived neurotrophic factor (BDNF) levels. Psychol. Med. 2014, 1-10.
    • (2014) Psychol. Med. , pp. 1-10
    • Rosa, A.R.1    Singh, N.2    Whitaker, E.3    de Brito, M.4    Lewis, A.M.5    Vieta, E.6    Churchill, G.C.7    Geddes, J.R.8    Goodwin, G.M.9
  • 108
    • 84870762786 scopus 로고    scopus 로고
    • Mitochondrial metabolism, sirtuins, and aging. Cold Spring Harb Perspect
    • Sack M.N., Finkel T. Mitochondrial metabolism, sirtuins, and aging. Cold Spring Harb Perspect. Biol. 2012, 4:a013102. 10.1101/cshperspect.
    • (2012) Biol. , vol.4 , pp. a013102
    • Sack, M.N.1    Finkel, T.2
  • 109
    • 84865581126 scopus 로고    scopus 로고
    • The Parkinson's disease-related genes act in mitochondrial homeostasis
    • Sai Y., Zou Z., Peng K., Dong Z. The Parkinson's disease-related genes act in mitochondrial homeostasis. Neurosci. Biobehav. Rev. 2012, 36:2034-2043.
    • (2012) Neurosci. Biobehav. Rev. , vol.36 , pp. 2034-2043
    • Sai, Y.1    Zou, Z.2    Peng, K.3    Dong, Z.4
  • 110
    • 84896029352 scopus 로고    scopus 로고
    • Neuropathological and neuromorphometric abnormalities in bipolar disorder: view from the medial prefrontal cortical network
    • Savitz J.B., Price J.L., Drevets W.C. Neuropathological and neuromorphometric abnormalities in bipolar disorder: view from the medial prefrontal cortical network. Neurosci. Biobehav. Rev. 2014, 42:132-147.
    • (2014) Neurosci. Biobehav. Rev. , vol.42 , pp. 132-147
    • Savitz, J.B.1    Price, J.L.2    Drevets, W.C.3
  • 111
    • 84870895644 scopus 로고    scopus 로고
    • A fresh look at complex I in microarray data: clues to understanding disease-specific mitochondrial alterations in bipolar disorder
    • Scola G., Kim H.K., Young L.T., Andreazza A.C. A fresh look at complex I in microarray data: clues to understanding disease-specific mitochondrial alterations in bipolar disorder. Biol. Psychiatry 2013, 73:e4-e5.
    • (2013) Biol. Psychiatry , vol.73 , pp. e4-e5
    • Scola, G.1    Kim, H.K.2    Young, L.T.3    Andreazza, A.C.4
  • 112
    • 1842454976 scopus 로고    scopus 로고
    • Does alpha-synuclein modulate dopaminergic synaptic content and tone at the synapse?
    • Sidhu A., Wersinger C., Vernier P. Does alpha-synuclein modulate dopaminergic synaptic content and tone at the synapse?. FASEB J. 2004, 18:637-647.
    • (2004) FASEB J. , vol.18 , pp. 637-647
    • Sidhu, A.1    Wersinger, C.2    Vernier, P.3
  • 113
    • 34247602617 scopus 로고    scopus 로고
    • Decreased level of mitochondrial RNA by glutamate in cultured cortical neurons
    • Sugiyama C., Kuramoto N., Seko K., Yoneda Y., Ogita K. Decreased level of mitochondrial RNA by glutamate in cultured cortical neurons. Neuroreport 2007, 18:827-830.
    • (2007) Neuroreport , vol.18 , pp. 827-830
    • Sugiyama, C.1    Kuramoto, N.2    Seko, K.3    Yoneda, Y.4    Ogita, K.5
  • 116
    • 0026094280 scopus 로고
    • A possible mechanism of mitochondrial dysfunction during cerebral ischemia: inhibition of mitochondrial respiration activity by arachidonic acid
    • Takeuchi Y., Morii H., Tamura M., Hayaishi O., Watanabe Y. A possible mechanism of mitochondrial dysfunction during cerebral ischemia: inhibition of mitochondrial respiration activity by arachidonic acid. Arch. Biochem. Biophys. 1991, 289:33-38.
    • (1991) Arch. Biochem. Biophys. , vol.289 , pp. 33-38
    • Takeuchi, Y.1    Morii, H.2    Tamura, M.3    Hayaishi, O.4    Watanabe, Y.5
  • 117
    • 0037490142 scopus 로고    scopus 로고
    • Reversible glutathionylation of complex I increases mitochondrial superoxide formation
    • Taylor E.R., Hurrell F., Shannon R.J., Lin T.K., Hirst J., Murphy M.P. Reversible glutathionylation of complex I increases mitochondrial superoxide formation. J. Biol. Chem. 2003, 278:19603-19610.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19603-19610
    • Taylor, E.R.1    Hurrell, F.2    Shannon, R.J.3    Lin, T.K.4    Hirst, J.5    Murphy, M.P.6
  • 120
    • 84887436276 scopus 로고    scopus 로고
    • SIRT3: A Central Regulator of Mitochondrial Adaptation in Health and Disease
    • Weir H.J., Lane J.D., Balthasar N. SIRT3: A Central Regulator of Mitochondrial Adaptation in Health and Disease. Genes. Cancer 2013, 4:118-124.
    • (2013) Genes. Cancer , vol.4 , pp. 118-124
    • Weir, H.J.1    Lane, J.D.2    Balthasar, N.3
  • 121
    • 0034531055 scopus 로고    scopus 로고
    • The economic burden of bipolar disease
    • Woods S.W. The economic burden of bipolar disease. J. Clin. Psychiatry 2000, 61(Supp 13):38-41.
    • (2000) J. Clin. Psychiatry , vol.61 , pp. 38-41
    • Woods, S.W.1
  • 122
    • 0036169830 scopus 로고    scopus 로고
    • Selective nitration of mitochondrial complex I by peroxynitrite: involvement in mitochondria dysfunction and cell death of dopaminergic SH-SY5Y cells
    • Yamamoto T., Maruyama W., Kato Y., Yi H., Shamoto-Nagai M., Tanaka M., Sato Y., Naoi M. Selective nitration of mitochondrial complex I by peroxynitrite: involvement in mitochondria dysfunction and cell death of dopaminergic SH-SY5Y cells. J. Neural Transm. 2002, 109:1-13.
    • (2002) J. Neural Transm. , vol.109 , pp. 1-13
    • Yamamoto, T.1    Maruyama, W.2    Kato, Y.3    Yi, H.4    Shamoto-Nagai, M.5    Tanaka, M.6    Sato, Y.7    Naoi, M.8


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