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Volumn 55, Issue , 2013, Pages 101-114

Mitochondria targeted therapeutic approaches in Parkinson's and Huntington's diseases

Author keywords

Co Q10; Creatine; Huntington's disease; Mitochondrial dysfunction; Neurodegenerative diseases; Parkinson's disease; PGC 1 ; Sirtuins

Indexed keywords

1,2,3,6 TETRAHYDRO 1 METHYL 4 PHENYLPYRIDINE; ANTIOXIDANT; BEZAFIBRATE; CELL NUCLEUS DNA; CHAPERONE; CREATINE; FENAZAQUIN; FENPYROXIMATE; HUNTINGTIN; HYBRID PROTEIN; LEUCINE RICH REPEAT KINASE 2; MITOCHONDRIAL DNA; MORTALIN; NITRIC OXIDE SYNTHASE; OXIDOREDUCTASE INHIBITOR; PARKIN; PEPTIDE; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PYRIDABEN; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); RESVERATROL; ROTENONE; SIRTUIN; SIRTUIN 1; TEBUNFENPYRAD; TRICHLOROETHYLENE; UBIDECARENONE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84875679362     PISSN: 10447431     EISSN: 10959327     Source Type: Journal    
DOI: 10.1016/j.mcn.2012.11.011     Document Type: Article
Times cited : (120)

References (199)
  • 1
    • 25444474703 scopus 로고    scopus 로고
    • Mitochondria take center stage in aging and neurodegeneration
    • Beal M.F. Mitochondria take center stage in aging and neurodegeneration. Ann. Neurol. 2005, 58:495-505.
    • (2005) Ann. Neurol. , vol.58 , pp. 495-505
    • Beal, M.F.1
  • 2
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin M.T., Beal M.F. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 2006, 443:787-795.
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 3
    • 0020680904 scopus 로고
    • Chronic parkinsonism in humans due to a product of meperidine-analog synthesis
    • Langston J.W., Ballard P., Tetrud J.W., Irwin I. Chronic parkinsonism in humans due to a product of meperidine-analog synthesis. Science 1983, 219:979-980.
    • (1983) Science , vol.219 , pp. 979-980
    • Langston, J.W.1    Ballard, P.2    Tetrud, J.W.3    Irwin, I.4
  • 4
    • 0021799202 scopus 로고
    • The clinical syndrome of striatal dopamine deficiency. Parkinsonism induced by 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)
    • Burns R.S., LeWitt P.A., Ebert M.H., Pakkenberg H., Kopin I.J. The clinical syndrome of striatal dopamine deficiency. Parkinsonism induced by 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). N. Engl. J. Med. 1985, 312:1418-1421.
    • (1985) N. Engl. J. Med. , vol.312 , pp. 1418-1421
    • Burns, R.S.1    LeWitt, P.A.2    Ebert, M.H.3    Pakkenberg, H.4    Kopin, I.J.5
  • 5
    • 57649171115 scopus 로고    scopus 로고
    • Mitochondrial approaches for neuroprotection
    • Chaturvedi R.K., Beal M.F. Mitochondrial approaches for neuroprotection. Ann. N. Y. Acad. Sci. 2008, 1147:395-412.
    • (2008) Ann. N. Y. Acad. Sci. , vol.1147 , pp. 395-412
    • Chaturvedi, R.K.1    Beal, M.F.2
  • 6
    • 29644447278 scopus 로고    scopus 로고
    • Rotenone model of Parkinson disease: multiple brain mitochondria dysfunctions after short term systemic rotenone intoxication
    • Panov A., Dikalov S., Shalbuyeva N., Taylor G., Sherer T., Greenamyre J.T. Rotenone model of Parkinson disease: multiple brain mitochondria dysfunctions after short term systemic rotenone intoxication. J. Biol. Chem. 2005, 280:42026-42035.
    • (2005) J. Biol. Chem. , vol.280 , pp. 42026-42035
    • Panov, A.1    Dikalov, S.2    Shalbuyeva, N.3    Taylor, G.4    Sherer, T.5    Greenamyre, J.T.6
  • 7
    • 66249144714 scopus 로고    scopus 로고
    • Chronic, low-dose rotenone reproduces Lewy neurites found in early stages of Parkinson's disease, reduces mitochondrial movement and slowly kills differentiated SH-SY5Y neural cells
    • Borland M.K., Trimmer P.A., Rubinstein J.D., Keeney P.M., Mohanakumar K., Liu L., Bennett J.P. Chronic, low-dose rotenone reproduces Lewy neurites found in early stages of Parkinson's disease, reduces mitochondrial movement and slowly kills differentiated SH-SY5Y neural cells. Mol. Neurodegener. 2008, 3:21.
    • (2008) Mol. Neurodegener. , vol.3 , pp. 21
    • Borland, M.K.1    Trimmer, P.A.2    Rubinstein, J.D.3    Keeney, P.M.4    Mohanakumar, K.5    Liu, L.6    Bennett, J.P.7
  • 8
    • 34249788747 scopus 로고    scopus 로고
    • Pesticides and impairment of mitochondrial function in relation with the parkinsonian syndrome
    • Gomez C., Bandez M.J., Navarro A. Pesticides and impairment of mitochondrial function in relation with the parkinsonian syndrome. Front. Biosci. 2007, 12:1079-1093.
    • (2007) Front. Biosci. , vol.12 , pp. 1079-1093
    • Gomez, C.1    Bandez, M.J.2    Navarro, A.3
  • 9
    • 0031859395 scopus 로고    scopus 로고
    • Mitochondrial DNA transmission of the mitochondrial defect in Parkinson's disease
    • Gu M., Cooper J.M., Taanman J.W., Schapira A.H. Mitochondrial DNA transmission of the mitochondrial defect in Parkinson's disease. Ann. Neurol. 1998, 44:177-186.
    • (1998) Ann. Neurol. , vol.44 , pp. 177-186
    • Gu, M.1    Cooper, J.M.2    Taanman, J.W.3    Schapira, A.H.4
  • 10
    • 71549164305 scopus 로고    scopus 로고
    • Cybrid models of Parkinson's disease show variable mitochondrial biogenesis and genotype-respiration relationships
    • Keeney P.M., Dunham L.D., Quigley C.K., Morton S.L., Bergquist K.E., Bennett J.P. Cybrid models of Parkinson's disease show variable mitochondrial biogenesis and genotype-respiration relationships. Exp. Neurol. 2009, 220:374-382.
    • (2009) Exp. Neurol. , vol.220 , pp. 374-382
    • Keeney, P.M.1    Dunham, L.D.2    Quigley, C.K.3    Morton, S.L.4    Bergquist, K.E.5    Bennett, J.P.6
  • 11
    • 67649806929 scopus 로고    scopus 로고
    • The cybrid model of sporadic Parkinson's disease
    • Trimmer P.A., Bennett J.P. The cybrid model of sporadic Parkinson's disease. Exp. Neurol. 2009, 218:320-325.
    • (2009) Exp. Neurol. , vol.218 , pp. 320-325
    • Trimmer, P.A.1    Bennett, J.P.2
  • 12
    • 79952205241 scopus 로고    scopus 로고
    • Direct regulation of complex I by mitochondrial MEF2D is disrupted in a mouse model of Parkinson disease and in human patients
    • She H., Yang Q., Shepherd K., Smith Y., Miller G., Testa C., Mao Z. Direct regulation of complex I by mitochondrial MEF2D is disrupted in a mouse model of Parkinson disease and in human patients. J. Clin. Invest. 2011, 121:930-940.
    • (2011) J. Clin. Invest. , vol.121 , pp. 930-940
    • She, H.1    Yang, Q.2    Shepherd, K.3    Smith, Y.4    Miller, G.5    Testa, C.6    Mao, Z.7
  • 17
    • 0028854722 scopus 로고
    • Point mutations of mitochondrial genome in Parkinson's disease
    • Ikebe S., Tanaka M., Ozawa T. Point mutations of mitochondrial genome in Parkinson's disease. Brain Res. Mol. Brain Res. 1995, 28:281-295.
    • (1995) Brain Res. Mol. Brain Res. , vol.28 , pp. 281-295
    • Ikebe, S.1    Tanaka, M.2    Ozawa, T.3
  • 19
    • 0033544323 scopus 로고    scopus 로고
    • Familial multisystem degeneration with parkinsonism associated with the 11778 mitochondrial DNA mutation
    • Simon D.K., Pulst S.M., Sutton J.P., Browne S.E., Beal M.F., Johns D.R. Familial multisystem degeneration with parkinsonism associated with the 11778 mitochondrial DNA mutation. Neurology 1999, 53:1787-1793.
    • (1999) Neurology , vol.53 , pp. 1787-1793
    • Simon, D.K.1    Pulst, S.M.2    Sutton, J.P.3    Browne, S.E.4    Beal, M.F.5    Johns, D.R.6
  • 20
    • 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., Khrapko K. Mitochondrial DNA deletions are abundant and cause functional impairment in aged human substantia nigra neurons. Nat. Genet. 2006, 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
  • 23
    • 33745028132 scopus 로고    scopus 로고
    • The role of mitochondria in inherited neurodegenerative diseases
    • Kwong J.Q., Beal M.F., Manfredi G. The role of mitochondria in inherited neurodegenerative diseases. J. Neurochem. 2006, 97:1659-1675.
    • (2006) J. Neurochem. , vol.97 , pp. 1659-1675
    • Kwong, J.Q.1    Beal, M.F.2    Manfredi, G.3
  • 25
    • 44049099669 scopus 로고    scopus 로고
    • Mitochondrial import and accumulation of alpha-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain
    • Devi L., Raghavendran V., Prabhu B.M., Avadhani N.G., Anandatheerthavarada H.K. Mitochondrial import and accumulation of alpha-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain. J. Biol. Chem. 2008, 283:9089-9100.
    • (2008) J. Biol. Chem. , vol.283 , pp. 9089-9100
    • Devi, L.1    Raghavendran, V.2    Prabhu, B.M.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5
  • 26
    • 47849083301 scopus 로고    scopus 로고
    • Quantitative proteomics of a presymptomatic A53T alpha-synuclein Drosophila model of Parkinson disease
    • Xun Z., Sowell R.A., Kaufman T.C., Clemmer D.E. Quantitative proteomics of a presymptomatic A53T alpha-synuclein Drosophila model of Parkinson disease. Mol. Cell. Proteomics 2008, 7:1191-1203.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1191-1203
    • Xun, Z.1    Sowell, R.A.2    Kaufman, T.C.3    Clemmer, D.E.4
  • 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., Masliah E. Enhanced substantia nigra mitochondrial pathology in human alpha-synuclein transgenic mice after treatment with MPTP. Exp. Neurol. 2004, 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
  • 35
    • 49649097747 scopus 로고    scopus 로고
    • Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress
    • Gautier C.A., Kitada T., Shen J. Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:11364-11369.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 11364-11369
    • Gautier, C.A.1    Kitada, T.2    Shen, J.3
  • 37
    • 34548021452 scopus 로고    scopus 로고
    • Drosophila DJ-1 mutants are sensitive to oxidative stress and show reduced lifespan and motor deficits
    • Lavara-Culebras E., Paricio N. Drosophila DJ-1 mutants are sensitive to oxidative stress and show reduced lifespan and motor deficits. Gene 2007, 400:158-165.
    • (2007) Gene , vol.400 , pp. 158-165
    • Lavara-Culebras, E.1    Paricio, N.2
  • 42
    • 1542348209 scopus 로고    scopus 로고
    • The energetics of Huntington's disease
    • Browne S.E., Beal M.F. The energetics of Huntington's disease. Neurochem. Res. 2004, 29:531-546.
    • (2004) Neurochem. Res. , vol.29 , pp. 531-546
    • Browne, S.E.1    Beal, M.F.2
  • 43
    • 0033965329 scopus 로고    scopus 로고
    • Higher sedentary energy expenditure in patients with Huntington's disease
    • Pratley R.E., Salbe A.D., Ravussin E., Caviness J.N. Higher sedentary energy expenditure in patients with Huntington's disease. Ann. Neurol. 2000, 47:64-70.
    • (2000) Ann. Neurol. , vol.47 , pp. 64-70
    • Pratley, R.E.1    Salbe, A.D.2    Ravussin, E.3    Caviness, J.N.4
  • 50
    • 0027741301 scopus 로고
    • Evidence for impairment of energy metabolism in vivo in Huntington's disease using localized 1H NMR spectroscopy
    • Jenkins B.G., Koroshetz W.J., Beal M.F., Rosen B.R. Evidence for impairment of energy metabolism in vivo in Huntington's disease using localized 1H NMR spectroscopy. Neurology 1993, 43:2689-2695.
    • (1993) Neurology , vol.43 , pp. 2689-2695
    • Jenkins, B.G.1    Koroshetz, W.J.2    Beal, M.F.3    Rosen, B.R.4
  • 51
    • 0031044805 scopus 로고    scopus 로고
    • Energy metabolism defects in Huntington's disease and effects of coenzyme Q10
    • Koroshetz W.J., Jenkins B.G., Rosen B.R., Beal M.F. Energy metabolism defects in Huntington's disease and effects of coenzyme Q10. Ann. Neurol. 1997, 41:160-165.
    • (1997) Ann. Neurol. , vol.41 , pp. 160-165
    • Koroshetz, W.J.1    Jenkins, B.G.2    Rosen, B.R.3    Beal, M.F.4
  • 52
    • 0033914747 scopus 로고    scopus 로고
    • Abnormal in vivo skeletal muscle energy metabolism in Huntington's disease and dentatorubropallidoluysian atrophy
    • Lodi R., Schapira A.H., Manners D., Styles P., Wood N.W., Taylor D.J., Warner T.T. Abnormal in vivo skeletal muscle energy metabolism in Huntington's disease and dentatorubropallidoluysian atrophy. Ann. Neurol. 2000, 48:72-76.
    • (2000) Ann. Neurol. , vol.48 , pp. 72-76
    • Lodi, R.1    Schapira, A.H.2    Manners, D.3    Styles, P.4    Wood, N.W.5    Taylor, D.J.6    Warner, T.T.7
  • 58
    • 24744444740 scopus 로고    scopus 로고
    • Mitochondrial respiration and ATP production are significantly impaired in striatal cells expressing mutant huntingtin
    • Milakovic T., Johnson G.V. Mitochondrial respiration and ATP production are significantly impaired in striatal cells expressing mutant huntingtin. J. Biol. Chem. 2005, 280:30773-30782.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30773-30782
    • Milakovic, T.1    Johnson, G.V.2
  • 59
    • 0027204154 scopus 로고
    • Age-dependent striatal excitotoxic lesions produced by the endogenous mitochondrial inhibitor malonate
    • Beal M.F., Brouillet E., Jenkins B., Henshaw R., Rosen B., Hyman B.T. Age-dependent striatal excitotoxic lesions produced by the endogenous mitochondrial inhibitor malonate. J. Neurochem. 1993, 61:1147-1150.
    • (1993) J. Neurochem. , vol.61 , pp. 1147-1150
    • Beal, M.F.1    Brouillet, E.2    Jenkins, B.3    Henshaw, R.4    Rosen, B.5    Hyman, B.T.6
  • 61
    • 0026357457 scopus 로고
    • 3-Nitropropionic acid-exogenous animal neurotoxin and possible human striatal toxin
    • Ludolph A.C., He F., Spencer P.S., Hammerstad J., Sabri M. 3-Nitropropionic acid-exogenous animal neurotoxin and possible human striatal toxin. Can. J. Neurol. Sci. 1991, 18:492-498.
    • (1991) Can. J. Neurol. Sci. , vol.18 , pp. 492-498
    • Ludolph, A.C.1    He, F.2    Spencer, P.S.3    Hammerstad, J.4    Sabri, M.5
  • 63
    • 37549045045 scopus 로고    scopus 로고
    • Huntington's disease and mitochondrial DNA deletions: event or regular mechanism for mutant huntingtin protein and CAG repeats expansion?!
    • Banoei M.M., Houshmand M., Panahi M.S., Shariati P., Rostami M., Manshadi M.D., Majidizadeh T. Huntington's disease and mitochondrial DNA deletions: event or regular mechanism for mutant huntingtin protein and CAG repeats expansion?!. Cell. Mol. Neurobiol. 2007, 27:867-875.
    • (2007) Cell. Mol. Neurobiol. , vol.27 , pp. 867-875
    • Banoei, M.M.1    Houshmand, M.2    Panahi, M.S.3    Shariati, P.4    Rostami, M.5    Manshadi, M.D.6    Majidizadeh, T.7
  • 69
    • 33947200596 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Huntington's disease: the bioenergetics of isolated and in situ mitochondria from transgenic mice
    • Oliveira J.M., Jekabsons M.B., Chen S., Lin A., Rego A.C., Goncalves J., Ellerby L.M., Nicholls D.G. Mitochondrial dysfunction in Huntington's disease: the bioenergetics of isolated and in situ mitochondria from transgenic mice. J. Neurochem. 2007, 101:241-249.
    • (2007) J. Neurochem. , vol.101 , pp. 241-249
    • Oliveira, J.M.1    Jekabsons, M.B.2    Chen, S.3    Lin, A.4    Rego, A.C.5    Goncalves, J.6    Ellerby, L.M.7    Nicholls, D.G.8
  • 70
    • 79551518229 scopus 로고    scopus 로고
    • Energy deficit in Huntington disease: why it matters
    • Mochel F., Haller R.G. Energy deficit in Huntington disease: why it matters. J. Clin. Invest. 2011, 121:493-499.
    • (2011) J. Clin. Invest. , vol.121 , pp. 493-499
    • Mochel, F.1    Haller, R.G.2
  • 71
    • 3543141113 scopus 로고    scopus 로고
    • Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release
    • Choo Y.S., Johnson G.V., MacDonald M., Detloff P.J., Lesort M. Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release. Hum. Mol. Genet. 2004, 13:1407-1420.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1407-1420
    • Choo, Y.S.1    Johnson, G.V.2    MacDonald, M.3    Detloff, P.J.4    Lesort, M.5
  • 76
    • 67349247037 scopus 로고    scopus 로고
    • Mitochondrial structural and functional dynamics in Huntington's disease
    • Reddy P.H., Mao P., Manczak M. Mitochondrial structural and functional dynamics in Huntington's disease. Brain Res. Rev. 2009, 61:33-48.
    • (2009) Brain Res. Rev. , vol.61 , pp. 33-48
    • Reddy, P.H.1    Mao, P.2    Manczak, M.3
  • 77
    • 33646136884 scopus 로고    scopus 로고
    • Mutant huntingtin aggregates impair mitochondrial movement and trafficking in cortical neurons
    • Chang D.T., Rintoul G.L., Pandipati S., Reynolds I.J. Mutant huntingtin aggregates impair mitochondrial movement and trafficking in cortical neurons. Neurobiol. Dis. 2006, 22:388-400.
    • (2006) Neurobiol. Dis. , vol.22 , pp. 388-400
    • Chang, D.T.1    Rintoul, G.L.2    Pandipati, S.3    Reynolds, I.J.4
  • 79
    • 79952585486 scopus 로고    scopus 로고
    • Abnormal mitochondrial dynamics, mitochondrial loss and mutant huntingtin oligomers in Huntington's disease: implications for selective neuronal damage
    • Shirendeb U., Reddy A.P., Manczak M., Calkins M.J., Mao P., Tagle D.A., Reddy P.H. Abnormal mitochondrial dynamics, mitochondrial loss and mutant huntingtin oligomers in Huntington's disease: implications for selective neuronal damage. Hum. Mol. Genet. 2011.
    • (2011) Hum. Mol. Genet.
    • Shirendeb, U.1    Reddy, A.P.2    Manczak, M.3    Calkins, M.J.4    Mao, P.5    Tagle, D.A.6    Reddy, P.H.7
  • 81
    • 58949099388 scopus 로고    scopus 로고
    • Effects of overexpression of huntingtin proteins on mitochondrial integrity
    • Wang H., Lim P.J., Karbowski M., Monteiro M.J. Effects of overexpression of huntingtin proteins on mitochondrial integrity. Hum. Mol. Genet. 2009, 18:737-752.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 737-752
    • Wang, H.1    Lim, P.J.2    Karbowski, M.3    Monteiro, M.J.4
  • 84
    • 84860836982 scopus 로고    scopus 로고
    • Light and electron microscopic characterization of the evolution of cellular pathology in the Hdh((CAG)150) Huntington's disease knock-in mouse
    • Bayram-Weston Z., Torres E.M., Jones L., Dunnett S.B., Brooks S.P. Light and electron microscopic characterization of the evolution of cellular pathology in the Hdh((CAG)150) Huntington's disease knock-in mouse. Brain Res. Bull. 2011.
    • (2011) Brain Res. Bull.
    • Bayram-Weston, Z.1    Torres, E.M.2    Jones, L.3    Dunnett, S.B.4    Brooks, S.P.5
  • 86
    • 14244264746 scopus 로고    scopus 로고
    • Ca2+-induced permeability transition in human lymphoblastoid cell mitochondria from normal and Huntington's disease individuals
    • Panov A.V., Lund S., Greenamyre J.T. Ca2+-induced permeability transition in human lymphoblastoid cell mitochondria from normal and Huntington's disease individuals. Mol. Cell. Biochem. 2005, 269:143-152.
    • (2005) Mol. Cell. Biochem. , vol.269 , pp. 143-152
    • Panov, A.V.1    Lund, S.2    Greenamyre, J.T.3
  • 89
    • 33845933438 scopus 로고    scopus 로고
    • Mutant huntingtin expression induces mitochondrial calcium handling defects in clonal striatal cells: functional consequences
    • Milakovic T., Quintanilla R.A., Johnson G.V. Mutant huntingtin expression induces mitochondrial calcium handling defects in clonal striatal cells: functional consequences. J. Biol. Chem. 2006, 281:34785-34795.
    • (2006) J. Biol. Chem. , vol.281 , pp. 34785-34795
    • Milakovic, T.1    Quintanilla, R.A.2    Johnson, G.V.3
  • 90
    • 41949126549 scopus 로고    scopus 로고
    • Calcium homeostasis and mitochondrial dysfunction in striatal neurons of Huntington disease
    • Lim D., Fedrizzi L., Tartari M., Zuccato C., Cattaneo E., Brini M., Carafoli E. Calcium homeostasis and mitochondrial dysfunction in striatal neurons of Huntington disease. J. Biol. Chem. 2008, 283:5780-5789.
    • (2008) J. Biol. Chem. , vol.283 , pp. 5780-5789
    • Lim, D.1    Fedrizzi, L.2    Tartari, M.3    Zuccato, C.4    Cattaneo, E.5    Brini, M.6    Carafoli, E.7
  • 92
    • 0037408279 scopus 로고    scopus 로고
    • Transcriptional abnormalities in Huntington disease
    • Sugars K.L., Rubinsztein D.C. Transcriptional abnormalities in Huntington disease. Trends Genet. 2003, 19:233-238.
    • (2003) Trends Genet. , vol.19 , pp. 233-238
    • Sugars, K.L.1    Rubinsztein, D.C.2
  • 93
    • 35348877164 scopus 로고    scopus 로고
    • Transcriptional signatures in Huntington's disease
    • Cha J.H. Transcriptional signatures in Huntington's disease. Prog. Neurobiol. 2007, 83:228-248.
    • (2007) Prog. Neurobiol. , vol.83 , pp. 228-248
    • Cha, J.H.1
  • 99
    • 1042289730 scopus 로고    scopus 로고
    • Decreased cAMP response element-mediated transcription: an early event in exon 1 and full-length cell models of Huntington's disease that contributes to polyglutamine pathogenesis
    • Sugars K.L., Brown R., Cook L.J., Swartz J., Rubinsztein D.C. Decreased cAMP response element-mediated transcription: an early event in exon 1 and full-length cell models of Huntington's disease that contributes to polyglutamine pathogenesis. J. Biol. Chem. 2004, 279:4988-4999.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4988-4999
    • Sugars, K.L.1    Brown, R.2    Cook, L.J.3    Swartz, J.4    Rubinsztein, D.C.5
  • 101
    • 77955017449 scopus 로고    scopus 로고
    • Impairment of PGC-1alpha expression, neuropathology and hepatic steatosis in a transgenic mouse model of Huntington's disease following chronic energy deprivation
    • Chaturvedi R.K., Calingasan N.Y., Yang L., Hennessey T., Johri A., Beal M.F. Impairment of PGC-1alpha expression, neuropathology and hepatic steatosis in a transgenic mouse model of Huntington's disease following chronic energy deprivation. Hum. Mol. Genet. 2010, 19:3190-3205.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 3190-3205
    • Chaturvedi, R.K.1    Calingasan, N.Y.2    Yang, L.3    Hennessey, T.4    Johri, A.5    Beal, M.F.6
  • 103
    • 33749042331 scopus 로고    scopus 로고
    • Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration
    • Cui L., Jeong H., Borovecki F., Parkhurst C.N., Tanese N., Krainc D. Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration. Cell 2006, 127:59-69.
    • (2006) Cell , vol.127 , pp. 59-69
    • Cui, L.1    Jeong, H.2    Borovecki, F.3    Parkhurst, C.N.4    Tanese, N.5    Krainc, D.6
  • 104
    • 24144463983 scopus 로고    scopus 로고
    • Metabolic control through the PGC-1 family of transcription coactivators
    • Lin J., Handschin C., Spiegelman B.M. Metabolic control through the PGC-1 family of transcription coactivators. Cell Metab. 2005, 1:361-370.
    • (2005) Cell Metab. , vol.1 , pp. 361-370
    • Lin, J.1    Handschin, C.2    Spiegelman, B.M.3
  • 105
    • 51649110738 scopus 로고    scopus 로고
    • PPAR: a therapeutic target in Parkinson's disease
    • Chaturvedi R.K., Beal M.F. PPAR: a therapeutic target in Parkinson's disease. J. Neurochem. 2008, 106:506-518.
    • (2008) J. Neurochem. , vol.106 , pp. 506-518
    • Chaturvedi, R.K.1    Beal, M.F.2
  • 107
    • 33750462349 scopus 로고    scopus 로고
    • PGC-1alpha, a new therapeutic target in Huntington's disease?
    • McGill J.K., Beal M.F. PGC-1alpha, a new therapeutic target in Huntington's disease?. Cell 2006, 127:465-468.
    • (2006) Cell , vol.127 , pp. 465-468
    • McGill, J.K.1    Beal, M.F.2
  • 111
    • 80052809265 scopus 로고    scopus 로고
    • Neuroprotective effects of creatine
    • Beal M.F. Neuroprotective effects of creatine. Amino Acids 2011, 40:1305-1313.
    • (2011) Amino Acids , vol.40 , pp. 1305-1313
    • Beal, M.F.1
  • 112
    • 65249129156 scopus 로고    scopus 로고
    • Creatine and its potential therapeutic value for targeting cellular energy impairment in neurodegenerative diseases
    • Adhihetty P.J., Beal M.F. Creatine and its potential therapeutic value for targeting cellular energy impairment in neurodegenerative diseases. Neuromolecular Med 2008, 10:275-290.
    • (2008) Neuromolecular Med , vol.10 , pp. 275-290
    • Adhihetty, P.J.1    Beal, M.F.2
  • 114
    • 4344680646 scopus 로고    scopus 로고
    • Additive neuroprotective effects of creatine and a cyclooxygenase 2 inhibitor against dopamine depletion in the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) mouse model of Parkinson's disease
    • Klivenyi P., Gardian G., Calingasan N.Y., Yang L., Beal M.F. Additive neuroprotective effects of creatine and a cyclooxygenase 2 inhibitor against dopamine depletion in the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) mouse model of Parkinson's disease. J. Mol. Neurosci. 2003, 21:191-198.
    • (2003) J. Mol. Neurosci. , vol.21 , pp. 191-198
    • Klivenyi, P.1    Gardian, G.2    Calingasan, N.Y.3    Yang, L.4    Beal, M.F.5
  • 116
    • 0038115294 scopus 로고    scopus 로고
    • Creatine therapy provides neuroprotection after onset of clinical symptoms in Huntington's disease transgenic mice
    • Dedeoglu A., Kubilus J.K., Yang L., Ferrante K.L., Hersch S.M., Beal M.F., Ferrante R.J. Creatine therapy provides neuroprotection after onset of clinical symptoms in Huntington's disease transgenic mice. J. Neurochem. 2003, 85:1359-1367.
    • (2003) J. Neurochem. , vol.85 , pp. 1359-1367
    • Dedeoglu, A.1    Kubilus, J.K.2    Yang, L.3    Ferrante, K.L.4    Hersch, S.M.5    Beal, M.F.6    Ferrante, R.J.7
  • 118
    • 65549091910 scopus 로고    scopus 로고
    • Combination therapy with coenzyme Q10 and creatine produces additive neuroprotective effects in models of Parkinson's and Huntington's diseases
    • Yang L., Calingasan N.Y., Wille E.J., Cormier K., Smith K., Ferrante R.J., Beal M.F. Combination therapy with coenzyme Q10 and creatine produces additive neuroprotective effects in models of Parkinson's and Huntington's diseases. J. Neurochem. 2009, 109:1427-1439.
    • (2009) J. Neurochem. , vol.109 , pp. 1427-1439
    • Yang, L.1    Calingasan, N.Y.2    Wille, E.J.3    Cormier, K.4    Smith, K.5    Ferrante, R.J.6    Beal, M.F.7
  • 120
    • 41349108666 scopus 로고    scopus 로고
    • Long-term creatine supplementation is safe in aged patients with Parkinson disease
    • Bender A., Samtleben W., Elstner M., Klopstock T. Long-term creatine supplementation is safe in aged patients with Parkinson disease. Nutr. Res. 2008, 28:172-178.
    • (2008) Nutr. Res. , vol.28 , pp. 172-178
    • Bender, A.1    Samtleben, W.2    Elstner, M.3    Klopstock, T.4
  • 121
    • 33846948238 scopus 로고    scopus 로고
    • Resistance training with creatine monohydrate improves upper-body strength in patients with Parkinson disease: a randomized trial
    • Hass C.J., Collins M.A., Juncos J.L. Resistance training with creatine monohydrate improves upper-body strength in patients with Parkinson disease: a randomized trial. Neurorehabil. Neural Repair 2007, 21:107-115.
    • (2007) Neurorehabil. Neural Repair , vol.21 , pp. 107-115
    • Hass, C.J.1    Collins, M.A.2    Juncos, J.L.3
  • 122
    • 33645894705 scopus 로고    scopus 로고
    • A randomized, double-blind, futility clinical trial of creatine and minocycline in early Parkinson disease
    • A randomized, double-blind, futility clinical trial of creatine and minocycline in early Parkinson disease. Neurology 2006, 66:664-671.
    • (2006) Neurology , vol.66 , pp. 664-671
  • 123
    • 44649153832 scopus 로고    scopus 로고
    • A pilot clinical trial of creatine and minocycline in early Parkinson disease: 18-month results
    • Investigators N.N.-P. A pilot clinical trial of creatine and minocycline in early Parkinson disease: 18-month results. Clin. Neuropharmacol. 2008, 31:141-150.
    • (2008) Clin. Neuropharmacol. , vol.31 , pp. 141-150
    • Investigators, N.N.-P.1
  • 124
    • 34147177574 scopus 로고    scopus 로고
    • Clinical research. Testing a novel strategy against Parkinson's disease
    • Couzin J. Clinical research. Testing a novel strategy against Parkinson's disease. Science 2007, 315:1778.
    • (2007) Science , vol.315 , pp. 1778
    • Couzin, J.1
  • 126
    • 0037379314 scopus 로고    scopus 로고
    • Bioenergetic approaches for neuroprotection in Parkinson's disease
    • (discussion S47-38; 2003)
    • Beal M.F. Bioenergetic approaches for neuroprotection in Parkinson's disease. Ann. Neurol. 2003, 53(Suppl. 3):S39-S47. (discussion S47-38; 2003).
    • (2003) Ann. Neurol. , vol.53 , Issue.SUPPL. 3
    • Beal, M.F.1
  • 127
    • 0028978106 scopus 로고
    • Coenzyme Q10 and nicotinamide and a free radical spin trap protect against MPTP neurotoxicity
    • Schulz J.B., Henshaw D.R., Matthews R.T., Beal M.F. Coenzyme Q10 and nicotinamide and a free radical spin trap protect against MPTP neurotoxicity. Exp. Neurol. 1995, 132:279-283.
    • (1995) Exp. Neurol. , vol.132 , pp. 279-283
    • Schulz, J.B.1    Henshaw, D.R.2    Matthews, R.T.3    Beal, M.F.4
  • 128
    • 0031594295 scopus 로고    scopus 로고
    • Coenzyme Q10 attenuates the 1-methyl-4-phenyl-1,2,3, tetrahydropyridine (MPTP) induced loss of striatal dopamine and dopaminergic axons in aged mice
    • Beal M.F., Matthews R.T., Tieleman A., Shults C.W. Coenzyme Q10 attenuates the 1-methyl-4-phenyl-1,2,3, tetrahydropyridine (MPTP) induced loss of striatal dopamine and dopaminergic axons in aged mice. Brain Res. 1998, 783:109-114.
    • (1998) Brain Res. , vol.783 , pp. 109-114
    • Beal, M.F.1    Matthews, R.T.2    Tieleman, A.3    Shults, C.W.4
  • 133
    • 0035960544 scopus 로고    scopus 로고
    • Coenzyme Q10 and remacemide hydrochloride ameliorate motor deficits in a Huntington's disease transgenic mouse model
    • Schilling G., Coonfield M.L., Ross C.A., Borchelt D.R. Coenzyme Q10 and remacemide hydrochloride ameliorate motor deficits in a Huntington's disease transgenic mouse model. Neurosci. Lett. 2001, 315:149-153.
    • (2001) Neurosci. Lett. , vol.315 , pp. 149-153
    • Schilling, G.1    Coonfield, M.L.2    Ross, C.A.3    Borchelt, D.R.4
  • 135
    • 85009226418 scopus 로고    scopus 로고
    • A randomized, placebo-controlled trial of coenzyme Q10 and remacemide in Huntington's disease
    • A randomized, placebo-controlled trial of coenzyme Q10 and remacemide in Huntington's disease. Neurology 2001, 57:397-404.
    • (2001) Neurology , vol.57 , pp. 397-404
  • 136
    • 0345451597 scopus 로고    scopus 로고
    • Absorption, tolerability, and effects on mitochondrial activity of oral coenzyme Q10 in parkinsonian patients
    • Shults C.W., Beal M.F., Fontaine D., Nakano K., Haas R.H. Absorption, tolerability, and effects on mitochondrial activity of oral coenzyme Q10 in parkinsonian patients. Neurology 1998, 50:793-795.
    • (1998) Neurology , vol.50 , pp. 793-795
    • Shults, C.W.1    Beal, M.F.2    Fontaine, D.3    Nakano, K.4    Haas, R.H.5
  • 138
    • 0037426566 scopus 로고    scopus 로고
    • Coenzyme Q10 supplementation provides mild symptomatic benefit in patients with Parkinson's disease
    • Muller T., Buttner T., Gholipour A.F., Kuhn W. Coenzyme Q10 supplementation provides mild symptomatic benefit in patients with Parkinson's disease. Neurosci. Lett. 2003, 341:201-204.
    • (2003) Neurosci. Lett. , vol.341 , pp. 201-204
    • Muller, T.1    Buttner, T.2    Gholipour, A.F.3    Kuhn, W.4
  • 139
    • 0041783516 scopus 로고    scopus 로고
    • The effect of coenzyme Q10 therapy in Parkinson disease could be symptomatic
    • (author reply 1172-1173)
    • Horstink M.W., van Engelen B.G. The effect of coenzyme Q10 therapy in Parkinson disease could be symptomatic. Arch. Neurol. 2003, 60:1170-1172. (author reply 1172-1173).
    • (2003) Arch. Neurol. , vol.60 , pp. 1170-1172
    • Horstink, M.W.1    Van Engelen, B.G.2
  • 140
    • 36649005196 scopus 로고    scopus 로고
    • Coenzyme Q10 in Parkinson's disease. Symptomatic or neuroprotective effects?
    • Storch A. Coenzyme Q10 in Parkinson's disease. Symptomatic or neuroprotective effects?. Nervenarzt 2007, 78:1378-1382.
    • (2007) Nervenarzt , vol.78 , pp. 1378-1382
    • Storch, A.1
  • 142
    • 3042717908 scopus 로고    scopus 로고
    • Pilot trial of high dosages of coenzyme Q10 in patients with Parkinson's disease
    • Shults C.W., Flint Beal M., Song D., Fontaine D. Pilot trial of high dosages of coenzyme Q10 in patients with Parkinson's disease. Exp. Neurol. 2004, 188:491-494.
    • (2004) Exp. Neurol. , vol.188 , pp. 491-494
    • Shults, C.W.1    Flint Beal, M.2    Song, D.3    Fontaine, D.4
  • 143
    • 33846115045 scopus 로고    scopus 로고
    • A randomized clinical trial of coenzyme Q10 and GPI-1485 in early Parkinson disease
    • NINDS-NETPD
    • NINDS-NETPD A randomized clinical trial of coenzyme Q10 and GPI-1485 in early Parkinson disease. Neurology 2007, 68:20-28.
    • (2007) Neurology , vol.68 , pp. 20-28
  • 144
    • 84860695796 scopus 로고    scopus 로고
    • PGC-1alpha at the intersection of bioenergetics regulation and neuron function: From Huntington's disease to Parkinson's disease and beyond
    • Tsunemi T., La Spada A.R. PGC-1alpha at the intersection of bioenergetics regulation and neuron function: From Huntington's disease to Parkinson's disease and beyond. Prog. Neurobiol. 2012, 97:142-151.
    • (2012) Prog. Neurobiol. , vol.97 , pp. 142-151
    • Tsunemi, T.1    La Spada, A.R.2
  • 145
    • 61849093278 scopus 로고    scopus 로고
    • Adipose tissue dysfunction tracks disease progression in two Huntington's disease mouse models
    • Phan J., Hickey M.A., Zhang P., Chesselet M.F., Reue K. Adipose tissue dysfunction tracks disease progression in two Huntington's disease mouse models. Hum. Mol. Genet. 2009, 18:1006-1016.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 1006-1016
    • Phan, J.1    Hickey, M.A.2    Zhang, P.3    Chesselet, M.F.4    Reue, K.5
  • 150
    • 84863011541 scopus 로고    scopus 로고
    • Pharmacologic activation of mitochondrial biogenesis exerts widespread beneficial effects in a transgenic mouse model of Huntington's disease
    • Johri A., Calingasan N.Y., Hennessey T.M., Sharma A., Yang L., Wille E., Chandra A., Beal M.F. Pharmacologic activation of mitochondrial biogenesis exerts widespread beneficial effects in a transgenic mouse model of Huntington's disease. Hum. Mol. Genet. 2012, 21:1124-1137.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1124-1137
    • Johri, A.1    Calingasan, N.Y.2    Hennessey, T.M.3    Sharma, A.4    Yang, L.5    Wille, E.6    Chandra, A.7    Beal, M.F.8
  • 151
    • 81955162873 scopus 로고    scopus 로고
    • PPARgamma rescue of the mitochondrial dysfunction in Huntington's disease
    • Chiang M.C., Chern Y., Huang R.N. PPARgamma rescue of the mitochondrial dysfunction in Huntington's disease. Neurobiol. Dis. 2012, 45:322-328.
    • (2012) Neurobiol. Dis. , vol.45 , pp. 322-328
    • Chiang, M.C.1    Chern, Y.2    Huang, R.N.3
  • 152
    • 42449092519 scopus 로고    scopus 로고
    • Gene expression-based screening identifies microtubule inhibitors as inducers of PGC-1alpha and oxidative phosphorylation
    • Arany Z., Wagner B.K., Ma Y., Chinsomboon J., Laznik D., Spiegelman B.M. Gene expression-based screening identifies microtubule inhibitors as inducers of PGC-1alpha and oxidative phosphorylation. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:4721-4726.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 4721-4726
    • Arany, Z.1    Wagner, B.K.2    Ma, Y.3    Chinsomboon, J.4    Laznik, D.5    Spiegelman, B.M.6
  • 153
    • 84863620242 scopus 로고    scopus 로고
    • Activating mitochondrial regulator PGC-1alpha expression by astrocytic NGF is a therapeutic strategy for Huntington's disease
    • Chen L.W., Horng L.Y., Wu C.L., Sung H.C., Wu R.T. Activating mitochondrial regulator PGC-1alpha expression by astrocytic NGF is a therapeutic strategy for Huntington's disease. Neuropharmacology 2012.
    • (2012) Neuropharmacology
    • Chen, L.W.1    Horng, L.Y.2    Wu, C.L.3    Sung, H.C.4    Wu, R.T.5
  • 154
    • 0141621061 scopus 로고    scopus 로고
    • NF-E2-related factor-2 mediates neuroprotection against mitochondrial complex I inhibitors and increased concentrations of intracellular calcium in primary cortical neurons
    • Lee J.M., Shih A.Y., Murphy T.H., Johnson J.A. NF-E2-related factor-2 mediates neuroprotection against mitochondrial complex I inhibitors and increased concentrations of intracellular calcium in primary cortical neurons. J. Biol. Chem. 2003, 278:37948-37956.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37948-37956
    • Lee, J.M.1    Shih, A.Y.2    Murphy, T.H.3    Johnson, J.A.4
  • 155
    • 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., Murphy T.H. Induction of the Nrf2-driven antioxidant response confers neuroprotection during mitochondrial stress in vivo. J. Biol. Chem. 2005, 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
  • 156
    • 68949213947 scopus 로고    scopus 로고
    • Mitochondria targeted peptides protect against 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine neurotoxicity
    • Yang L., Zhao K., Calingasan N.Y., Luo G., Szeto H.H., Beal M.F. Mitochondria targeted peptides protect against 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine neurotoxicity. Antioxid. Redox Signal. 2009, 11:2095-2104.
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 2095-2104
    • Yang, L.1    Zhao, K.2    Calingasan, N.Y.3    Luo, G.4    Szeto, H.H.5    Beal, M.F.6
  • 157
    • 77953537441 scopus 로고    scopus 로고
    • Triterpenoids CDDO-ethyl amide and CDDO-trifluoroethyl amide improve the behavioral phenotype and brain pathology in a transgenic mouse model of Huntington's disease
    • Stack C., Ho D., Wille E., Calingasan N.Y., Williams C., Liby K., Sporn M., Dumont M., Beal M.F. Triterpenoids CDDO-ethyl amide and CDDO-trifluoroethyl amide improve the behavioral phenotype and brain pathology in a transgenic mouse model of Huntington's disease. Free Radic. Biol. Med. 2010, 49:147-158.
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 147-158
    • Stack, C.1    Ho, D.2    Wille, E.3    Calingasan, N.Y.4    Williams, C.5    Liby, K.6    Sporn, M.7    Dumont, M.8    Beal, M.F.9
  • 159
    • 33748310632 scopus 로고    scopus 로고
    • Effect of resveratrol on 3-nitropropionic acid-induced biochemical and behavioural changes: possible neuroprotective mechanisms
    • Kumar P., Padi S.S., Naidu P.S., Kumar A. Effect of resveratrol on 3-nitropropionic acid-induced biochemical and behavioural changes: possible neuroprotective mechanisms. Behav. Pharmacol. 2006, 17:485-492.
    • (2006) Behav. Pharmacol. , vol.17 , pp. 485-492
    • Kumar, P.1    Padi, S.S.2    Naidu, P.S.3    Kumar, A.4
  • 161
    • 77955660387 scopus 로고    scopus 로고
    • Resveratrol protects against peripheral deficits in a mouse model of Huntington's disease
    • Ho D.J., Calingasan N.Y., Wille E., Dumont M., Beal M.F. Resveratrol protects against peripheral deficits in a mouse model of Huntington's disease. Exp. Neurol. 2010, 225:74-84.
    • (2010) Exp. Neurol. , vol.225 , pp. 74-84
    • Ho, D.J.1    Calingasan, N.Y.2    Wille, E.3    Dumont, M.4    Beal, M.F.5
  • 163
    • 1842533573 scopus 로고    scopus 로고
    • Striatal cells from mutant huntingtin knock-in mice are selectively vulnerable to mitochondrial complex II inhibitor-induced cell death through a non-apoptotic pathway
    • Ruan Q., Lesort M., MacDonald M.E., Johnson G.V. Striatal cells from mutant huntingtin knock-in mice are selectively vulnerable to mitochondrial complex II inhibitor-induced cell death through a non-apoptotic pathway. Hum. Mol. Genet. 2004, 13:669-681.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 669-681
    • Ruan, Q.1    Lesort, M.2    MacDonald, M.E.3    Johnson, G.V.4
  • 165
    • 84855395163 scopus 로고    scopus 로고
    • Mutant huntingtin's interaction with mitochondrial protein Drp1 impairs mitochondrial biogenesis and causes defective axonal transport and synaptic degeneration in Huntington's disease
    • Shirendeb U.P., Calkins M.J., Manczak M., Anekonda V., Dufour B., McBride J.L., Mao P., Reddy P.H. Mutant huntingtin's interaction with mitochondrial protein Drp1 impairs mitochondrial biogenesis and causes defective axonal transport and synaptic degeneration in Huntington's disease. Hum. Mol. Genet. 2012, 21:406-420.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 406-420
    • Shirendeb, U.P.1    Calkins, M.J.2    Manczak, M.3    Anekonda, V.4    Dufour, B.5    McBride, J.L.6    Mao, P.7    Reddy, P.H.8
  • 166
    • 79952585486 scopus 로고    scopus 로고
    • Abnormal mitochondrial dynamics, mitochondrial loss and mutant huntingtin oligomers in Huntington's disease: implications for selective neuronal damage
    • Shirendeb U., Reddy A.P., Manczak M., Calkins M.J., Mao P., Tagle D.A., Reddy P.H. Abnormal mitochondrial dynamics, mitochondrial loss and mutant huntingtin oligomers in Huntington's disease: implications for selective neuronal damage. Hum. Mol. Genet. 2011, 20:1438-1455.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 1438-1455
    • Shirendeb, U.1    Reddy, A.P.2    Manczak, M.3    Calkins, M.J.4    Mao, P.5    Tagle, D.A.6    Reddy, P.H.7
  • 167
    • 29244462838 scopus 로고    scopus 로고
    • In vitro analysis of huntingtin-mediated transcriptional repression reveals multiple transcription factor targets
    • Zhai W., Jeong H., Cui L., Krainc D., Tjian R. In vitro analysis of huntingtin-mediated transcriptional repression reveals multiple transcription factor targets. Cell 2005, 123:1241-1253.
    • (2005) Cell , vol.123 , pp. 1241-1253
    • Zhai, W.1    Jeong, H.2    Cui, L.3    Krainc, D.4    Tjian, R.5
  • 168
  • 169
    • 79954616687 scopus 로고    scopus 로고
    • PARK6 PINK1 mutants are defective in maintaining mitochondrial membrane potential and inhibiting ROS formation of substantia nigra dopaminergic neurons
    • Wang H.L., Chou A.H., Wu A.S., Chen S.Y., Weng Y.H., Kao Y.C., Yeh T.H., Chu P.J., Lu C.S. PARK6 PINK1 mutants are defective in maintaining mitochondrial membrane potential and inhibiting ROS formation of substantia nigra dopaminergic neurons. Biochim. Biophys. Acta 2011, 1812:674-684.
    • (2011) Biochim. Biophys. Acta , vol.1812 , pp. 674-684
    • Wang, H.L.1    Chou, A.H.2    Wu, A.S.3    Chen, S.Y.4    Weng, Y.H.5    Kao, Y.C.6    Yeh, T.H.7    Chu, P.J.8    Lu, C.S.9
  • 170
    • 35349030746 scopus 로고    scopus 로고
    • PINK1 mutants associated with recessive Parkinson's disease are defective in inhibiting mitochondrial release of cytochrome c
    • Wang H.L., Chou A.H., Yeh T.H., Li A.H., Chen Y.L., Kuo Y.L., Tsai S.R., Yu S.T. PINK1 mutants associated with recessive Parkinson's disease are defective in inhibiting mitochondrial release of cytochrome c. Neurobiol. Dis. 2007, 28:216-226.
    • (2007) Neurobiol. Dis. , vol.28 , pp. 216-226
    • Wang, H.L.1    Chou, A.H.2    Yeh, T.H.3    Li, A.H.4    Chen, Y.L.5    Kuo, Y.L.6    Tsai, S.R.7    Yu, S.T.8
  • 181
    • 78049383132 scopus 로고    scopus 로고
    • Mitochondrial alpha-synuclein accumulation impairs complex I function in dopaminergic neurons and results in increased mitophagy in vivo
    • Chinta S.J., Mallajosyula J.K., Rane A., Andersen J.K. Mitochondrial alpha-synuclein accumulation impairs complex I function in dopaminergic neurons and results in increased mitophagy in vivo. Neurosci. Lett. 2010, 486:235-239.
    • (2010) Neurosci. Lett. , vol.486 , pp. 235-239
    • Chinta, S.J.1    Mallajosyula, J.K.2    Rane, A.3    Andersen, J.K.4
  • 182
    • 84863325404 scopus 로고    scopus 로고
    • Alpha-synuclein impairs normal dynamics of mitochondria in cell and animal models of Parkinson's disease
    • Xie W., Chung K.K. Alpha-synuclein impairs normal dynamics of mitochondria in cell and animal models of Parkinson's disease. J. Neurochem. 2012.
    • (2012) J. Neurochem.
    • Xie, W.1    Chung, K.K.2
  • 186
    • 35748954034 scopus 로고    scopus 로고
    • Paraquat induces dopaminergic dysfunction and proteasome impairment in DJ-1-deficient mice
    • Yang W., Chen L., Ding Y., Zhuang X., Kang U.J. Paraquat induces dopaminergic dysfunction and proteasome impairment in DJ-1-deficient mice. Hum. Mol. Genet. 2007, 16:2900-2910.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 2900-2910
    • Yang, W.1    Chen, L.2    Ding, Y.3    Zhuang, X.4    Kang, U.J.5
  • 187
    • 84860539187 scopus 로고    scopus 로고
    • Parkinson's disease-associated DJ-1 mutations impair mitochondrial dynamics and cause mitochondrial dysfunction
    • Wang X., Petrie T.G., Liu Y., Liu J., Fujioka H., Zhu X. Parkinson's disease-associated DJ-1 mutations impair mitochondrial dynamics and cause mitochondrial dysfunction. J. Neurochem. 2012, 121:830-839.
    • (2012) J. Neurochem. , vol.121 , pp. 830-839
    • Wang, X.1    Petrie, T.G.2    Liu, Y.3    Liu, J.4    Fujioka, H.5    Zhu, X.6
  • 190
    • 67650243261 scopus 로고    scopus 로고
    • Parkin-induced mitophagy in the pathogenesis of Parkinson disease
    • Narendra D., Tanaka A., Suen D.F., Youle R.J. Parkin-induced mitophagy in the pathogenesis of Parkinson disease. Autophagy 2009, 5:706-708.
    • (2009) Autophagy , vol.5 , pp. 706-708
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 191
    • 77952326081 scopus 로고    scopus 로고
    • Disease-causing mutations in parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy
    • Lee J.Y., Nagano Y., Taylor J.P., Lim K.L., Yao T.P. Disease-causing mutations in parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy. J. Cell. Biol. 2010, 189:671-679.
    • (2010) J. Cell. Biol. , vol.189 , pp. 671-679
    • Lee, J.Y.1    Nagano, Y.2    Taylor, J.P.3    Lim, K.L.4    Yao, T.P.5
  • 192
    • 79953231682 scopus 로고    scopus 로고
    • Parkin ubiquitinates Drp1 for proteasome-dependent degradation: implication of dysregulated mitochondrial dynamics in Parkinson disease
    • Wang H., Song P., Du L., Tian W., Yue W., Liu M., Li D., Wang B., Zhu Y., Cao C., Zhou J., Chen Q. Parkin ubiquitinates Drp1 for proteasome-dependent degradation: implication of dysregulated mitochondrial dynamics in Parkinson disease. J. Biol. Chem. 2011, 286:11649-11658.
    • (2011) J. Biol. Chem. , vol.286 , pp. 11649-11658
    • Wang, H.1    Song, P.2    Du, L.3    Tian, W.4    Yue, W.5    Liu, M.6    Li, D.7    Wang, B.8    Zhu, Y.9    Cao, C.10    Zhou, J.11    Chen, Q.12
  • 193
    • 79960826207 scopus 로고    scopus 로고
    • The PINK1/Parkin pathway regulates mitochondrial dynamics and function in mammalian hippocampal and dopaminergic neurons
    • Yu W., Sun Y., Guo S., Lu B. The PINK1/Parkin pathway regulates mitochondrial dynamics and function in mammalian hippocampal and dopaminergic neurons. Hum. Mol. Genet. 2011, 20:3227-3240.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 3227-3240
    • Yu, W.1    Sun, Y.2    Guo, S.3    Lu, B.4
  • 194
    • 78650025189 scopus 로고    scopus 로고
    • Mitochondrial impairment in patients with Parkinson disease with the G2019S mutation in LRRK2
    • Mortiboys H., Johansen K.K., Aasly J.O., Bandmann O. Mitochondrial impairment in patients with Parkinson disease with the G2019S mutation in LRRK2. Neurology 2010, 75:2017-2020.
    • (2010) Neurology , vol.75 , pp. 2017-2020
    • Mortiboys, H.1    Johansen, K.K.2    Aasly, J.O.3    Bandmann, O.4
  • 195
    • 84863728713 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 disturbs mitochondrial dynamics via Dynamin-like protein
    • Niu J., Yu M., Wang C., Xu Z. Leucine-rich repeat kinase 2 disturbs mitochondrial dynamics via Dynamin-like protein. J. Neurochem. 2012, 122:650-658.
    • (2012) J. Neurochem. , vol.122 , pp. 650-658
    • Niu, J.1    Yu, M.2    Wang, C.3    Xu, Z.4
  • 196
    • 44649153832 scopus 로고    scopus 로고
    • A pilot clinical trial of creatine and minocycline in early Parkinson disease: 18-month results
    • Investigators., N.N.-P.
    • Investigators., N.N.-P. A pilot clinical trial of creatine and minocycline in early Parkinson disease: 18-month results. Clin. Neuropharmacol. 2008, 31:141-150.
    • (2008) Clin. Neuropharmacol. , vol.31 , pp. 141-150
  • 197
    • 84867693278 scopus 로고    scopus 로고
    • Design innovations and baseline findings in a long-term Parkinson's trial: the national institute of neurological disorders and stroke exploratory trials in Parkinson's Disease Long-Term Study-1
    • Elm J.J. Design innovations and baseline findings in a long-term Parkinson's trial: the national institute of neurological disorders and stroke exploratory trials in Parkinson's Disease Long-Term Study-1. Mov. Disord. 2012, 27:1513-1521.
    • (2012) Mov. Disord. , vol.27 , pp. 1513-1521
    • Elm, J.J.1
  • 198
    • 33846115045 scopus 로고    scopus 로고
    • A randomized clinical trial of coenzyme Q10 and GPI-1485 in early Parkinson disease
    • A randomized clinical trial of coenzyme Q10 and GPI-1485 in early Parkinson disease. Neurology 2007, 68:20-28.
    • (2007) Neurology , vol.68 , pp. 20-28


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