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Volumn 23, Issue 1, 2012, Pages 13-28

Mitochondrial and metabolic-based protective strategies in Huntington's disease: The case of creatine and coenzyme Q

Author keywords

Huntington's disease; metabolic dysfunction; mitochondria; neuroprotection

Indexed keywords

ALPHA TOCOPHEROL; CREATINE; HUNTINGTIN; MITOCHONDRIAL DNA; POLYGLUTAMINE; UBIDECARENONE;

EID: 84860539153     PISSN: 03341763     EISSN: None     Source Type: Journal    
DOI: 10.1515/rns.2011.060     Document Type: Review
Times cited : (20)

References (190)
  • 2
    • 65249129156 scopus 로고    scopus 로고
    • Creatine and its potential therapeutic value for targeting cellular energy impairment in neuro-degenerative diseases
    • Adhihetty, P.J. and Beal, M.F. (2008). Creatine and its potential therapeutic value for targeting cellular energy impairment in neuro-degenerative diseases. Neuromol. Med. 10, 275-290.
    • (2008) Neuromol. Med. , vol.10 , pp. 275-290
    • Adhihetty, P.J.1    Beal, M.F.2
  • 3
    • 49449107322 scopus 로고    scopus 로고
    • Evidence of apoptosis and mitochondrial abnormalities in peripheral blood cells of Huntington's disease patients
    • Almeida, S., Sarmento-Ribeiro, A.B., Januário, C., Rego, A.C., and Oliveira, C.R. (2008). Evidence of apoptosis and mitochondrial abnormalities in peripheral blood cells of Huntington's disease patients. Biochem. Biophys. Res. Commun. 374, 599-603.
    • (2008) Biochem. Biophys. Res. Commun. , vol.374 , pp. 599-603
    • Almeida, S.1    Sarmento-Ribeiro, A.B.2    Januário, C.3    Rego, A.C.4    Oliveira, C.R.5
  • 4
    • 77953951286 scopus 로고    scopus 로고
    • Dysregulation of CREB activation and histone acetylation in 3-nitropropionic acid-treated cortical neurons: Prevention by BDNF and NGF
    • Almeida, S., Cunha-Oliveira, T., Laço, M., Oliveira, C.R., and Rego, A.C. (2010). Dysregulation of CREB activation and histone acetylation in 3-nitropropionic acid-treated cortical neurons: prevention by BDNF and NGF. Neurotox. Res. 17, 399-405.
    • (2010) Neurotox. Res. , Issue.17 , pp. 399-405
    • Almeida, S.1    Cunha-Oliveira, T.2    Laço, M.3    Oliveira, C.R.4    Rego, A.C.5
  • 8
    • 15444363304 scopus 로고    scopus 로고
    • NR2A and NR2B receptor gene variations modify age at onset in Huntington disease
    • DOI 10.1007/s10048-004-0198-8
    • Arning, L., Kraus, P.H., Valentin, S., Saft, C., Andrich, J., and Epplen, J.T. (2005). NR2A and NR2B receptor gene variations modify age at onset in Huntington disease. Neurogenetics 6, 25-28. (Pubitemid 40394827)
    • (2005) Neurogenetics , vol.6 , Issue.1 , pp. 25-28
    • Arning, L.1    Kraus, P.H.2    Valentin, S.3    Saft, C.4    Andrich, J.5    Epplen, J.T.6
  • 9
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • DOI 10.1038/nature02998
    • Arrasate, M., Mitra, S., Schweitzer, E.S., Segal, M.R., and Finkbeiner, S. (2004). Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431, 805-810. (Pubitemid 39434070)
    • (2004) Nature , vol.431 , Issue.7010 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 10
    • 77649110090 scopus 로고    scopus 로고
    • The relationship between uric acid levels and Huntington's disease progression
    • Auinger, P., Kieburtz, K., and McDermott, M.P. (2010). The relationship between uric acid levels and Huntington's disease progression. Mov. Disord. 25, 224-228.
    • (2010) Mov. Disord. , vol.25 , pp. 224-228
    • Auinger, P.1    Kieburtz, K.2    McDermott, M.P.3
  • 14
    • 44449137435 scopus 로고    scopus 로고
    • Antioxidants cannot suppress the lethal phenotype of a Drosophila melanogaster model of Huntington's disease
    • DOI 10.1139/G08-012
    • Bahadorani, S. and Hilliker, A.J. (2008). Antioxidants cannot suppress the lethal phenotype of a Drosophila melanogaster model of Huntington's disease. Genome 51, 392-395. (Pubitemid 351768973)
    • (2008) Genome , vol.51 , Issue.5 , pp. 392-395
    • Bahadorani, S.1    Hilliker, A.J.2
  • 15
    • 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., and Majidizadeh, T. (2007). Huntington's disease and mitochondrial DNA deletions: event or regular mechanism for mutant huntingtin protein and CAG repeats expansion? Cell. Mol. Neurobiol. 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
  • 16
    • 0038701684 scopus 로고    scopus 로고
    • Huntingtin aggregation and toxicity in Huntington's disease
    • DOI 10.1016/S0140-6736(03)13304-1
    • Bates, G. (2003). Huntingtin aggregation and toxicity in Huntington's disease. Lancet 361, 1642-1644. (Pubitemid 36579005)
    • (2003) Lancet , vol.361 , Issue.9369 , pp. 1642-1644
    • Bates, G.1
  • 17
    • 80052809265 scopus 로고    scopus 로고
    • Neuroprotective effects of creatine
    • Beal, M.F. (2011). Neuroprotective effects of creatine. Amino Acids 40, 1305-1313.
    • (2011) Amino Acids , vol.40 , pp. 1305-1313
    • Beal, M.F.1
  • 21
    • 54849422301 scopus 로고    scopus 로고
    • Huntingtin modulates transcription, occupies gene promoters in vivo, and binds directly to DNA in a polyglutamine-dependent manner
    • Benn, C.L., Sun, T., Sadri-Vakili, G., McFarland, K.N., DiRocco, D.P., Yohrling, G.J., Clark, T.W., Bouzou, B., and Cha, J.H. (2008). Huntingtin modulates transcription, occupies gene promoters in vivo, and binds directly to DNA in a polyglutamine-dependent manner. J. Neurosci. 28, 10720-10733.
    • (2008) J. Neurosci. , vol.28 , pp. 10720-10733
    • Benn, C.L.1    Sun, T.2    Sadri-Vakili, G.3    McFarland, K.N.4    Di Rocco, D.P.5    Yohrling, G.J.6    Clark, T.W.7    Bouzou, B.8    Cha, J.H.9
  • 22
    • 4444302167 scopus 로고    scopus 로고
    • Deranged neuronal calcium signaling and Huntington disease
    • DOI 10.1016/j.bbrc.2004.08.035, PII S0006291X04017735
    • Bezprozvanny, I. and Hayden, M.R. (2004). Deranged neuronal calcium signaling and Huntington disease. Biochem. Biophys. Res. Commun. 322, 1310-1317. (Pubitemid 39164659)
    • (2004) Biochemical and Biophysical Research Communications , vol.322 , Issue.4 , pp. 1310-1317
    • Bezprozvanny, I.1    Hayden, M.R.2
  • 25
    • 29144468251 scopus 로고    scopus 로고
    • 3-Nitropropionic acid: A mitochondrial toxin to uncover physiopathological mechanisms underlying striatal degeneration in Huntington's disease
    • DOI 10.1111/j.1471-4159.2005.03515.x
    • Brouillet, E., Jacquard, C., Bizat, N., and Blum, D. (2005). 3-Nitrop-ropionic acid: a mitochondrial toxin to uncover physiopathologi-cal mechanisms underlying striatal degeneration in Huntington's disease. J. Neurochem. 95, 1521-1540. (Pubitemid 41804051)
    • (2005) Journal of Neurochemistry , vol.95 , Issue.6 , pp. 1521-1540
    • Brouillet, E.1    Jacquard, C.2    Bizat, N.3    Blum, D.4
  • 26
    • 57649187103 scopus 로고    scopus 로고
    • Mitochondria and Huntington's disease patho-genesis. Insight from genetic and chemical models
    • Browne, S.E. (2008). Mitochondria and Huntington's disease patho-genesis. Insight from genetic and chemical models. Ann. NY Acad. Sci. 1147, 358-382.
    • (2008) Ann. NY Acad. Sci. , vol.1147 , pp. 358-382
    • Browne, S.E.1
  • 28
    • 3042513691 scopus 로고    scopus 로고
    • Mitochondria dysfunction of Alzheimer's disease cybrids enhances Aβ toxicity
    • DOI 10.1111/j.1471-4159.2004.02438.x
    • Cardoso, S.M., Santana, I., Swerdlow, R.H., and Oliveira, C.R. (2004). Mitochondria dysfunction of Alzheimer's disease cybrids enhances A β toxicity. J. Neurochem. 89, 1417-1426. (Pubitemid 38802663)
    • (2004) Journal of Neurochemistry , vol.89 , Issue.6 , pp. 1417-1426
    • Cardoso, S.M.1    Santana, I.2    Swerdlow, R.H.3    Oliveira, C.R.4
  • 29
    • 0035282594 scopus 로고    scopus 로고
    • Loss of normal huntingtin function: New developments in Huntington's disease research
    • DOI 10.1016/S0166-2236(00)01721-5, PII S0166223600017215
    • Cattaneo, E., Rigamonti, D., Goffredo, D., Zuccato, C., Squitieri, F., and Sipione, S. (2001). Loss of normal huntingtin function: new developments in Huntington's disease research. Trends Neurosci. 24, 182-188. (Pubitemid 32166824)
    • (2001) Trends in Neurosciences , vol.24 , Issue.3 , pp. 182-188
    • Cattaneo, E.1    Rigamonti, D.2    Goffredo, D.3    Zuccato, C.4    Squitieri, F.5    Sipione, S.6
  • 30
    • 28644433087 scopus 로고    scopus 로고
    • Normal huntingtin function: An alternative approach to Huntington's disease
    • DOI 10.1038/nrn1806
    • Cattaneo, E., Zuccato, C., and Tartari, M. (2005). Normal huntingtin function: an alternative approach to Huntington's disease. Nat. Rev. Neurosci. 6, 919-930. (Pubitemid 41753086)
    • (2005) Nature Reviews Neuroscience , vol.6 , Issue.12 , pp. 919-930
    • Cattaneo, E.1    Zuccato, C.2    Tartari, M.3
  • 31
    • 63449090757 scopus 로고    scopus 로고
    • Huntingtin as an essential integrator of intracellular vesicular trafficking
    • Caviston, J.P. and Holzbaur, E.L. (2009). Huntingtin as an essential integrator of intracellular vesicular trafficking. Trends Cell Biol. 19, 147-155.
    • (2009) Trends Cell Biol. , vol.19 , pp. 147-155
    • Caviston, J.P.1    Holzbaur, E.L.2
  • 32
    • 1642387890 scopus 로고    scopus 로고
    • Creatine supplementation increases glucose oxidation and AMPK phosphorylation and reduces lactate production in L6 rat skeletal muscle cells
    • DOI 10.1113/jphysiol.2003.056291
    • Ceddia, R.B. and Sweeney, G. (2004). Creatine supplementation increases glucose oxidation and AMPK phosphorylation and reduces lactate production in L6 rat skeletal muscle cells. J. Physiol. 555, 409-421. (Pubitemid 38380000)
    • (2004) Journal of Physiology , vol.555 , Issue.2 , pp. 409-421
    • Ceddia, R.B.1    Sweeney, G.2
  • 36
    • 0028238418 scopus 로고
    • Platelet-mediated transformation of mtDNA-less human cells: Analysis of phenotypic variability among clones from normal individuals-and complementation behavior of the tRNALys mutation causing myoclonic epilepsy and ragged red fibers
    • Chomyn, A., Lai, S.T., Shakeley, R., Bresolin, N., Scarlato, G., and Attardi, G. (1994). Platelet-mediated transformation of mtDNA-less human cells: analysis of phenotypic variability among clones from normal individuals-and complementation behavior of the tRNALys mutation causing myoclonic epilepsy and ragged red fibers. Am. J. Hum. Genet. 54, 966-974.
    • (1994) Am. J. Hum. Genet. , vol.54 , pp. 966-974
    • Chomyn, A.1    Lai, S.T.2    Shakeley, R.3    Bresolin, N.4    Scarlato, G.5    Attardi, G.6
  • 37
    • 3543141113 scopus 로고    scopus 로고
    • Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release
    • DOI 10.1093/hmg/ddh162
    • Choo, Y.S., Johnson, G.V., MacDonald, M., Detloff, P.J., and Lesort, M. (2004). Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release. Hum. Mol. Genet. 13, 1407-1420. (Pubitemid 39023049)
    • (2004) Human Molecular Genetics , vol.13 , Issue.14 , pp. 1407-1420
    • Choo, Y.S.1    Johnson, G.V.W.2    MacDonald, M.3    Detloff, P.J.4    Lesort, M.5
  • 40
    • 33749042331 scopus 로고    scopus 로고
    • Transcriptional repression of PGC-1α by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration
    • DOI 10.1016/j.cell.2006.09.015, PII S0092867406012050
    • Cui, L., Jeong, H., Borovecki, F., Parkhurst, C.N., Tanese, N., and Krainc, D. (2006). Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neuro-degeneration. Cell 127, 59-69. (Pubitemid 44466642)
    • (2006) Cell , vol.127 , Issue.1 , pp. 59-69
    • Cui, L.1    Jeong, H.2    Borovecki, F.3    Parkhurst, C.N.4    Tanese, N.5    Krainc, D.6
  • 41
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation
    • DOI 10.1016/S0092-8674(00)80513-9
    • Davies, S.W., Turmaine, M., Cozens, B.A., DiFiglia, M., Sharp, A.H., Ross, C.A., Scherzinger, E., Wanker, E.E., Mangiarini, L., and Bates, G.P. (1997). Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 90, 537-548. (Pubitemid 27347243)
    • (1997) Cell , vol.90 , Issue.3 , pp. 537-548
    • Davies, S.W.1    Turmaine, M.2    Cozens, B.A.3    DiFiglia, M.4    Sharp, A.H.5    Ross, C.A.6    Scherzinger, E.7    Wanker, E.E.8    Mangiarini, L.9    Bates, G.P.10
  • 44
    • 33644623231 scopus 로고    scopus 로고
    • Insulin neuroprotection against oxidative stress in cortical neurons-Involvement of uric acid and glutathione antioxidant defenses
    • Duarte, A.I., Santos, M.S., Oliveira, C.R., and Rego, A.C. (2005). Insulin neuroprotection against oxidative stress in cortical neurons-Involvement of uric acid and glutathione antioxidant defenses. Free Radic. Biol. Med. 39, 876-889.
    • (2005) Free Radic. Biol. Med. , vol.39 , pp. 876-889
    • Duarte, A.I.1    Santos, M.S.2    Oliveira, C.R.3    Rego, A.C.4
  • 47
    • 0021927818 scopus 로고
    • Diabetes mellitus in Huntington disease
    • Farrer, L.A. (1985). Diabetes mellitus in Huntington disease. Clin. Genet. 27, 62-67. (Pubitemid 15193407)
    • (1985) Clinical Genetics , vol.27 , Issue.1 , pp. 62-67
    • Farrer, L.A.1
  • 48
    • 30044438329 scopus 로고    scopus 로고
    • P53 tumor suppressor protein regulates the levels of huntingtin gene expression
    • DOI 10.1038/sj.onc.1209021
    • Feng, Z., Jin, S., Zupnick, A., Hoh, J., de Stanchina, E., Lowe, S., Prives, C., and Levine, A.J. (2006). p53 tumor suppressor protein regulates the levels of huntingtin gene expression. Oncogene 25, 1-7. (Pubitemid 43049998)
    • (2006) Oncogene , vol.25 , Issue.1 , pp. 1-7
    • Feng, Z.1    Jin, S.2    Zupnick, A.3    Hoh, J.4    De Stanchina, E.5    Lowe, S.6    Prives, C.7    Levine, A.J.8
  • 53
    • 67650468768 scopus 로고    scopus 로고
    • Wild-type but not mutant hun-tingtin modulates the transcriptional activity of liver X receptors
    • Futter, M., Diekmann, H., Schoenmakers, E., Sadiq, O., Chatterjee, K., and Rubinsztein, D.C. (2009). Wild-type but not mutant hun-tingtin modulates the transcriptional activity of liver X receptors. J. Med. Genet. 46, 438-446.
    • (2009) J. Med. Genet. , vol.46 , pp. 438-446
    • Futter, M.1    Diekmann, H.2    Schoenmakers, E.3    Sadiq, O.4    Chatterjee, K.5    Rubinsztein, D.C.6
  • 54
    • 0342368660 scopus 로고    scopus 로고
    • Proton magnetic resonance spectroscopy of cerebrospinal fluid in neurodegenerative disease: Indication of glial energy impairment in huntington chorea, but not parkinson disease
    • DOI 10.1002/1097-4547(20000615)60:6<779::AID-JNR10>3.0.CO;2-M
    • Gårseth, M., Sonnewald, U., White, L.R., Rød, M., Zwart, J.A., Nygaard, O., and Aasly, J. (2000). Proton magnetic resonance spectroscopy of cerebrospinal fluid in neurodegenerative disease: indication of glial energy impairment in Huntington chorea, but not Parkinson disease. J. Neurosci. Res. 60, 779-782. (Pubitemid 30399549)
    • (2000) Journal of Neuroscience Research , vol.60 , Issue.6 , pp. 779-782
    • Garseth, M.1    Sonnewald, U.2    White, L.R.3    Rod, M.4    Zwart, J.-A.5    Nygaard, O.6    Aasly, J.7
  • 56
    • 45149107487 scopus 로고    scopus 로고
    • Mechanisms of neurodegeneration in Huntington's disease
    • DOI 10.1111/j.1460-9568.2008.06310.x
    • Gil, J.M. and Rego, A.C. (2008). Mechanisms of neurodegeneration in Huntington's disease. Eur. J. Neurosci. 27, 2803-2820. (Pubitemid 351832229)
    • (2008) European Journal of Neuroscience , vol.27 , Issue.11 , pp. 2803-2820
    • Gil, J.M.1    Rego, A.C.2
  • 59
    • 0034994207 scopus 로고    scopus 로고
    • Early degenerative changes in transgenic mice expressing mutant huntingtin involve dendritic abnormalities but no impairment of mitochondrial energy production
    • DOI 10.1006/exnr.2000.7626
    • Guidetti, P., Charles, V., Chen, E.Y., Reddy, P.H., Kordower, J.H., Whetsell, W.O., Schwarcz, R., and Tagle, D.A. (2001). Early degenerative changes in transgenic mice expressing mutant huntingtin involve dendritic abnormalities but no impairment of mitochondrial energy production. Exp. Neurol. 169, 340-350. (Pubitemid 32524428)
    • (2001) Experimental Neurology , vol.169 , Issue.2 , pp. 340-350
    • Guidetti, P.1    Charles, V.2    Chen, E.-Y.3    Reddy P.Hemachandra4    Kordower, J.H.5    Whetsell Jr., W.O.6    Schwarcz, R.7    Tagle, D.A.8
  • 61
    • 79952615363 scopus 로고    scopus 로고
    • Preferential accumulation of N-terminal mutant hunting-tin in the nuclei of striatal neurons is regulated by phosphoryla-tion
    • Havel, L.S., Wang, C.E., Wade, B., Huang, B., Li, S., and Li, X.J. (2011). Preferential accumulation of N-terminal mutant hunting-tin in the nuclei of striatal neurons is regulated by phosphoryla-tion. Hum. Mol. Genet. 20, 1424-1437.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 1424-1437
    • Havel, L.S.1    Wang, C.E.2    Wade, B.3    Huang, B.4    Li, S.5    Li, X.J.6
  • 64
    • 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., and Beal, M.F. (2010). Resveratrol protects against peripheral deficits in a mouse model of Huntington's disease. Exp. Neurol. 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
  • 66
    • 85009226418 scopus 로고    scopus 로고
    • A randomized, placebo-controlled trial of coenzyme Q10 and remacemide in Huntington's disease
    • Huntington Study Group
    • Huntington Study Group. (2001). A randomized, placebo-controlled trial of coenzyme Q10 and remacemide in Huntington's disease. Neurology 57, 397-404.
    • (2001) Neurology , vol.57 , pp. 397-404
  • 67
    • 80054883676 scopus 로고    scopus 로고
    • Modifications of p53 and the DNA damage response in cells expressing mutant form of the protein Huntingtin
    • Illuzzi, J.L., Vickers, C.A., and Kmiec, E.B. (2011). Modifications of p53 and the DNA damage response in cells expressing mutant form of the protein Huntingtin. J. Mol. Neurosci. 45, 256-268.
    • (2011) J. Mol. Neurosci. , vol.45 , pp. 256-268
    • Illuzzi, J.L.1    Vickers, C.A.2    Kmiec, E.B.3
  • 72
    • 0027741301 scopus 로고
    • 1H NMR spectroscopy
    • Jenkins, B.G., Koroshetz, W.J., Beal, M.F., and Rosen, B.R. (1993). Evidence for impairment of energy metabolism in vivo in Huntington's disease using localized 1H NMR spectroscopy. Neurology 43, 2689-2695. (Pubitemid 24004570)
    • (1993) Neurology , vol.43 , Issue.12 , pp. 2689-2695
    • Jenkins, B.G.1    Koroshetz, W.J.2    Beal, M.F.3    Rosen, B.R.4
  • 74
    • 29244483093 scopus 로고    scopus 로고
    • 10 and vitamin E on brain energy metabolism in the animal model of Huntington's disease
    • DOI 10.1016/j.neuint.2005.09.002, PII S0197018605002317
    • Kasparová, S., Sumbalová, Z., Bystrický, P., Kucharská, J., Liptaj, T., Mlynárik, V., and Gvozdjá ková, A. (2006). Effect of coenzyme Q10 and vitamin E on brain energy metabolism in the animal model of Huntington's disease. Neurochem. Int. 48, 93-99. (Pubitemid 41832443)
    • (2006) Neurochemistry International , vol.48 , Issue.2 , pp. 93-99
    • Kasparova, S.1    Sumbalova, Z.2    Bystricky, P.3    Kucharska, J.4    Liptaj, T.5    Mlynarik, V.6    Gvozdjakova, A.7
  • 75
    • 35348880250 scopus 로고    scopus 로고
    • Drug targeting of dysregulated transcription in Huntington's disease
    • DOI 10.1016/j.pneurobio.2007.02.005, PII S0301008207000482, Chromatin Dysfunction in Huntington's Disease
    • Kazantsev, A.G. and Hersch, S.M. (2007). Drug targeting of dys-regulated transcription in Huntington's disease. Prog. Neurobiol. 83, 249-259. (Pubitemid 47588641)
    • (2007) Progress in Neurobiology , vol.83 , Issue.4 , pp. 249-259
    • Kazantsev, A.G.1    Hersch, S.M.2
  • 77
    • 0035940412 scopus 로고    scopus 로고
    • Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpaindependent proteolysis
    • DOI 10.1073/pnas.221451398
    • Kim, Y.J., Yi, Y., Sapp, E., Wang, Y., Cuiffo, B., Kegel, K.B., Qin, Z.H., Aronin, N., and DiFiglia, M. (2001). Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis. Proc. Natl. Acad. Sci. USA 98, 12784-12789. (Pubitemid 33020022)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.22 , pp. 12784-12789
    • Kim, Y.J.1    Yi, Y.2    Sapp, E.3    Wang, Y.4    Cuiffo, B.5    Kegel, K.B.6    Qin, Z.-H.7    Aronin, N.8    DiFiglia, M.9
  • 79
    • 0024448458 scopus 로고
    • Human cells lacking mtDNA: Repopulation with exogenous mitochondria by complementation
    • King, M.P. and Attardi, G. (1989). Human cells lacking mtDNA: repopulation with exogenous mitochondria by complementation. Science 246, 500-503. (Pubitemid 19273941)
    • (1989) Science , vol.246 , Issue.4929 , pp. 500-503
    • King, M.P.1    Attardi, G.2
  • 80
    • 0035115942 scopus 로고    scopus 로고
    • Progression of symptoms in the early and middle stages of Huntington disease
    • Kirkwood, S.C., Su, J.L., Conneally, P., and Foroud, T. (2001). Progression of symptoms in the early and middle stages of Huntington disease. Arch. Neurol. 58, 273-278. (Pubitemid 32163165)
    • (2001) Archives of Neurology , vol.58 , Issue.2 , pp. 273-278
    • Kirkwood, S.C.1    Su, J.L.2    Conneally, P.M.3    Foroud, T.4
  • 87
    • 0022946353 scopus 로고
    • Brain energy metabolism and dopaminergic function in Huntington's disease measured in vivo using positron emission tomography
    • Leenders, K.L., Frackowiak, R.S., Quinn, N., and Marsden, C.D. (1986). Brain energy metabolism and dopaminergic function in Huntington's disease measured in vivo using positron emission tomography. Mov. Disord. 1, 69-77.
    • (1986) Mov. Disord. , vol.1 , pp. 69-77
    • Leenders, K.L.1    Frackowiak, R.S.2    Quinn, N.3    Marsden, C.D.4
  • 88
    • 33847060541 scopus 로고    scopus 로고
    • Mitochondrial complex I: Structure, function, and implications in neurodegeneration
    • Lenaz, G., Baracca, A., Fato, R., Genova, M.L., and Solaini, G. (2006). Mitochondrial complex I: structure, function, and implications in neurodegeneration. Ital. J. Biochem. 55, 232-253.
    • (2006) Ital. J. Biochem. , vol.55 , pp. 232-253
    • Lenaz, G.1    Baracca, A.2    Fato, R.3    Genova, M.L.4    Solaini, G.5
  • 90
    • 1242338856 scopus 로고    scopus 로고
    • Huntingtin-protein interactions and the pathogenesis of Huntington's disease
    • Li, S.H. and Li, X.J. (2004). Huntingtin-protein interactions and the pathogenesis of Huntington's disease. Trends Genet. 20, 146-154.
    • (2004) Trends Genet. , vol.20 , pp. 146-154
    • Li, S.H.1    Li, X.J.2
  • 92
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • DOI 10.1038/nature05292, PII NATURE05292
    • Lin, M.T. and Beal, M.F. (2006). Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443, 787-795. (Pubitemid 44622683)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 94
    • 24144463983 scopus 로고    scopus 로고
    • Metabolic control through the PGC-1 family of transcription coactivators
    • DOI 10.1016/j.cmet.2005.05.004, PII S1550413105001427
    • Lin, J., Handschin, C., and Spiegelman, B.M. (2005). Metabolic control through the PGC-1 family of transcription coactivators. Cell Metab. 1, 361-370. (Pubitemid 43960626)
    • (2005) Cell Metabolism , vol.1 , Issue.6 , pp. 361-370
    • Lin, J.1    Handschin, C.2    Spiegelman, B.M.3
  • 96
    • 0033914747 scopus 로고    scopus 로고
    • Abnormal in vivo skeletal muscle energy metabolism in Huntington's disease and dentatorubropallidoluysian atrophy
    • DOI 10.1002/1531-8249(200007)48:1<72::AID-ANA11>3.0.CO;2-I
    • Lodi, R., Schapira, A.H., Manners, D., Styles, P., Wood, N.W., Taylor, D.J., and Warner, T.T. (2000). Abnormal in vivo skeletal muscle energy metabolism in Huntington's disease and dentatorubropal-lidoluysian atrophy. Ann. Neurol. 48, 72-76. (Pubitemid 30432433)
    • (2000) Annals of Neurology , vol.48 , Issue.1 , pp. 72-76
    • Lodi, R.1    Schapira, A.H.V.2    Manners, D.3    Styles, P.4    Wood, N.W.5    Taylor, D.J.6    Warner, T.T.7
  • 98
    • 71749102014 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in human breast cancer cells and their transmito-chondrial cybrids
    • Ma, Y., Bai, R.K., Trieu, R., and Wong, L.J. (2010). Mitochondrial dysfunction in human breast cancer cells and their transmito-chondrial cybrids. Biochim. Biophys. Acta 1797, 29-37.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 29-37
    • Ma, Y.1    Bai, R.K.2    Trieu, R.3    Wong, L.J.4
  • 100
    • 79957509694 scopus 로고    scopus 로고
    • Mitogen-and stress-activated protein kinase 1-induced neuroprotection in Huntington's disease: Role on chromatin remodeling at the PGC-1-α promoter
    • Martin, E., Betuing, S., Pagès, C., Cambon, K., Auregan, G., Deglon, N., Roze, E., and Caboche, J. (2011a). Mitogen-and stress-activated protein kinase 1-induced neuroprotection in Huntington's disease: role on chromatin remodeling at the PGC-1-α promoter. Hum. Mol. Genet. 20, 2422-2434.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 2422-2434
    • Martin, E.1    Betuing, S.2    Pagès, C.3    Cambon, K.4    Auregan, G.5    Deglon, N.6    Roze, E.7    Caboche, J.8
  • 103
    • 0037197778 scopus 로고    scopus 로고
    • Alteration of nuclear glyceraldehyde-3-phosphate dehydrogenase structure in Huntington's disease fibroblasts
    • DOI 10.1016/S0169-328X(02)00160-2, PII S0169328X02001602
    • Mazzola, J.L. and Sirover, M.A. (2002). Alteration of nuclear glycer-aldehyde-3-phosphate dehydrogenase structure in Huntington's disease fibroblasts. Brain Res. Mol. Brain Res. 100, 95-101. (Pubitemid 34465582)
    • (2002) Molecular Brain Research , vol.100 , Issue.1-2 , pp. 95-101
    • Mazzola, J.L.1    Sirover, M.A.2
  • 105
    • 24744444740 scopus 로고    scopus 로고
    • Mitochondrial respiration and ATP production are significantly impaired in striatal cells expressing mutant huntingtin
    • DOI 10.1074/jbc.M504749200
    • Milakovic, T. and Johnson, G.V. (2005). Mitochondrial respiration and ATP production are significantly impaired in stri-atal cells expressing mutant huntingtin. J. Biol. Chem. 280, 30773-30782. (Pubitemid 41291807)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.35 , pp. 30773-30782
    • Milakovic, T.1    Johnson, G.V.W.2
  • 106
    • 33845933438 scopus 로고    scopus 로고
    • Mutant Huntingtin expression induces mitochondrial calcium handling defects in clonal striatal cells: Functional consequences
    • DOI 10.1074/jbc.M603845200
    • Milakovic, T., Quintanilla, R.A., and Johnson, G.V. (2006). Mutant huntingtin expression induces mitochondrial calcium handling defects in clonal striatal cells: functional consequences. J. Biol. Chem. 281, 34785-34795. (Pubitemid 46036517)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.46 , pp. 34785-34795
    • Milakovic, T.1    Quintanilla, R.A.2    Johnson, G.V.W.3
  • 107
    • 0032860432 scopus 로고    scopus 로고
    • The selective vulnerability of striatopallidal neurons
    • DOI 10.1016/S0301-0082(99)00019-2, PII S0301008299000192
    • Mitchell, I.J., Cooper, A.J., and Griffiths, M.R. (1999). The selective vulnerability of striatopallidal neurons. Prog. Neurobiol. 59, 691-719. (Pubitemid 29457588)
    • (1999) Progress in Neurobiology , vol.59 , Issue.6 , pp. 691-719
    • Mitchell, I.J.1    Cooper, A.J.2    Griffiths, M.R.3
  • 108
    • 79551518229 scopus 로고    scopus 로고
    • Energy deficit in Huntington disease: Why it matters
    • Mochel, F. and Haller, R.G. (2011). Energy deficit in Huntington disease: why it matters. J. Clin. Invest. 121, 493-499.
    • (2011) J. Clin. Invest. , vol.121 , pp. 493-499
    • Mochel, F.1    Haller, R.G.2
  • 109
    • 77950547661 scopus 로고    scopus 로고
    • Formation of polyglutamine inclusions in a wide range of non-CNS tissues in the HdhQ150 knock-in mouse model of Huntington's disease
    • Moffitt, H., McPhail, G.D., Woodman, B., Hobbs, C., and Bates, G.P. (2009). Formation of polyglutamine inclusions in a wide range of non-CNS tissues in the HdhQ150 knock-in mouse model of Huntington's disease. PLoS One 4, e8025.
    • (2009) PLoS One , vol.4
    • Moffitt, H.1    McPhail, G.D.2    Woodman, B.3    Hobbs, C.4    Bates, G.P.5
  • 111
    • 0031447451 scopus 로고    scopus 로고
    • Depletion of mitochondrial DNA by ddC in untransformed human cell lines
    • Nelson, I., Hanna, M.G., Wood, N.W., and Harding, A.E. (1997). Depletion of mitochondrial DNA by ddC in untransformed human cell lines. Somat. Cell Mol. Genet. 23, 287-290. (Pubitemid 28162723)
    • (1997) Somatic Cell and Molecular Genetics , vol.23 , Issue.4 , pp. 287-290
    • Nelson, I.1    Hanna, M.G.2    Wood, N.W.3    Harding, A.E.4
  • 113
    • 0001477910 scopus 로고    scopus 로고
    • Differential effects of creatine depletion on the regulation of enzyme activities and on creatine-stimulated mitochondrial respiration in skeletal muscle, heart, and brain
    • DOI 10.1016/0005-2728(96)00074-6
    • O'Gorman, E., Beutner, G., Wallimann, T., and Brdiczka, D. (1996). Differential effects of creatine depletion on the regulation of enzyme activities and on creatine-stimulated mitochondrial respiration in skeletal muscle, heart, and brain. Biochim. Biophys. Acta 1276, 161-170. (Pubitemid 26308733)
    • (1996) Biochimica et Biophysica Acta - Bioenergetics , vol.1276 , Issue.2 , pp. 161-170
    • O'Gorman, E.1    Beutner, G.2    Wallimann, T.3    Brdiczka, D.4
  • 114
    • 51749107237 scopus 로고    scopus 로고
    • Increased glucose metabolism and ATP level in brain tissue of Huntington's disease transgenic mice
    • Oláh, J., Klivényi, P., Gardián, G., Vécsei, L., Orosz, F., Kovacs, G.G., Westerhoff, H.V., and Ovádi, J. (2008). Increased glucose metabolism and ATP level in brain tissue of Huntington's disease transgenic mice. FEBS J. 275, 4740-4755.
    • (2008) FEBS J. , vol.275 , pp. 4740-4755
    • Oláh, J.1    Klivényi, P.2    Gardián, G.3    Vécsei, L.4    Orosz, F.5    Kovacs, G.G.6    Westerhoff, H.V.7    Ovádi, J.8
  • 115
    • 64149094332 scopus 로고    scopus 로고
    • 2+ buffering differences of intact neurons and astrocytes from cortex and striatum
    • 2+ buffering differences of intact neurons and astrocytes from cortex and striatum. J. Biol. Chem. 284, 5010-5020.
    • (2009) J. Biol. Chem. , vol.284 , pp. 5010-5020
    • Oliveira, J.M.1    Gonçalves, J.2
  • 117
    • 33947200596 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Huntington's disease: The bioenergetics of isolated and in situ mitochondria from transgenic mice
    • DOI 10.1111/j.1471-4159.2006.04361.x
    • Oliveira, J.M., Jekabsons, M.B., Chen, S., Lin, A., Rego, A.C., Gonçalves, J., Ellerby, L.M., and Nicholls, D.G. (2007). Mitochondrial dysfunction in Huntington's disease: the bioener-getics of isolated and in situ mitochondria from transgenic mice. J. Neurochem. 101, 241-249. (Pubitemid 46426480)
    • (2007) Journal of Neurochemistry , vol.101 , Issue.1 , pp. 241-249
    • Oliveira, J.M.A.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
  • 118
    • 77949352928 scopus 로고    scopus 로고
    • Acute polyglutamine expression in inducible mouse model unravels ubiquitin/protea-some system impairment and permanent recovery attributable to aggregate formation
    • Ortega, Z., Díaz-Hernández, M., Maynard, C.J., Hernández, F., Dantuma, N.P., and Lucas, J.J. (2010). Acute polyglutamine expression in inducible mouse model unravels ubiquitin/protea-some system impairment and permanent recovery attributable to aggregate formation. J Neurosci. 30, 3675-3688.
    • (2010) J Neurosci. , vol.30 , pp. 3675-3688
    • Ortega, Z.1    Díaz-Hernández, M.2    Maynard, C.J.3    Hernández, F.4    Dantuma, N.P.5    Lucas, J.J.6
  • 119
    • 0032252708 scopus 로고    scopus 로고
    • Evaluation of morphological changes after treatment with coenzyme Q10 (CoQ10) in endothelin-1 induced experimental ischemia in the rat
    • Ostrowski, R., Piotrowski, P., Pankowska, T., and Smialek, M. (1998). Evaluation of morphological changes after treatment with coenzyme Q10 (CoQ10) in endothelin-1 induced experimental ischemia in the rat. Folia Neuropathol. 36, 185-188. (Pubitemid 128548565)
    • (1998) Folia Neuropathologica , vol.36 , Issue.3 , pp. 185-188
    • Ostrowski, R.P.1    Piotrowski, P.2    Pankowska, T.3    Smialek, M.4
  • 121
    • 0025087726 scopus 로고
    • Evidence for a defect in NADH:ubiquinone oxidoreductase (complex I) in Huntington's disease
    • Parker, W.D., Boyson, S.J., Luder, A.S., and Parks, J.K. (1990). Evidence for a defect in NADH: ubiquinone oxidoreductase (complex I) in Huntington's disease. Neurology 40, 1231-1234. (Pubitemid 20244981)
    • (1990) Neurology , vol.40 , Issue.8 , pp. 1231-1234
    • Parker Jr., W.D.1    Boyson, S.J.2    Luder, A.S.3    Parks, J.K.4
  • 124
    • 33747602312 scopus 로고    scopus 로고
    • Hypothalamic-endocrine aspects in Huntington's disease
    • DOI 10.1111/j.1460-9568.2006.04985.x
    • Petersén, A. and Björkqvist, M. (2006). Hypothalamic- endocrine aspects in Huntington's disease. Eur. J. Neurosci. 24, 961-967. (Pubitemid 44268127)
    • (2006) European Journal of Neuroscience , vol.24 , Issue.4 , pp. 961-967
    • Petersen, A.1    Bjorkqvist, M.2
  • 125
    • 0015521813 scopus 로고
    • Increased frequency of diabetes mellitus in patients with Huntington's chorea
    • Podolsky, S., Leopold, N.A., and Sax, D.S. (1972). Increased frequency of diabetes mellitus in patients with Huntington's chorea. Lancet i, 1356-1358.
    • (1972) Lancet , vol.1 , pp. 1356-1358
    • Podolsky, S.1    Leopold, N.A.2    Sax, D.S.3
  • 129
    • 78650899306 scopus 로고    scopus 로고
    • Platelet mitochondrial complex i and i + III activities do not correlate with cerebral mitochondrial oxi-dative metabolism
    • Powers, W.J., Haas, R.H., Le, T., Videen, T.O., Markham, J., and Perlmutter, J.S. (2011). Platelet mitochondrial complex I and I + III activities do not correlate with cerebral mitochondrial oxi-dative metabolism. J. Cereb. Blood Flow Metab. 31, e1-e5.
    • (2011) J. Cereb. Blood Flow Metab. , vol.31
    • Powers, W.J.1    Haas, R.H.2    Le, T.3    Videen, T.O.4    Markham, J.5    Perlmutter, J.S.6
  • 130
    • 0033010987 scopus 로고    scopus 로고
    • Recent advances in understanding the pathogenesis of Huntington's disease
    • DOI 10.1016/S0166-2236(99)01415-0, PII S0166223699014150
    • Reddy, P.H., Williams, M., and Tagle, D.A. (1999). Recent advances in understanding the pathogenesis of Huntington's disease. Trends Neurosci. 22, 248-255. (Pubitemid 29259990)
    • (1999) Trends in Neurosciences , vol.22 , Issue.6 , pp. 248-255
    • Reddy, P.H.1    Williams, M.2    Tagle, D.A.3
  • 133
    • 0035805504 scopus 로고    scopus 로고
    • Huntingtin's neuroprotective activity occurs via inhibition of procaspase-9 processing
    • Rigamonti, D., Sipione, S., Goffredo, D., Zuccato, C., Fossale, E., and Cattaneo, E. (2001). Huntingtin's neuroprotective activity occurs via inhibition of procaspase-9 processing. J. Biol. Chem. 276, 14545-14548.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14545-14548
    • Rigamonti, D.1    Sipione, S.2    Goffredo, D.3    Zuccato, C.4    Fossale, E.5    Cattaneo, E.6
  • 135
    • 33745233087 scopus 로고    scopus 로고
    • Regulation of intracellular trafficking of huntingtin-associated protein-1 is critical for TrkA protein levels and neurite outgrowth
    • DOI 10.1523/JNEUROSCI.1251-06.2006
    • Rong, J., McGuire, J.R., Fang, Z.H., Sheng, G., Shin, J.Y., Li, S.H., and Li, X.J. (2006). Regulation of intracellular trafficking of huntingtin-associated protein-1 is critical for TrkA protein levels and neurite outgrowth. J. Neurosci. 26, 6019-6030. (Pubitemid 44318368)
    • (2006) Journal of Neuroscience , vol.26 , Issue.22 , pp. 6019-6030
    • Rong, J.1    McGuire, J.R.2    Fang, Z.-H.3    Sheng, G.4    Shin, J.-Y.5    Li, S.-H.6    Li, X.-J.7
  • 136
    • 77957993152 scopus 로고    scopus 로고
    • Mitochondrial-associated metabolic changes and neurodegeneration in Huntington's disease-from clinical features to the bench
    • Rosenstock, T.R., Duarte, A.I., and Rego, A.C. (2010). Mitochondrial-associated metabolic changes and neurodegeneration in Huntington's disease-from clinical features to the bench. Curr. Drug Targets 11, 1218-1236.
    • (2010) Curr. Drug Targets , vol.11 , pp. 1218-1236
    • Rosenstock, T.R.1    Duarte, A.I.2    Rego, A.C.3
  • 137
    • 27644596641 scopus 로고    scopus 로고
    • What is the role of protein aggregation in neurodegeneration?
    • DOI 10.1038/nrm1742, PII N1742
    • Ross, C.A. and Poirier, M.A. (2005). Opinion: What is the role of protein aggregation in neurodegeneration? Nat. Rev. Mol. Cell Biol. 6, 891-898. (Pubitemid 41568738)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.11 , pp. 891-898
    • Ross, C.A.1    Poirier, M.A.2
  • 139
    • 79953232671 scopus 로고    scopus 로고
    • Exercise increases mitochondrial PGC-1alpha content and promotes nuclear-mitochondrial crosstalk to coordinate mitochondrial biogenesis
    • Safdar, A., Little, J.P., Stokl, A.J., Hettinga, B.P., Akhtar, M., and Tarnopolsky, M.A. (2011). Exercise increases mitochondrial PGC-1alpha content and promotes nuclear-mitochondrial crosstalk to coordinate mitochondrial biogenesis. J. Biol. Chem. 286, 10605-10617.
    • (2011) J. Biol. Chem. , vol.286 , pp. 10605-10617
    • Safdar, A.1    Little, J.P.2    Stokl, A.J.3    Hettinga, B.P.4    Akhtar, M.5    Tarnopolsky, M.A.6
  • 141
    • 69949102831 scopus 로고    scopus 로고
    • Huntington's disease: The current state of research with peripheral tissues
    • Sassone, J., Colciago, C., Cislaghi, G., Silani, V., and Ciammola, A. (2009). Huntington's disease: the current state of research with peripheral tissues. Exp. Neurol. 219, 385-397.
    • (2009) Exp. Neurol. , vol.219 , pp. 385-397
    • Sassone, J.1    Colciago, C.2    Cislaghi, G.3    Silani, V.4    Ciammola, A.5
  • 143
    • 0032851595 scopus 로고    scopus 로고
    • Increased apoptosis of Huntington disease lymphoblasts associated with repeat length-dependent mitochondrial depolarization
    • DOI 10.1038/13518
    • Sawa, A., Wiegand, G.W., Cooper, J., Margolis, R.L., Sharp, A.H., Lawler, J.F., Jr., Greenamyre, J.T., Snyder, S.H., and Ross, C.A. (1999). Increased apoptosis of Huntington disease lymphoblasts associated with repeat length-dependent mitochondrial depolarization. Nat. Med. 5, 1194-1198. (Pubitemid 29474426)
    • (1999) Nature Medicine , vol.5 , Issue.10 , pp. 1194-1198
    • Sawa, A.1    Wiegand, G.W.2    Cooper, J.3    Margolis, R.L.4    Sharp, A.H.5    Lawler Jr., J.F.6    Greenamyre, J.T.7    Snyder, S.H.8    Ross, C.A.9
  • 144
    • 0028997519 scopus 로고
    • Mitochondria: Beyond oxidative phosphorylation
    • Schatz, G. (1995). Mitochondria: beyond oxidative phosphorylation. Biochim. Biophys. Acta 1271, 123-126.
    • (1995) Biochim. Biophys. Acta , vol.1271 , pp. 123-126
    • Schatz, G.1
  • 145
    • 0035960544 scopus 로고    scopus 로고
    • Coenzyme Q10 and remacemide hydrochloride ameliorate motor deficits in a Huntington's disease transgenic mouse model
    • DOI 10.1016/S0304-3940(01)02326-6, PII S0304394001023266
    • Schilling, G., Coonfield, M.L., Ross, C.A., and Borchelt, D.R. (2001). Coenzyme Q10 and remacemide hydrochloride ameliorate motor deficits in a Huntington's disease transgenic mouse model. Neurosci. Lett. 315, 149-153. (Pubitemid 33079072)
    • (2001) Neuroscience Letters , vol.315 , Issue.3 , pp. 149-153
    • Schilling, G.1    Coonfield, M.L.2    Ross, C.A.3    Borchelt, D.R.4
  • 147
    • 77957790499 scopus 로고    scopus 로고
    • Early changes in the hypothalamic region in prodromal Huntington disease revealed by MRI analysis
    • and Huntington Study Group PREDICT-HD Investigators.
    • Soneson, C., Fontes, M., Zhou, Y., Denisov, V., Paulsen, J.S., Kirik, D., Petersén, A., and Huntington Study Group PREDICT-HD Investigators. (2010). Early changes in the hypothalamic region in prodromal Huntington disease revealed by MRI analysis. Neurobiol. Dis. 40, 531-543.
    • (2010) Neurobiol. Dis. , vol.40 , pp. 531-543
    • Soneson, C.1    Fontes, M.2    Zhou, Y.3    Denisov, V.4    Paulsen, J.S.5    Kirik, D.6    Petersén, A.7
  • 148
    • 79952443408 scopus 로고    scopus 로고
    • Mutant huntingtin binds the mitochondrial fission GTPase dynamin-related protein-1 and increases its enzymatic activity
    • Song, W., Chen, J., Petrilli, A., Liot, G., Klinglmayr, E., Zhou, Y., Poquiz, P., Tjong, J., Pouladi, M.A., Hayden, M.R., et al. (2011). Mutant huntingtin binds the mitochondrial fission GTPase dynamin-related protein-1 and increases its enzymatic activity. Nat. Med. 17, 377-382.
    • (2011) Nat. Med. , vol.17 , pp. 377-382
    • Song, W.1    Chen, J.2    Petrilli, A.3    Liot, G.4    Klinglmayr, E.5    Zhou, Y.6    Poquiz, P.7    Tjong, J.8    Pouladi, M.A.9    Hayden, M.R.10
  • 150
    • 0027276977 scopus 로고
    • Neuronal loss in the hippocampus in Huntington's disease: A comparison with HIV infection
    • Spargo, E., Everall, I.P., and Lantos, P.L. (1993). Neuronal loss in the hippocampus in Huntington's disease: a comparison with HIV infection. J. Neurol. Neurosurg. Psychiatry 56, 487-491. (Pubitemid 23171778)
    • (1993) Journal of Neurology Neurosurgery and Psychiatry , vol.56 , Issue.5 , pp. 487-491
    • Spargo, E.1    Everall, I.P.2    Lantos, P.L.3
  • 151
    • 26444489119 scopus 로고    scopus 로고
    • Connected to death: The (unexpurgated) mitochondrial pathway of apoptosis
    • DOI 10.1126/science.1117105
    • Spierings, D., McStay, G., Saleh, M., Bender, C., Chipuk, J., Maurer, U., and Green, D.R. (2005). Connected to death: the (unexpur-gated) mitochondrial pathway of apoptosis. Science 310, 66-67. (Pubitemid 41434533)
    • (2005) Science , vol.310 , Issue.5745 , pp. 66-67
    • Spierings, D.1    McStay, G.2    Saleh, M.3    Bender, C.4    Chipuk, J.5    Maurer, U.6    Green, D.R.7
  • 152
    • 77955398297 scopus 로고    scopus 로고
    • Uncovering the true prevalence of Huntington's disease
    • Spinney, L. (2010). Uncovering the true prevalence of Huntington's disease. Lancet Neurol. 9, 760-761.
    • (2010) Lancet Neurol. , vol.9 , pp. 760-761
    • Spinney, L.1
  • 155
    • 57649171133 scopus 로고    scopus 로고
    • Evidence of oxidant damage in Huntington's disease: Translational strategies using antioxidants
    • Stack, E.C., Matson, W.R., and Ferrante, R.J. (2008). Evidence of oxidant damage in Huntington's disease: translational strategies using antioxidants. Ann. NY Acad. Sci. 1147, 79-92.
    • (2008) Ann. NY Acad. Sci. , vol.1147 , pp. 79-92
    • Stack, E.C.1    Matson, W.R.2    Ferrante, R.J.3
  • 157
    • 0035897405 scopus 로고    scopus 로고
    • Identities of sequestered proteins in aggregates from cells with induced polyglutamine expression
    • DOI 10.1083/jcb.153.2.283
    • Suhr, S.T., Senut, M.C., Whitelegge, J.P., Faull, K.F., Cuizon, D.B., and Gage, F.H. (2001). Identities of sequestered proteins in aggregates from cells with induced polyglutamine expression. J. Cell Biol. 153, 283-294. (Pubitemid 34280215)
    • (2001) Journal of Cell Biology , vol.153 , Issue.2 , pp. 283-294
    • Suhr, S.T.1    Senut, M.-C.2    Whitelegge, J.P.3    Faull, K.F.4    Cuizon, D.B.5    Gage, F.H.6
  • 159
    • 34347353834 scopus 로고    scopus 로고
    • Mitochondria in cybrids containing mtDNA from persons with mitochondriopathies
    • DOI 10.1002/jnr.21167
    • Swerdlow, R.H. (2007). Mitochondria in cybrids containing mtDNA from persons with mitochondriopathies. J. Neurosci. Res. 85, 3416-3428. (Pubitemid 350058530)
    • (2007) Journal of Neuroscience Research , vol.85 , Issue.15 , pp. 3416-3428
    • Swerdlow, R.H.1
  • 161
    • 0032900574 scopus 로고    scopus 로고
    • Biochemical abnormalities and excitotoxicity in Huntington's disease brain
    • DOI 10.1002/1531-8249(199901)45:1<25::AID-ART6>3.0.CO;2-E
    • Tabrizi, S.J., Cleeter, M.W., Xuereb, J., Taanman, J.W., Cooper, J.M., and Schapira, A.H. (1999). Biochemical abnormalities and exci-totoxicity in Huntington's disease brain. Ann. Neurol. 45, 25-32. (Pubitemid 29036428)
    • (1999) Annals of Neurology , vol.45 , Issue.1 , pp. 25-32
    • Tabrizi, S.J.1    Cleeter, M.W.J.2    Xuereb, J.3    Taanman, J.-W.4    Cooper, J.M.5    Schapira, A.H.V.6
  • 162
    • 0033982887 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and free radical damage in the Huntington R6/2 transgenic mouse
    • DOI 10.1002/1531-8249(200001)47:1<80::AID-ANA13>3.0.CO;2-K
    • Tabrizi, S.J., Workman, J., Hart, P.E., Mangiarini, L., Mahal, A., Bates, G., Cooper, J.M., and Schapira, A.H. (2000). Mitochondrial dysfunction and free radical damage in the Huntington R6/2 trans-genic mouse. Ann. Neurol. 47, 80-86. (Pubitemid 30033653)
    • (2000) Annals of Neurology , vol.47 , Issue.1 , pp. 80-86
    • Tabrizi, S.J.1    Workman, J.2    Hart, P.E.3    Mangiarini, L.4    Mahal, A.5    Bates, G.6    Cooper, J.M.7    Schapira, A.H.V.8
  • 163
    • 18144370445 scopus 로고    scopus 로고
    • High-dose creatine therapy for Huntington disease: A 2-year clinical and MRS study
    • DOI 10.1212/01.WNL.0000160388.96242.77
    • Tabrizi, S.J., Blamire, A.M., Manners, D.N., Rajagopalan, B., Styles, P., Schapira, A.H., and Warner, T.T. (2005). High-dose creatine therapy for Huntington disease: a 2-year clinical and MRS study. Neurology 64, 1655-1656. (Pubitemid 40617715)
    • (2005) Neurology , vol.64 , Issue.9 , pp. 1655-1656
    • Tabrizi, S.J.1    Blamire, A.M.2    Manners, D.N.3    Rajagopalan, B.4    Styles, P.5    Schapira, A.H.V.6    Warner, T.T.7
  • 164
    • 79954630190 scopus 로고    scopus 로고
    • Gene expression pro-filing of R6/2 transgenic mice with different CAG repeat lengths reveals genes associated with disease onset and progression in Huntington's disease
    • Tang, B., Seredenina, T., Coppola, G., Kuhn, A., Geschwind, D.H., Luthi-Carter, R., and Thomas, E.A. (2011). Gene expression pro-filing of R6/2 transgenic mice with different CAG repeat lengths reveals genes associated with disease onset and progression in Huntington's disease. Neurobiol. Dis. 42, 459-467.
    • (2011) Neurobiol. Dis. , vol.42 , pp. 459-467
    • Tang, B.1    Seredenina, T.2    Coppola, G.3    Kuhn, A.4    Geschwind, D.H.5    Luthi-Carter, R.6    Thomas, E.A.7
  • 165
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group
    • The Huntington's Disease Collaborative Research Group (1993). A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 72, 971-983.
    • (1993) Cell , vol.72 , pp. 971-983
  • 166
    • 67649806929 scopus 로고    scopus 로고
    • The cybrid model of sporadic Parkinson's disease
    • Trimmer, P.A. and Bennett, J.P., Jr. (2009). The cybrid model of sporadic Parkinson's disease. Exp. Neurol. 218, 320-325.
    • (2009) Exp. Neurol. , vol.218 , pp. 320-325
    • Trimmer, P.A.1    Bennett Jr., J.P.2
  • 167
    • 0029893076 scopus 로고    scopus 로고
    • Production of transmitochondrial mouse cell lines by cybrid rescue of rhodamine-6G pre-treated L-cells
    • DOI 10.1007/BF02374379
    • Trounce, I. and Wallace, D.C. (1996). Production of transmitochon-drial mouse cell lines by cybrid rescue of rhodamine-6G pre-treated L-cells. Somat. Cell Mol. Genet. 22, 81-85. (Pubitemid 26177599)
    • (1996) Somatic Cell and Molecular Genetics , vol.22 , Issue.1 , pp. 81-85
    • Trounce, I.1    Wallace, D.C.2
  • 168
    • 67349196013 scopus 로고    scopus 로고
    • Metabonomic characterization of the 3-nitropropionic acid rat model of Huntington's disease
    • Tsang, T.M., Haselden, J.N., and Holmes, E. (2009). Metabonomic characterization of the 3-nitropropionic acid rat model of Huntington's disease. Neurochem. Res. 34, 1261-1271.
    • (2009) Neurochem. Res. , vol.34 , pp. 1261-1271
    • Tsang, T.M.1    Haselden, J.N.2    Holmes, E.3
  • 170
    • 35348941757 scopus 로고    scopus 로고
    • Clinical correlates of mitochondrial function in Huntington's disease muscle
    • DOI 10.1002/mds.21540
    • Turner, C., Cooper, J.M., and Schapira, A.H. (2007). Clinical correlates of mitochondrial function in Huntington's disease muscle. Mov. Disord. 22, 1715-1721. (Pubitemid 47597594)
    • (2007) Movement Disorders , vol.22 , Issue.12 , pp. 1715-1721
    • Turner, C.1    Cooper, J.M.2    Schapira, A.H.V.3
  • 174
    • 1542350108 scopus 로고    scopus 로고
    • Genetic and environmental factors in the pathogenesis of Huntington's disease
    • DOI 10.1007/s10048-003-0169-5
    • van Dellen, A. and Hannan, A.J. (2004). Genetic and environmental factors in the pathogenesis of Huntington's disease. Neurogenetics 5, 9-17. (Pubitemid 38297468)
    • (2004) Neurogenetics , vol.5 , Issue.1 , pp. 9-17
    • Van Dellen, A.1    Hannan, A.J.2
  • 175
    • 0034979580 scopus 로고    scopus 로고
    • The oxidative phosphorylation (OXPHOS) system: Nuclear genes and human genetic diseases
    • DOI 10.1002/bies.1071
    • van den Heuvel, L. and Smeitink, J. (2001). The oxidative phospho-rylation (OXPHOS) system: nuclear genes and human genetic diseases. Bioessays 23, 518-525. (Pubitemid 32575612)
    • (2001) BioEssays , vol.23 , Issue.6 , pp. 518-525
    • Van Den Heuvel, L.1    Smeitink, J.2
  • 176
    • 22144494670 scopus 로고    scopus 로고
    • Degenerate mitochondria
    • DOI 10.1038/sj.embor.7400440
    • van der Giezen, M. and Tovar, J. (2005). Degenerate mitochondria. EMBO Rep. 6, 525-530. (Pubitemid 40973960)
    • (2005) EMBO Reports , vol.6 , Issue.6 , pp. 525-530
    • Van Der Giezen, M.1    Tovar, J.2
  • 177
    • 0031867231 scopus 로고    scopus 로고
    • Wild-type and mutant huntingtins function in vesicle trafficking in the secretory and endocytic pathways
    • DOI 10.1006/exnr.1998.6832
    • Velier, J., Kim, M., Schwarz, C., Kim, T.W., Sapp, E., Chase, K., Aronin, N., and DiFiglia, M. (1998). Wild-type and mutant hun-tingtins function in vesicle trafficking in the secretory and endo-cytic pathways. Exp. Neurol. 152, 34-40. (Pubitemid 28366964)
    • (1998) Experimental Neurology , vol.152 , Issue.1 , pp. 34-40
    • Velier, J.1    Kim, M.2    Schwarz, C.3    Kim, T.W.4    Sapp, E.5    Chase, K.6    Aronin, N.7    DiFiglia, M.8
  • 179
    • 0034676455 scopus 로고    scopus 로고
    • Surfing the p53 network
    • Vogelstein, B., Lane, D., and Levine, A.J. (2000). Surfing the p53 network. Nature 408, 307-310.
    • (2000) Nature , vol.408 , pp. 307-310
    • Vogelstein, B.1    Lane, D.2    Levine, A.J.3
  • 182
    • 0037794452 scopus 로고    scopus 로고
    • Detection of mitochondrial DNA deletion by a modified PCR method in a 60Co radiation-exposed patient
    • Wang, Z.C., Wang, X.M., Jiao, B.H., Jin, Y.X., Miao, M.Y., Zhu, K.J., and Ni, Q.G. (2003). Detection of mitochondrial DNA deletion by a modified PCR method in a 60Co radiation-exposed patient. IUBMB Life 55, 133-137.
    • (2003) IUBMB Life , vol.55 , pp. 133-137
    • Wang, Z.C.1    Wang, X.M.2    Jiao, B.H.3    Jin, Y.X.4    Miao, M.Y.5    Zhu, K.J.6    Ni, Q.G.7
  • 184
    • 0036850529 scopus 로고    scopus 로고
    • Aggregated poly-glutamine peptides delivered to nuclei are toxic to mammalian cells
    • Yang, W., Dunlap, J.R., Andrews, R.B., and Wetzel, R. (2002). Aggregated poly-glutamine peptides delivered to nuclei are toxic to mammalian cells. Hum. Mol. Genet. 11, 2905-2917.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2905-2917
    • Yang, W.1    Dunlap, J.R.2    Andrews, R.B.3    Wetzel, R.4
  • 185
    • 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., and Beal, M.F. (2009). Combination therapy with coenzyme Q10 and creatine produces additive neuroprotective effects in models of Parkinson's and Huntington's diseases. J. Neurochem. 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
  • 186
    • 33846502074 scopus 로고    scopus 로고
    • Coenzyme Q10: A review of its promise as a neuroprotectant
    • Young, A.J., Johnson, S., Steffens, D.C., and Doraiswamy, P.M. (2007). Coenzyme Q10: a review of its promise as a neuropro-tectant. CNS Spectr. 12, 62-68. (Pubitemid 46155305)
    • (2007) CNS Spectrums , vol.12 , Issue.1 , pp. 62-68
    • Young, A.J.1    Johnson, S.2    Steffens, D.C.3    Doraiswamy, P.M.4
  • 187
  • 188
    • 29244462838 scopus 로고    scopus 로고
    • In vitro analysis of huntingtin-mediated transcriptional repression reveals multiple transcription factor targets
    • DOI 10.1016/j.cell.2005.10.030, PII S0092867405012286
    • Zhai, W., Jeong, H., Cui, L., Krainc, D., and Tjian, R. (2005). In vitro analysis of huntingtin-mediated transcriptional repression reveals multiple transcription factor targets. Cell 123, 1241-1253. (Pubitemid 41821782)
    • (2005) Cell , vol.123 , Issue.7 , pp. 1241-1253
    • Zhai, W.1    Jeong, H.2    Cui, L.3    Krainc, D.4    Tjian, R.5
  • 189
    • 65249125897 scopus 로고    scopus 로고
    • P53 mediates mitochondria dysfunction-triggered autophagy activation and cell death in rat striatum
    • Zhang, X.D., Wang, Y., Wang, Y., Zhang, X., Han, R., Wu, J.C., Liang, Z.Q., Gu, Z.L., Han, F., Fukunaga, K., et al. (2009). p53 mediates mitochondria dysfunction-triggered autophagy activation and cell death in rat striatum. Autophagy 5, 339-350.
    • (2009) Autophagy , vol.5 , pp. 339-350
    • Zhang, X.D.1    Wang, Y.2    Wang, Y.3    Zhang, X.4    Han, R.5    Wu, J.C.6    Liang, Z.Q.7    Gu, Z.L.8    Han, F.9    Fukunaga, K.10


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