메뉴 건너뛰기




Volumn 338, Issue 2, 2015, Pages 183-193

Rosiglitazone activation of PPARγ-dependent signaling is neuroprotective in mutant huntingtin expressing cells

Author keywords

Huntingtin; Huntington's Disease; Neuroprotection; PGC1 ; PPAR ; Rosiglitazone

Indexed keywords

2 CHLORO 5 NITROBENZANILIDE; APOPTOSIS SIGNAL REGULATING KINASE 1; GLUCOSE REGULATED PROTEIN 78; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 70; HEAT SHOCK TRANSCRIPTION FACTOR 1; HUNTINGTIN; MITOCHONDRIAL TRANSCRIPTION FACTOR A; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; PROTEASOME; ROSIGLITAZONE; TRANSCRIPTION FACTOR NRF1; UBIQUITIN; 2,4 THIAZOLIDINEDIONE DERIVATIVE; DNA BINDING PROTEIN; HEAT SHOCK PROTEIN; HSF1 PROTEIN, MOUSE; HUNTINGTON PROTEIN, MOUSE; NERVE PROTEIN; NEUROPROTECTIVE AGENT; NUCLEAR PROTEIN; TRANSCRIPTION FACTOR;

EID: 84944717552     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2015.09.005     Document Type: Article
Times cited : (36)

References (76)
  • 1
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M., Sapp E., Chase K.O., Davies S.W., Bates G.P., Vonsattel J.P., Aronin N. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 1997, 277:1990-1993.
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 2
    • 0022876328 scopus 로고
    • Huntington's disease. Pathogenesis and management
    • Martin J.B., Gusella J.F. Huntington's disease. Pathogenesis and management. N Engl. J. Med. 1986, 315:1267-1276.
    • (1986) N Engl. J. Med. , vol.315 , pp. 1267-1276
    • Martin, J.B.1    Gusella, J.F.2
  • 4
    • 0034754875 scopus 로고    scopus 로고
    • Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation
    • Waelter S., Boeddrich A., Lurz R., Scherzinger E., Lueder G., Lehrach H., Wanker E.E. Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation. Mol. Biol. Cell 2001, 12:1393-1407.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1393-1407
    • Waelter, S.1    Boeddrich, A.2    Lurz, R.3    Scherzinger, E.4    Lueder, G.5    Lehrach, H.6    Wanker, E.E.7
  • 5
    • 0033010987 scopus 로고    scopus 로고
    • Recent advances in understanding the pathogenesis of Huntington's disease
    • Reddy P.H., Williams M., Tagle D.A. Recent advances in understanding the pathogenesis of Huntington's disease. Trends Neurosci. 1999, 22:248-255.
    • (1999) Trends Neurosci. , vol.22 , pp. 248-255
    • Reddy, P.H.1    Williams, M.2    Tagle, D.A.3
  • 6
    • 84866556522 scopus 로고    scopus 로고
    • Protein aggregates in Huntington's disease
    • Arrasate M., Finkbeiner S. Protein aggregates in Huntington's disease. Exp. Neurol. 2012, 238:1-11.
    • (2012) Exp. Neurol. , vol.238 , pp. 1-11
    • Arrasate, M.1    Finkbeiner, S.2
  • 7
    • 0034641589 scopus 로고    scopus 로고
    • Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity
    • Jana N.R., Tanaka M., Wang G., Nukina N. Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity. Hum. Mol. Genet. 2000, 9:2009-2018.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2009-2018
    • Jana, N.R.1    Tanaka, M.2    Wang, G.3    Nukina, N.4
  • 8
    • 0035897405 scopus 로고    scopus 로고
    • Identities of sequestered proteins in aggregates from cells with induced polyglutamine expression
    • Suhr S.T., Senut M.C., Whitelegge J.P., Faull K.F., Cuizon D.B., Gage F.H. Identities of sequestered proteins in aggregates from cells with induced polyglutamine expression. J. Cell Biol. 2001, 153:283-294.
    • (2001) J. Cell Biol. , vol.153 , 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
  • 10
    • 68049096318 scopus 로고    scopus 로고
    • The A2A adenosine receptor rescues the urea cycle deficiency of Huntington's disease by enhancing the activity of the ubiquitin-proteasome system
    • Chiang M.C., Chen H.M., Lai H.L., Chen H.W., Chou S.Y., Chen C.M., Tsai F.J., Chern Y. The A2A adenosine receptor rescues the urea cycle deficiency of Huntington's disease by enhancing the activity of the ubiquitin-proteasome system. Hum. Mol. Genet. 2009, 18:2929-2942.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 2929-2942
    • Chiang, M.C.1    Chen, H.M.2    Lai, H.L.3    Chen, H.W.4    Chou, S.Y.5    Chen, C.M.6    Tsai, F.J.7    Chern, Y.8
  • 12
    • 84875679362 scopus 로고    scopus 로고
    • Mitochondria targeted therapeutic approaches in Parkinson's and Huntington's diseases
    • Chaturvedi R.K., Beal M.F. Mitochondria targeted therapeutic approaches in Parkinson's and Huntington's diseases. Mol. Cell. Neurosci. 2013, 55:101-114.
    • (2013) Mol. Cell. Neurosci. , vol.55 , pp. 101-114
    • Chaturvedi, R.K.1    Beal, M.F.2
  • 14
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh H., Matsuzawa A., Tobiume K., Saegusa K., Takeda K., Inoue K., Hori S., Kakizuka A., Ichijo H. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev. 2002, 16:1345-1355.
    • (2002) Genes Dev. , vol.16 , pp. 1345-1355
    • Nishitoh, H.1    Matsuzawa, A.2    Tobiume, K.3    Saegusa, K.4    Takeda, K.5    Inoue, K.6    Hori, S.7    Kakizuka, A.8    Ichijo, H.9
  • 15
    • 0035936764 scopus 로고    scopus 로고
    • Obesity and the regulation of energy balance
    • Spiegelman B.M., Flier J.S. Obesity and the regulation of energy balance. Cell 2001, 104:531-543.
    • (2001) Cell , vol.104 , pp. 531-543
    • Spiegelman, B.M.1    Flier, J.S.2
  • 16
    • 14544303179 scopus 로고    scopus 로고
    • PPAR gamma, 10 years later
    • Lazar M.A. PPAR gamma, 10 years later. Biochimie 2005, 87:9-13.
    • (2005) Biochimie , vol.87 , pp. 9-13
    • Lazar, M.A.1
  • 17
    • 28944446431 scopus 로고    scopus 로고
    • The many faces of PPARgamma
    • Lehrke M., Lazar M.A. The many faces of PPARgamma. Cell 2005, 123:993-999.
    • (2005) Cell , vol.123 , pp. 993-999
    • Lehrke, M.1    Lazar, M.A.2
  • 19
    • 33744994576 scopus 로고    scopus 로고
    • PPARgamma as a therapeutic target in central nervous system diseases
    • Sundararajan S., Jiang Q., Heneka M., Landreth G. PPARgamma as a therapeutic target in central nervous system diseases. Neurochem. Int. 2006, 49:136-144.
    • (2006) Neurochem. Int. , vol.49 , pp. 136-144
    • Sundararajan, S.1    Jiang, Q.2    Heneka, M.3    Landreth, G.4
  • 20
    • 33745265189 scopus 로고    scopus 로고
    • PPARgamma agonists as new therapeutic agents for the treatment of Alzheimer's disease
    • Landreth G. PPARgamma agonists as new therapeutic agents for the treatment of Alzheimer's disease. Exp. Neurol. 2006, 199:245-248.
    • (2006) Exp. Neurol. , vol.199 , pp. 245-248
    • Landreth, G.1
  • 21
    • 84860365643 scopus 로고    scopus 로고
    • Pharmacological manipulation of peroxisome proliferator-activated receptor gamma (PPARgamma) reveals a role for anti-oxidant protection in a model of Parkinson's disease
    • Martin H.L., Mounsey R.B., Mustafa S., Sathe K., Teismann P. Pharmacological manipulation of peroxisome proliferator-activated receptor gamma (PPARgamma) reveals a role for anti-oxidant protection in a model of Parkinson's disease. Exp. Neurol. 2012, 235:528-538.
    • (2012) Exp. Neurol. , vol.235 , pp. 528-538
    • Martin, H.L.1    Mounsey, R.B.2    Mustafa, S.3    Sathe, K.4    Teismann, P.5
  • 22
    • 54449092109 scopus 로고    scopus 로고
    • Rosiglitazone treatment prevents mitochondrial dysfunction in mutant huntingtin-expressing cells: possible role of peroxisome proliferator-activated receptor-gamma (PPARgamma) in the pathogenesis of Huntington disease
    • Quintanilla R.A., Jin Y.N., Fuenzalida K., Bronfman M., Johnson G.V. Rosiglitazone treatment prevents mitochondrial dysfunction in mutant huntingtin-expressing cells: possible role of peroxisome proliferator-activated receptor-gamma (PPARgamma) in the pathogenesis of Huntington disease. J. Biol. Chem. 2008, 283:25628-25637.
    • (2008) J. Biol. Chem. , vol.283 , pp. 25628-25637
    • Quintanilla, R.A.1    Jin, Y.N.2    Fuenzalida, K.3    Bronfman, M.4    Johnson, G.V.5
  • 24
    • 79960564783 scopus 로고    scopus 로고
    • The dysfunction of hepatic transcriptional factors in mice with Huntington's Disease
    • Chiang M.C., Chern Y., Juo C.G. The dysfunction of hepatic transcriptional factors in mice with Huntington's Disease. Biochim. Biophys. Acta 2011, 1812:1111-1120.
    • (2011) Biochim. Biophys. Acta , vol.1812 , pp. 1111-1120
    • Chiang, M.C.1    Chern, Y.2    Juo, C.G.3
  • 25
    • 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
  • 26
    • 17144386565 scopus 로고    scopus 로고
    • CAMP-response element-binding protein contributes to suppression of the A2A adenosine receptor promoter by mutant Huntingtin with expanded polyglutamine residues
    • Chiang M.C., Lee Y.C., Huang C.L., Chern Y. cAMP-response element-binding protein contributes to suppression of the A2A adenosine receptor promoter by mutant Huntingtin with expanded polyglutamine residues. J. Biol. Chem. 2005, 280:14331-14340.
    • (2005) J. Biol. Chem. , vol.280 , pp. 14331-14340
    • Chiang, M.C.1    Lee, Y.C.2    Huang, C.L.3    Chern, Y.4
  • 27
    • 84860336997 scopus 로고    scopus 로고
    • Beta-adrenoceptor pathway enhances mitochondrial function in human neural stem cells via rotary cell culture system
    • Chiang M.C., Lin H., Cheng Y.C., Yen C.H., Huang R.N., Lin K.H. Beta-adrenoceptor pathway enhances mitochondrial function in human neural stem cells via rotary cell culture system. J. Neurosci. Methods 2012, 207:130-136.
    • (2012) J. Neurosci. Methods , vol.207 , pp. 130-136
    • Chiang, M.C.1    Lin, H.2    Cheng, Y.C.3    Yen, C.H.4    Huang, R.N.5    Lin, K.H.6
  • 28
    • 84891898130 scopus 로고    scopus 로고
    • Rosiglitazone promotes neurite outgrowth and mitochondrial function in N2A cells via PPARgamma pathway
    • Chiang M.C., Cheng Y.C., Chen H.M., Liang Y.J., Yen C.H. Rosiglitazone promotes neurite outgrowth and mitochondrial function in N2A cells via PPARgamma pathway. Mitochondrion 2014, 14:7-17.
    • (2014) Mitochondrion , vol.14 , pp. 7-17
    • Chiang, M.C.1    Cheng, Y.C.2    Chen, H.M.3    Liang, Y.J.4    Yen, C.H.5
  • 30
    • 34249692543 scopus 로고    scopus 로고
    • Systematic uncovering of multiple pathways underlying the pathology of Huntington disease by an acid-cleavable isotope-coded affinity tag approach
    • Chiang M.C., Juo C.G., Chang H.H., Chen H.M., Yi E.C., Chern Y. Systematic uncovering of multiple pathways underlying the pathology of Huntington disease by an acid-cleavable isotope-coded affinity tag approach. Mol. Cell. Proteom. 2007, 6:781-797.
    • (2007) Mol. Cell. Proteom. , vol.6 , pp. 781-797
    • Chiang, M.C.1    Juo, C.G.2    Chang, H.H.3    Chen, H.M.4    Yi, E.C.5    Chern, Y.6
  • 31
    • 84870911857 scopus 로고    scopus 로고
    • PPARgamma regulates the mitochondrial dysfunction in human neural stem cells with tumor necrosis factor alpha
    • Chiang M.C., Cheng Y.C., Lin K.H., Yen C.H. PPARgamma regulates the mitochondrial dysfunction in human neural stem cells with tumor necrosis factor alpha. Neuroscience 2013, 229:118-129.
    • (2013) Neuroscience , vol.229 , pp. 118-129
    • Chiang, M.C.1    Cheng, Y.C.2    Lin, K.H.3    Yen, C.H.4
  • 33
    • 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
  • 34
    • 0037326196 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-gamma coactivator 1 alpha (PGC-1 alpha): transcriptional coactivator and metabolic regulator
    • Puigserver P., Spiegelman B.M. Peroxisome proliferator-activated receptor-gamma coactivator 1 alpha (PGC-1 alpha): transcriptional coactivator and metabolic regulator. Endocr. Rev. 2003, 24:78-90.
    • (2003) Endocr. Rev. , vol.24 , pp. 78-90
    • Puigserver, P.1    Spiegelman, B.M.2
  • 35
    • 80054037000 scopus 로고    scopus 로고
    • Changes in BiP availability reveal hypersensitivity to acute endoplasmic reticulum stress in cells expressing mutant huntingtin
    • Lajoie P., Snapp E.L. Changes in BiP availability reveal hypersensitivity to acute endoplasmic reticulum stress in cells expressing mutant huntingtin. J. Cell Sci. 2011, 124:3332-3343.
    • (2011) J. Cell Sci. , vol.124 , pp. 3332-3343
    • Lajoie, P.1    Snapp, E.L.2
  • 36
    • 84871490319 scopus 로고    scopus 로고
    • Examining the safety of PPAR agonists-current trends and future prospects
    • Bortolini M., Wright M.B., Bopst M., Balas B. Examining the safety of PPAR agonists-current trends and future prospects. Expert Opin. Drug Saf. 2013, 12:65-79.
    • (2013) Expert Opin. Drug Saf. , vol.12 , pp. 65-79
    • Bortolini, M.1    Wright, M.B.2    Bopst, M.3    Balas, B.4
  • 37
    • 0034651101 scopus 로고    scopus 로고
    • Inflammatory mechanisms in Alzheimer's disease: inhibition of beta-amyloid-stimulated proinflammatory responses and neurotoxicity by PPARgamma agonists
    • Combs C.K., Johnson D.E., Karlo J.C., Cannady S.B., Landreth G.E. Inflammatory mechanisms in Alzheimer's disease: inhibition of beta-amyloid-stimulated proinflammatory responses and neurotoxicity by PPARgamma agonists. J. Neurosci.: Off. J. Soc. Neurosci. 2000, 20:558-567.
    • (2000) J. Neurosci.: Off. J. Soc. Neurosci. , vol.20 , pp. 558-567
    • Combs, C.K.1    Johnson, D.E.2    Karlo, J.C.3    Cannady, S.B.4    Landreth, G.E.5
  • 38
    • 44049091481 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-gamma in amyotrophic lateral sclerosis and Huntington's disease
    • Kiaei M. Peroxisome proliferator-activated receptor-gamma in amyotrophic lateral sclerosis and Huntington's disease. PPAR Res. 2008, 2008:418765.
    • (2008) PPAR Res. , vol.2008 , pp. 418765
    • Kiaei, M.1
  • 39
    • 34249995108 scopus 로고    scopus 로고
    • Molecular targets of non-steroidal anti-inflammatory drugs in neurodegenerative diseases
    • Lleo A., Galea E., Sastre M. Molecular targets of non-steroidal anti-inflammatory drugs in neurodegenerative diseases. Cell. Mol. Life Sci.: CMLS 2007, 64:1403-1418.
    • (2007) Cell. Mol. Life Sci.: CMLS , vol.64 , pp. 1403-1418
    • Lleo, A.1    Galea, E.2    Sastre, M.3
  • 40
    • 26044473385 scopus 로고    scopus 로고
    • Atypical diabetes associated with inclusion formation in the R6/2 mouse model of Huntington's disease is not improved by treatment with hypoglycaemic agents
    • Hunt M.J., Morton A.J. Atypical diabetes associated with inclusion formation in the R6/2 mouse model of Huntington's disease is not improved by treatment with hypoglycaemic agents. Exp. Brain Res.: Experimentelle Hirnforschung 2005, 166:220-229.
    • (2005) Exp. Brain Res.: Experimentelle Hirnforschung , vol.166 , pp. 220-229
    • Hunt, M.J.1    Morton, A.J.2
  • 41
    • 77953706084 scopus 로고    scopus 로고
    • Pioglitazone ameliorates behavioral, biochemical and cellular alterations in quinolinic acid induced neurotoxicity: possible role of peroxisome proliferator activated receptor-Upsilon (PPARUpsilon) in Huntington's disease
    • Kalonia H., Kumar P., Kumar A. Pioglitazone ameliorates behavioral, biochemical and cellular alterations in quinolinic acid induced neurotoxicity: possible role of peroxisome proliferator activated receptor-Upsilon (PPARUpsilon) in Huntington's disease. Pharmacol. Biochem. Behav. 2010, 96:115-124.
    • (2010) Pharmacol. Biochem. Behav. , vol.96 , pp. 115-124
    • Kalonia, H.1    Kumar, P.2    Kumar, A.3
  • 42
    • 79957858160 scopus 로고    scopus 로고
    • Protective effect of pioglitazone, a PPARgamma ligand, in a 3 nitropropionic acid model of Huntington's disease
    • Napolitano M., Costa L., Palermo R., Giovenco A., Vacca A., Gulino A. Protective effect of pioglitazone, a PPARgamma ligand, in a 3 nitropropionic acid model of Huntington's disease. Brain Res. Bull. 2011, 85:231-237.
    • (2011) Brain Res. Bull. , vol.85 , pp. 231-237
    • Napolitano, M.1    Costa, L.2    Palermo, R.3    Giovenco, A.4    Vacca, A.5    Gulino, A.6
  • 43
    • 84856035740 scopus 로고    scopus 로고
    • Metabolic state determines sensitivity to cellular stress in Huntington disease: normalization by activation of PPARgamma
    • Jin Y.N., Hwang W.Y., Jo C., Johnson G.V. Metabolic state determines sensitivity to cellular stress in Huntington disease: normalization by activation of PPARgamma. PLoS One 2012, 7:e30406.
    • (2012) PLoS One , vol.7 , pp. e30406
    • Jin, Y.N.1    Hwang, W.Y.2    Jo, C.3    Johnson, G.V.4
  • 44
    • 77954424991 scopus 로고    scopus 로고
    • The interrelationship between mitochondrial dysfunction and transcriptional dysregulation in Huntington disease
    • Jin Y.N., Johnson G.V. The interrelationship between mitochondrial dysfunction and transcriptional dysregulation in Huntington disease. J. Bioenerg. Biomembr. 2010, 42:199-205.
    • (2010) J. Bioenerg. Biomembr. , vol.42 , pp. 199-205
    • Jin, Y.N.1    Johnson, G.V.2
  • 45
    • 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
  • 46
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases
    • Sherman M.Y., Goldberg A.L. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 2001, 29:15-32.
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 47
    • 34249085552 scopus 로고    scopus 로고
    • Proteasomes: machines for all reasons
    • Demartino G.N., Gillette T.G. Proteasomes: machines for all reasons. Cell 2007, 129:659-662.
    • (2007) Cell , vol.129 , pp. 659-662
    • Demartino, G.N.1    Gillette, T.G.2
  • 48
    • 84890146490 scopus 로고    scopus 로고
    • Proteostasis and neurodegeneration: the roles of proteasomal degradation and autophagy
    • Tanaka K., Matsuda N. Proteostasis and neurodegeneration: the roles of proteasomal degradation and autophagy. Biochim. Biophys. Acta 2014, 1843:197-204.
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 197-204
    • Tanaka, K.1    Matsuda, N.2
  • 49
    • 77952565165 scopus 로고    scopus 로고
    • Illuminating the ubiquitin/proteasome system
    • Salomons F.A., Acs K., Dantuma N.P. Illuminating the ubiquitin/proteasome system. Exp. Cell Res. 2010, 316:1289-1295.
    • (2010) Exp. Cell Res. , vol.316 , pp. 1289-1295
    • Salomons, F.A.1    Acs, K.2    Dantuma, N.P.3
  • 50
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N.F., Sampat R.M., Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 2001, 292:1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 51
    • 35748959676 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in health and disease of the nervous system
    • Hegde A.N., Upadhya S.C. The ubiquitin-proteasome pathway in health and disease of the nervous system. Trends Neurosci. 2007, 30:587-595.
    • (2007) Trends Neurosci. , vol.30 , pp. 587-595
    • Hegde, A.N.1    Upadhya, S.C.2
  • 52
    • 84890203542 scopus 로고    scopus 로고
    • Regulation of proteasome activity in health and disease
    • Schmidt M., Finley D. Regulation of proteasome activity in health and disease. Biochim. Biophys. Acta 2014, 1843:13-25.
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 13-25
    • Schmidt, M.1    Finley, D.2
  • 54
    • 41549129945 scopus 로고    scopus 로고
    • Impaired ubiquitin-proteasome system activity in the synapses of Huntington's disease mice
    • Wang J., Wang C.-E., Orr A., Tydlacka S., Li S.-H., Li X.-J. Impaired ubiquitin-proteasome system activity in the synapses of Huntington's disease mice. J. Cell Biol. 2008, 180:1177-1189.
    • (2008) J. Cell Biol. , vol.180 , pp. 1177-1189
    • Wang, J.1    Wang, C.-E.2    Orr, A.3    Tydlacka, S.4    Li, S.-H.5    Li, X.-J.6
  • 55
    • 34548331451 scopus 로고    scopus 로고
    • Is the ubiquitin-proteasome system impaired in Huntington's disease?
    • Ortega Z., Diaz-Hernandez M., Lucas J.J. Is the ubiquitin-proteasome system impaired in Huntington's disease?. Cell. Mol. Life Sci.: CMLS 2007, 64:2245-2257.
    • (2007) Cell. Mol. Life Sci.: CMLS , vol.64 , pp. 2245-2257
    • Ortega, Z.1    Diaz-Hernandez, M.2    Lucas, J.J.3
  • 56
    • 33846696670 scopus 로고    scopus 로고
    • Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin
    • Yang H., Zhong X., Ballar P., Luo S., Shen Y., Rubinsztein D.C., Monteiro M.J., Fang S. Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin. Exp. Cell Res. 2007, 313:538-550.
    • (2007) Exp. Cell Res. , vol.313 , pp. 538-550
    • Yang, H.1    Zhong, X.2    Ballar, P.3    Luo, S.4    Shen, Y.5    Rubinsztein, D.C.6    Monteiro, M.J.7    Fang, S.8
  • 58
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: cellular functions and molecular mechanism
    • Mayer M.P., Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci.: CMLS 2005, 62:670-684.
    • (2005) Cell. Mol. Life Sci.: CMLS , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 59
    • 35648993510 scopus 로고    scopus 로고
    • To be, or not to be-molecular chaperones in protein degradation
    • Arndt V., Rogon C., Hohfeld J. To be, or not to be-molecular chaperones in protein degradation. Cell. Mol. Life Sci.: CMLS 2007, 64:2525-2541.
    • (2007) Cell. Mol. Life Sci.: CMLS , vol.64 , pp. 2525-2541
    • Arndt, V.1    Rogon, C.2    Hohfeld, J.3
  • 60
    • 3242695184 scopus 로고    scopus 로고
    • Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach
    • Hay D.G., Sathasivam K., Tobaben S., Stahl B., Marber M., Mestril R., Mahal A., Smith D.L., Woodman B., Bates G.P. Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach. Hum. Mol. Genet. 2004, 13:1389-1405.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1389-1405
    • Hay, D.G.1    Sathasivam, K.2    Tobaben, S.3    Stahl, B.4    Marber, M.5    Mestril, R.6    Mahal, A.7    Smith, D.L.8    Woodman, B.9    Bates, G.P.10
  • 61
    • 34548608465 scopus 로고    scopus 로고
    • Modulation of polyglutamine inclusion formation by the Hsp70 chaperone machine
    • Rujano M.A., Kampinga H.H., Salomons F.A. Modulation of polyglutamine inclusion formation by the Hsp70 chaperone machine. Exp. Cell Res. 2007, 313:3568-3578.
    • (2007) Exp. Cell Res. , vol.313 , pp. 3568-3578
    • Rujano, M.A.1    Kampinga, H.H.2    Salomons, F.A.3
  • 62
    • 0034646426 scopus 로고    scopus 로고
    • Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease
    • Wyttenbach A., Carmichael J., Swartz J., Furlong R.A., Narain Y., Rankin J., Rubinsztein D.C. Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease. Proc. Natl. Acad. Sci. USA 2000, 97:2898-2903.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2898-2903
    • Wyttenbach, A.1    Carmichael, J.2    Swartz, J.3    Furlong, R.A.4    Narain, Y.5    Rankin, J.6    Rubinsztein, D.C.7
  • 64
    • 16544383250 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer
    • Wacker J.L., Zareie M.H., Fong H., Sarikaya M., Muchowski P.J. Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer. Nat. Struct. Mol. Biol. 2004, 11:1215-1222.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1215-1222
    • Wacker, J.L.1    Zareie, M.H.2    Fong, H.3    Sarikaya, M.4    Muchowski, P.J.5
  • 65
    • 84893497938 scopus 로고    scopus 로고
    • Roles of Hsp104 and trehalose in solubilisation of mutant huntingtin in heat shocked Saccharomyces cerevisiae cells
    • Saleh A.A., Gune U.S., Chaudhary R.K., Turakhiya A.P., Roy I. Roles of Hsp104 and trehalose in solubilisation of mutant huntingtin in heat shocked Saccharomyces cerevisiae cells. Biochim. Biophys. Acta 2014, 1843:746-757.
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 746-757
    • Saleh, A.A.1    Gune, U.S.2    Chaudhary, R.K.3    Turakhiya, A.P.4    Roy, I.5
  • 66
    • 27144524290 scopus 로고    scopus 로고
    • Active HSF1 significantly suppresses polyglutamine aggregate formation in cellular and mouse models
    • Fujimoto M., Takaki E., Hayashi T., Kitaura Y., Tanaka Y., Inouye S., Nakai A. Active HSF1 significantly suppresses polyglutamine aggregate formation in cellular and mouse models. J. Biol. Chem. 2005, 280:34908-34916.
    • (2005) J. Biol. Chem. , vol.280 , pp. 34908-34916
    • Fujimoto, M.1    Takaki, E.2    Hayashi, T.3    Kitaura, Y.4    Tanaka, Y.5    Inouye, S.6    Nakai, A.7
  • 67
    • 33847093475 scopus 로고    scopus 로고
    • Thiazolidinedione class of peroxisome proliferator-activated receptor {gamma} agonists prevents neuronal damage, motor dysfunction, myelin loss, neuropathic pain, and inflammation after spinal cord injury in adult rats
    • Park S.-W., Yi J.-H., Miranpuri G., Satriotomo I., Bowen K., Resnick D.K., Vemuganti R. Thiazolidinedione class of peroxisome proliferator-activated receptor {gamma} agonists prevents neuronal damage, motor dysfunction, myelin loss, neuropathic pain, and inflammation after spinal cord injury in adult rats. J. Pharmacol. Exp. Ther. 2007, 320:1002-1012.
    • (2007) J. Pharmacol. Exp. Ther. , vol.320 , pp. 1002-1012
    • Park, S.-W.1    Yi, J.-H.2    Miranpuri, G.3    Satriotomo, I.4    Bowen, K.5    Resnick, D.K.6    Vemuganti, R.7
  • 70
    • 39649114320 scopus 로고    scopus 로고
    • Inhibition of endoplasmic reticulum stress counteracts neuronal cell death and protein aggregation caused by N-terminal mutant huntingtin proteins
    • Reijonen S., Putkonen N., Norremolle A., Lindholm D., Korhonen L. Inhibition of endoplasmic reticulum stress counteracts neuronal cell death and protein aggregation caused by N-terminal mutant huntingtin proteins. Exp. Cell Res. 2008, 314:950-960.
    • (2008) Exp. Cell Res. , vol.314 , pp. 950-960
    • Reijonen, S.1    Putkonen, N.2    Norremolle, A.3    Lindholm, D.4    Korhonen, L.5
  • 72
    • 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
  • 73
    • 0034703874 scopus 로고    scopus 로고
    • Intranuclear huntingtin increases the expression of caspase-1 and induces apoptosis
    • Li S.H., Lam S., Cheng A.L., Li X.J. Intranuclear huntingtin increases the expression of caspase-1 and induces apoptosis. Hum. Mol. Genet. 2000, 9:2859-2867.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2859-2867
    • Li, S.H.1    Lam, S.2    Cheng, A.L.3    Li, X.J.4
  • 76
    • 37549060702 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma up-regulates the Bcl-2 anti-apoptotic protein in neurons and induces mitochondrial stabilization and protection against oxidative stress and apoptosis
    • Fuenzalida K., Quintanilla R., Ramos P., Piderit D., Fuentealba R.A., Martinez G., Inestrosa N.C., Bronfman M. Peroxisome proliferator-activated receptor gamma up-regulates the Bcl-2 anti-apoptotic protein in neurons and induces mitochondrial stabilization and protection against oxidative stress and apoptosis. J. Biol. Chem. 2007, 282:37006-37015.
    • (2007) J. Biol. Chem. , vol.282 , pp. 37006-37015
    • Fuenzalida, K.1    Quintanilla, R.2    Ramos, P.3    Piderit, D.4    Fuentealba, R.A.5    Martinez, G.6    Inestrosa, N.C.7    Bronfman, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.