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Volumn 6, Issue 9, 2010, Pages

Experimental and computational analysis of polyglutamine-mediated cytotoxicity

Author keywords

[No Author keywords available]

Indexed keywords

CELL DEATH; CYTOTOXICITY; ENZYMES; NEURODEGENERATIVE DISEASES; STOCHASTIC MODELS; STOCHASTIC SYSTEMS;

EID: 78049415823     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1000944     Document Type: Article
Times cited : (14)

References (37)
  • 1
    • 0034982171 scopus 로고    scopus 로고
    • Ubiquitin and the molecular pathology of neurodegenerative diseases
    • Lowe J, Mayer J, Landon M, Layfield R (2001) Ubiquitin and the molecular pathology of neurodegenerative diseases. Adv Exp Med Biol 487: 169-186.
    • (2001) Adv Exp Med Biol , vol.487 , pp. 169-186
    • Lowe, J.1    Mayer, J.2    Landon, M.3    Layfield, R.4
  • 3
    • 51149121890 scopus 로고    scopus 로고
    • Depletion of 26S proteasomes in mouse brain neurons causes neurodegeneration and Lewy-like inclusions resembling human pale bodies
    • Bedford L, Hay D, Devoy A, Paine S, Powe DG, et al. (2008) Depletion of 26S proteasomes in mouse brain neurons causes neurodegeneration and Lewy-like inclusions resembling human pale bodies. J Neurosci 28: 8189-8198.
    • (2008) J Neurosci , vol.28 , pp. 8189-8198
    • Bedford, L.1    Hay, D.2    Devoy, A.3    Paine, S.4    Powe, D.G.5
  • 4
    • 63249135140 scopus 로고    scopus 로고
    • Single neuron ubiquitin-proteasome dynamics accompanying inclusion body formation in huntington disease
    • Mitra S, Tsvetkov AS, Finkbeiner S (2009) Single neuron ubiquitin-proteasome dynamics accompanying inclusion body formation in huntington disease. J Biol Chem 284: 4398-4403.
    • (2009) J Biol Chem , vol.284 , pp. 4398-4403
    • Mitra, S.1    Tsvetkov, A.S.2    Finkbeiner, S.3
  • 5
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S (2004) Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431: 805-810.
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 6
    • 33846262456 scopus 로고    scopus 로고
    • Abnormalities of the nucleus and nuclear inclusions in neurodegenerative disease: A work in progress
    • Woulfe JM (2007) Abnormalities of the nucleus and nuclear inclusions in neurodegenerative disease: a work in progress. Neuropathol Appl Neurobiol 33: 2-42.
    • (2007) Neuropathol Appl Neurobiol , vol.33 , pp. 2-42
    • Woulfe, J.M.1
  • 7
    • 0031446233 scopus 로고    scopus 로고
    • Intranuclear neuronal inclusions: A common pathogenic mechanism for glutamine-repeat neurodegenerative diseases?
    • Ross CA (1997) Intranuclear neuronal inclusions: a common pathogenic mechanism for glutamine-repeat neurodegenerative diseases? Neuron 19: 1147-1150.
    • (1997) Neuron , vol.19 , pp. 1147-1150
    • Ross, C.A.1
  • 8
    • 33751080354 scopus 로고    scopus 로고
    • Huntingtin inclusion bodies are iron-dependent centers of oxidative events
    • Firdaus WJ, Wyttenbach A, Giuliano P, Kretz-Remy C, Currie RW, et al. (2006) Huntingtin inclusion bodies are iron-dependent centers of oxidative events. FEBS J 273: 5428-5441.
    • (2006) FEBS J , vol.273 , pp. 5428-5441
    • Firdaus, W.J.1    Wyttenbach, A.2    Giuliano, P.3    Kretz-Remy, C.4    Currie, R.W.5
  • 9
    • 47749118777 scopus 로고    scopus 로고
    • Activation of p38MAPK contributes to expanded polyglutamine-induced cytotoxicity
    • Tsirigotis M, Baldwin RM, Tang MY, Lorimer IA, Gray DA (2008) Activation of p38MAPK contributes to expanded polyglutamine-induced cytotoxicity. PLoS One 3: e2130.
    • (2008) PLoS One , vol.3
    • Tsirigotis, M.1    Baldwin, R.M.2    Tang, M.Y.3    Lorimer, I.A.4    Gray, D.A.5
  • 10
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitinproteasome system by protein aggregation
    • Bence NF, Sampat RM, Kopito RR (2001) Impairment of the ubiquitinproteasome system by protein aggregation. Science 292: 1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 11
    • 38149065992 scopus 로고    scopus 로고
    • An in silico model of the ubiquitinproteasome system that incorporates normal homeostasis and age-related decline
    • Proctor CJ, Tsirigotis M, Gray DA (2007) An in silico model of the ubiquitinproteasome system that incorporates normal homeostasis and age-related decline. BMC Syst Biol 1: 17.
    • (2007) BMC Syst Biol , vol.1 , pp. 17
    • Proctor, C.J.1    Tsirigotis, M.2    Gray, D.A.3
  • 12
    • 33644652951 scopus 로고    scopus 로고
    • Proteasome regulation of oxidative stress in aging and age-related diseases of the CNS
    • Ding Q, Dimayuga E, Keller JN (2006) Proteasome regulation of oxidative stress in aging and age-related diseases of the CNS. Antioxid Redox Signal 8: 163-172.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 163-172
    • Ding, Q.1    Dimayuga, E.2    Keller, J.N.3
  • 13
    • 69949098489 scopus 로고    scopus 로고
    • Proteasome inactivation promotes p38 mitogen-activated protein kinase-dependent phosphatidylinositol 3-kinase activation and increases interleukin-8 production in retinal pigment epithelial cells
    • Fernandes AF, Bian Q, Jiang JK, Thomas CJ, Taylor A, et al. (2009) Proteasome inactivation promotes p38 mitogen-activated protein kinase-dependent phosphatidylinositol 3-kinase activation and increases interleukin-8 production in retinal pigment epithelial cells. Mol Biol Cell 20: 3690-3699.
    • (2009) Mol Biol Cell , vol.20 , pp. 3690-3699
    • Fernandes, A.F.1    Bian, Q.2    Jiang, J.K.3    Thomas, C.J.4    Taylor, A.5
  • 14
    • 27744561355 scopus 로고    scopus 로고
    • Role of protein turnover in the activation of p38 mitogen-activated protein kinase in rat pinealocytes
    • Ho AK, McNeil L, Terriff D, Price DM, Chik CL (2005) Role of protein turnover in the activation of p38 mitogen-activated protein kinase in rat pinealocytes. Biochem Pharmacol 70: 1840-1850.
    • (2005) Biochem Pharmacol , vol.70 , pp. 1840-1850
    • Ho, A.K.1    McNeil, L.2    Terriff, D.3    Price, D.M.4    Chik, C.L.5
  • 15
    • 53149144701 scopus 로고    scopus 로고
    • Explaining oscillations and variability in the p53- Mdm2 system
    • Proctor CJ, Gray DA (2008) Explaining oscillations and variability in the p53- Mdm2 system. BMC Syst Biol 2: 75.
    • (2008) BMC Syst Biol , vol.2 , pp. 75
    • Proctor, C.J.1    Gray, D.A.2
  • 16
    • 0036566675 scopus 로고    scopus 로고
    • Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin
    • Wyttenbach A, Sauvageot O, Carmichael J, Diaz-Latoud C, Arrigo AP, et al. (2002) Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin. Hum Mol Genet 11: 1137-1151.
    • (2002) Hum Mol Genet , vol.11 , pp. 1137-1151
    • Wyttenbach, A.1    Sauvageot, O.2    Carmichael, J.3    Diaz-Latoud, C.4    Arrigo, A.P.5
  • 17
    • 77149164811 scopus 로고    scopus 로고
    • Feedback between p21 and reactive oxygen production is necessary for cell senescence
    • Passos JF, Nelson G, Wang C, Richter T, Simillion C, et al. (2010) Feedback between p21 and reactive oxygen production is necessary for cell senescence. Mol Syst Biol 6: 347.
    • (2010) Mol Syst Biol , vol.6 , pp. 347
    • Passos, J.F.1    Nelson, G.2    Wang, C.3    Richter, T.4    Simillion, C.5
  • 18
    • 2442645048 scopus 로고    scopus 로고
    • Proteasome inhibition alters neural mitochondrial homeostasis and mitochondria turnover
    • Sullivan PG, Dragicevic NB, Deng JH, Bai Y, Dimayuga E, et al. (2004) Proteasome inhibition alters neural mitochondrial homeostasis and mitochondria turnover. J Biol Chem 279: 20699-20707.
    • (2004) J Biol Chem , vol.279 , pp. 20699-20707
    • Sullivan, P.G.1    Dragicevic, N.B.2    Deng, J.H.3    Bai, Y.4    Dimayuga, E.5
  • 20
    • 62849122468 scopus 로고    scopus 로고
    • DNA breakage and induction of DNA damage response proteins precede the appearance of visible mutant huntingtin aggregates
    • Illuzzi J, Yerkes S, Parekh-Olmedo H, Kmiec EB (2009) DNA breakage and induction of DNA damage response proteins precede the appearance of visible mutant huntingtin aggregates. J Neurosci Res 87: 733-747.
    • (2009) J Neurosci Res , vol.87 , pp. 733-747
    • Illuzzi, J.1    Yerkes, S.2    Parekh-Olmedo, H.3    Kmiec, E.B.4
  • 21
    • 75649085703 scopus 로고    scopus 로고
    • Coordinated regulation of autophagy by p38alpha MAPK through mAtg9 and p38IP
    • Webber JL, Tooze SA (2010) Coordinated regulation of autophagy by p38alpha MAPK through mAtg9 and p38IP. EMBO J 29: 27-40.
    • (2010) EMBO J , vol.29 , pp. 27-40
    • Webber, J.L.1    Tooze, S.A.2
  • 22
    • 0038493550 scopus 로고    scopus 로고
    • Characterization of chronic low-level proteasome inhibition on neural homeostasis
    • Ding Q, Dimayuga E, Martin S, Bruce-Keller AJ, Nukala V, et al. (2003) Characterization of chronic low-level proteasome inhibition on neural homeostasis. J Neurochem 86: 489-497.
    • (2003) J Neurochem , vol.86 , pp. 489-497
    • Ding, Q.1    Dimayuga, E.2    Martin, S.3    Bruce-Keller, A.J.4    Nukala, V.5
  • 23
    • 37849042536 scopus 로고    scopus 로고
    • A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin
    • Sarkar S, Krishna G, Imarisio S, Saiki S, O'Kane CJ, et al. (2008) A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin. Hum Mol Genet 17: 170-178.
    • (2008) Hum Mol Genet , vol.17 , pp. 170-178
    • Sarkar, S.1    Krishna, G.2    Imarisio, S.3    Saiki, S.4    O'Kane, C.J.5
  • 24
    • 77949352928 scopus 로고    scopus 로고
    • Acute polyglutamine expression in inducible mouse model unravels ubiquitin/proteasome system impairment and permanent recovery attributable to aggregate formation
    • Ortega Z, Diaz-Hernandez M, Maynard CJ, Hernandez F, Dantuma NP, et al. (2010) Acute polyglutamine expression in inducible mouse model unravels ubiquitin/proteasome 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    Diaz-Hernandez, M.2    Maynard, C.J.3    Hernandez, F.4    Dantuma, N.P.5
  • 25
    • 0037342537 scopus 로고    scopus 로고
    • The systems biology markup language (SBML): A medium for representation and exchange of biochemical network models
    • Hucka M, Finney A, Sauro HM, Bolouri H, Doyle JC, et al. (2003) The systems biology markup language (SBML): a medium for representation and exchange of biochemical network models. Bioinformatics 19: 524-531.
    • (2003) Bioinformatics , vol.19 , pp. 524-531
    • Hucka, M.1    Finney, A.2    Sauro, H.M.3    Bolouri, H.4    Doyle, J.C.5
  • 27
    • 33645429016 scopus 로고
    • Exact stochastic simulation of coupled chemical reactions
    • Gillespie DT (1977) Exact stochastic simulation of coupled chemical reactions. J Phys Chem 31: 2340-2361.
    • (1977) J Phys Chem , vol.31 , pp. 2340-2361
    • Gillespie, D.T.1
  • 30
    • 33644877164 scopus 로고    scopus 로고
    • BioModels Database: A free, centralized database of curated, published, quantitative kinetic models of biochemical and cellular systems
    • Le Novere N, Bornstein B, Broicher A, Courtot M, Donizelli M, et al. (2006) BioModels Database: a free, centralized database of curated, published, quantitative kinetic models of biochemical and cellular systems. Nucleic Acids Res 34: D689-691.
    • (2006) Nucleic Acids Res , vol.34
    • Le Novere, N.1    Bornstein, B.2    Broicher, A.3    Courtot, M.4    Donizelli, M.5
  • 31
    • 5644299462 scopus 로고    scopus 로고
    • Different ataxin-2 antibodies display different immunoreactive profiles
    • Turnbull VJ, Storey E, Tarlac V, Walsh R, Stefani D, et al. (2004) Different ataxin-2 antibodies display different immunoreactive profiles. Brain Research 1027: 103-116.
    • (2004) Brain Research , vol.1027 , pp. 103-116
    • Turnbull, V.J.1    Storey, E.2    Tarlac, V.3    Walsh, R.4    Stefani, D.5
  • 32
    • 18844426044 scopus 로고    scopus 로고
    • Imaging b-amyloid fibrils in Alzheimer's disease: A critical analysis through simulation of amyloid fibril polymerization
    • Shoghi-Jadid K, Barrio JR, Kepe V, Wu H-M, Small GW, et al. (2005) Imaging b-amyloid fibrils in Alzheimer's disease: a critical analysis through simulation of amyloid fibril polymerization. Nucl Med Biol 32: 337-351.
    • (2005) Nucl Med Biol , vol.32 , pp. 337-351
    • Shoghi-Jadid, K.1    Barrio, J.R.2    Kepe, V.3    Wu, H.-M.4    Small, G.W.5
  • 33
    • 7044233147 scopus 로고    scopus 로고
    • Biochemical, ultrastructural, and reversibility studies on huntingtin filaments isolated from mouse and human brain
    • Diaz-Hernandez M, Moreno-Herrero F, Gomez-Ramos P, Moran MA, Ferrer I, et al. (2004) Biochemical, ultrastructural, and reversibility studies on huntingtin filaments isolated from mouse and human brain. J Neurosci 24: 9361-9371.
    • (2004) J Neurosci , vol.24 , pp. 9361-9371
    • Diaz-Hernandez, M.1    Moreno-Herrero, F.2    Gomez-Ramos, P.3    Moran, M.A.4    Ferrer, I.5
  • 34
    • 18344414746 scopus 로고    scopus 로고
    • The Ab peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction
    • Huang X, Atwood CS, Hartshorn MA, Multhaup G, Goldstein LE, et al. (1999) The Ab peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction. Biochemistry 38: 7609-7616.
    • (1999) Biochemistry , vol.38 , pp. 7609-7616
    • Huang, X.1    Atwood, C.S.2    Hartshorn, M.A.3    Multhaup, G.4    Goldstein, L.E.5
  • 35
    • 77954379810 scopus 로고    scopus 로고
    • Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool
    • Olshina MA, Angley LM, Ramdzan YM, Tang J, Bailey MF, et al. Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool. J Biol Chem 285: 21807-21816.
    • J Biol Chem , vol.285 , pp. 21807-21816
    • Olshina, M.A.1    Angley, L.M.2    Ramdzan, Y.M.3    Tang, J.4    Bailey, M.F.5
  • 36
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitinproteasome system by protein aggregation
    • Bence NF, Sampat RM, Kopito RR (2001) Impairment of the ubiquitinproteasome system by protein aggregation. Science 292: 1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 37
    • 2642543359 scopus 로고    scopus 로고
    • 15-deoxy-delta 12, 14-Prostaglandin J2 prevents reactive oxygen species generation and mitochondrial membrane depolarization induced by oxidative stress
    • Garg T, Chang J (2004) 15-deoxy-delta 12, 14-Prostaglandin J2 prevents reactive oxygen species generation and mitochondrial membrane depolarization induced by oxidative stress. BMC Pharmacol 4: 6.
    • (2004) BMC Pharmacol , vol.4 , pp. 6
    • Garg, T.1    Chang, J.2


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