메뉴 건너뛰기




Volumn 648, Issue , 2010, Pages 3-23

Protein misfolding and cellular stress: An overview

(2)  Gregersen, Niels a   Bross, Peter a  

a NONE

Author keywords

Antioxidative defense; Heat shock response; Oxidative stress; Protein misfolding; Protein quality control system; Reactive carbonyl compounds; Reactive nitrogen species; Reactive oxygen species; Unfolded protein response

Indexed keywords

CARBONYL DERIVATIVE; MITOCHONDRIAL PROTEIN; NITRIC OXIDE SYNTHASE; NITROGEN OXIDE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; SUPEROXIDE;

EID: 79952036205     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-60761-756-3_1     Document Type: Chapter
Times cited : (125)

References (88)
  • 1
    • 58149199728 scopus 로고    scopus 로고
    • A pause for thought along the co-translational folding pathway
    • Komar AA (2009) A pause for thought along the co-translational folding pathway. Trends Biochem Sci 34:16–24
    • (2009) Trends Biochem Sci , vol.34 , pp. 16-24
    • Komar, A.A.1
  • 2
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl FU, Hayer-Hartl M (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295: 1852–1858
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 3
    • 30344462410 scopus 로고    scopus 로고
    • Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells
    • Albanese V, Yam AY, Baughman J, Parnot C, Frydman J (2006) Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells. Cell 124:75–88
    • (2006) Cell , vol.124 , pp. 75-88
    • Albanese, V.1    Yam, A.Y.2    Baughman, J.3    Parnot, C.4    Frydman, J.5
  • 4
    • 9644280977 scopus 로고    scopus 로고
    • Cooperation of molecular chaperones with the ubiquitin/proteasome system
    • Esser C, Alberti S, Hohfeld J (2004) Cooperation of molecular chaperones with the ubiquitin/proteasome system. Biochim Biophys Acta 1695:171–188
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 171-188
    • Esser, C.1    Alberti, S.2    Hohfeld, J.3
  • 5
    • 23144443884 scopus 로고    scopus 로고
    • Protein quality control: Chaperones culling corrupt conformations
    • McClellan AJ, Tam S, Kaganovich D, Frydman J (2005) Protein quality control: chaperones culling corrupt conformations. Nat Cell Biol 7:736–741
    • (2005) Nat Cell Biol , vol.7 , pp. 736-741
    • McClellan, A.J.1    Tam, S.2    Kaganovich, D.3    Frydman, J.4
  • 6
    • 0022555843 scopus 로고
    • The heat-shock response
    • Lindquist S (1986) The heat-shock response. Annu Rev Biochem 55:1151–1191
    • (1986) Annu Rev Biochem , vol.55 , pp. 1151-1191
    • Lindquist, S.1
  • 7
    • 37849022851 scopus 로고    scopus 로고
    • Mitochondrial stress signaling: A pathway unfolds
    • Broadley SA, Hartl FU (2008) Mitochondrial stress signaling: a pathway unfolds. Trends Cell Biol 18:1–4
    • (2008) Trends Cell Biol , vol.18 , pp. 1-4
    • Broadley, S.A.1    Hartl, F.U.2
  • 8
    • 0037299969 scopus 로고    scopus 로고
    • Stress proteins in neural cells: Functional roles in health and disease
    • Richter-Landsberg C, Goldbaum O (2003) Stress proteins in neural cells: functional roles in health and disease. Cell Mol Life Sci 60:337–349
    • (2003) Cell Mol Life Sci , vol.60 , pp. 337-349
    • Richter-Landsberg, C.1    Goldbaum, O.2
  • 10
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • Morimoto RI (2008) Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev 22: 1427–1438
    • (2008) Genes Dev , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 11
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • Schubert U, Anton LC, Gibbs J, Norbury CC, Yewdell JW, Bennink JR (2000) Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 404:770–774
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1    Anton, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5    Bennink, J.R.6
  • 12
    • 15244339962 scopus 로고    scopus 로고
    • Neurodegeneration caused by the translation of nonsense: Does macromolecular misfolding impair the syn-chrony of gene expression?
    • Connolly JB (2005) Neurodegeneration caused by the translation of nonsense: does macromolecular misfolding impair the syn-chrony of gene expression? Med Hypotheses 64:968–972
    • (2005) Med Hypotheses , vol.64 , pp. 968-972
    • Connolly, J.B.1
  • 13
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R (1998) Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 94:471–480
    • (1998) Cell , vol.94 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5
  • 14
    • 0035147404 scopus 로고    scopus 로고
    • Molecular chaperones and the art of recognizing a lost cause
    • McClellan AJ, Frydman J (2001) Molecular chaperones and the art of recognizing a lost cause. Nat Cell Biol 3:E51–E53
    • (2001) Nat Cell Biol , vol.3 , pp. E51-E53
    • McClellan, A.J.1    Frydman, J.2
  • 15
    • 60749101582 scopus 로고    scopus 로고
    • Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1
    • Westerheide SD, Anckar J, Stevens SM Jr, Sistonen L, Morimoto RI (2009) Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1. Science 323:1063–1066
    • (2009) Science , vol.323 , pp. 1063-1066
    • Westerheide, S.D.1    Anckar, J.2    Stevens, S.M.3    Sistonen, L.4    Morimoto, R.I.5
  • 16
    • 34249671789 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and molecular pathways of disease
    • Pieczenik SR, Neustadt J (2007) Mitochondrial dysfunction and molecular pathways of disease. Exp Mol Pathol 83:84–92
    • (2007) Exp Mol Pathol , vol.83 , pp. 84-92
    • Pieczenik, S.R.1    Neustadt, J.2
  • 17
    • 23144451444 scopus 로고    scopus 로고
    • Oxidative stress: Molecular perception and transduction of signals triggering antioxidant gene defenses
    • Scandalios JG (2005) Oxidative stress: molecular perception and transduction of signals triggering antioxidant gene defenses. Braz J Med Biol Res 38:995–1014
    • (2005) Braz J Med Biol Res , vol.38 , pp. 995-1014
    • Scandalios, J.G.1
  • 18
    • 34250864375 scopus 로고    scopus 로고
    • Reactive carbonyls and oxidative stress: Potential for therapeutic intervention
    • Ellis EM (2007) Reactive carbonyls and oxidative stress: potential for therapeutic intervention. Pharmacol Ther 115:13–24
    • (2007) Pharmacol Ther , vol.115 , pp. 13-24
    • Ellis, E.M.1
  • 19
    • 34447131004 scopus 로고    scopus 로고
    • Molecular mechanisms of nitrosative stress-mediated protein misfolding in neurodegenerative diseases
    • Nakamura T, Lipton SA (2007) Molecular mechanisms of nitrosative stress-mediated protein misfolding in neurodegenerative diseases. Cell Mol Life Sci 64:1609–1620
    • (2007) Cell Mol Life Sci , vol.64 , pp. 1609-1620
    • Nakamura, T.1    Lipton, S.A.2
  • 20
    • 4344677922 scopus 로고    scopus 로고
    • Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and “aggresomes” during oxidative stress, aging, and disease
    • Grune T, Jung T, Merker K, Davies KJ (2004) Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and “aggresomes” during oxidative stress, aging, and disease. Int J Biochem Cell Biol 36:2519–2530
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2519-2530
    • Grune, T.1    Jung, T.2    Merker, K.3    Davies, K.J.4
  • 21
    • 33644639061 scopus 로고    scopus 로고
    • Proteasomal defense of oxidative protein modifications
    • Poppek D, Grune T (2006) Proteasomal defense of oxidative protein modifications. Antioxid Redox Signal 8:173–184
    • (2006) Antioxid Redox Signal , vol.8 , pp. 173-184
    • Poppek, D.1    Grune, T.2
  • 22
    • 35848957485 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and oxidative stress: A vicious cycle or a double-edged sword?
    • Malhotra JD, Kaufman RJ (2007) Endoplasmic reticulum stress and oxidative stress: a vicious cycle or a double-edged sword? Antioxid Redox Signal 9:2277–2293
    • (2007) Antioxid Redox Signal , vol.9 , pp. 2277-2293
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 23
    • 0742323115 scopus 로고    scopus 로고
    • Mitochondrial calcium uptake stimulates nitric oxide production in mitochondria of bovine vascular endothelial cells
    • Dedkova EN, Ji X, Lipsius SL, Blatter LA (2004) Mitochondrial calcium uptake stimulates nitric oxide production in mitochondria of bovine vascular endothelial cells. Am J Physiol Cell Physiol 286:C406–C415
    • (2004) Am J Physiol Cell Physiol , vol.286 , pp. C406-C415
    • Dedkova, E.N.1    Ji, X.2    Lipsius, S.L.3    Blatter, L.A.4
  • 24
    • 58949099388 scopus 로고    scopus 로고
    • Effects of overexpression of huntingtin proteins on mitochondrial integrity
    • Wang H, Lim PJ, Karbowski M, Monteiro MJ (2009) Effects of overexpression of huntingtin proteins on mitochondrial integrity. Hum Mol Genet 18:737–752
    • (2009) Hum Mol Genet , vol.18 , pp. 737-752
    • Wang, H.1    Lim, P.J.2    Karbowski, M.3    Monteiro, M.J.4
  • 27
    • 65549139675 scopus 로고    scopus 로고
    • Regulation of the aging process by autophagy
    • Salminen A, Kaarniranta K (2009) Regulation of the aging process by autophagy. Trends Mol Med 15:217–224
    • (2009) Trends Mol Med , vol.15 , pp. 217-224
    • Salminen, A.1    Kaarniranta, K.2
  • 28
    • 46349099816 scopus 로고    scopus 로고
    • Novel mechanism of elimination of malfunctioning mitochondria (Mitoptosis): Formation of mitoptotic bodies and extrusion of mitochondrial material from the cell
    • Lyamzaev KG, Nepryakhina OK, Saprunova VB, Bakeeva LE, Pletjushkina OY, Chernyak BV, Skulachev VP (2008) Novel mechanism of elimination of malfunctioning mitochondria (mitoptosis): formation of mitoptotic bodies and extrusion of mitochondrial material from the cell. Biochim Biophys Acta 1777:817–825
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 817-825
    • Lyamzaev, K.G.1    Nepryakhina, O.K.2    Saprunova, V.B.3    Bakeeva, L.E.4    Pletjushkina, O.Y.5    Chernyak, B.V.6    Skulachev, V.P.7
  • 30
    • 28544442609 scopus 로고    scopus 로고
    • Protein translocation across biological membranes
    • Wickner W, Schekman R (2005) Protein translocation across biological membranes. Science 310:1452–1456
    • (2005) Science , vol.310 , pp. 1452-1456
    • Wickner, W.1    Schekman, R.2
  • 33
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder M, Kaufman RJ (2005) The mammalian unfolded protein response. Annu Rev Biochem 74:739–789
    • (2005) Annu Rev Biochem , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 34
    • 41749108854 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in disease pathogenesis
    • Lin JH, Walter P, Yen TS (2008) Endoplasmic reticulum stress in disease pathogenesis. Annu Rev Pathol 3:399–425
    • (2008) Annu Rev Pathol , vol.3 , pp. 399-425
    • Lin, J.H.1    Walter, P.2    Yen, T.S.3
  • 36
    • 35348827324 scopus 로고    scopus 로고
    • That which does not kill me makes me stronger: Adapting to chronic ER stress
    • Rutkowski DT, Kaufman RJ (2007) That which does not kill me makes me stronger: adapting to chronic ER stress. Trends Biochem Sci 32:469–476
    • (2007) Trends Biochem Sci , vol.32 , pp. 469-476
    • Rutkowski, D.T.1    Kaufman, R.J.2
  • 37
    • 0346487261 scopus 로고    scopus 로고
    • Role of calcium and superoxide dismutase in sensitizing mitochondria to peroxynitrite-induced permeability transition
    • Brookes PS, rley-Usmar VM (2004) Role of calcium and superoxide dismutase in sensitizing mitochondria to peroxynitrite-induced permeability transition. Am J Physiol Heart Circ Physiol 286:H39–H46
    • (2004) Am J Physiol Heart Circ Physiol , vol.286 , pp. H39-H46
    • Brookes, P.S.1    Rley-Usmar, V.M.2
  • 38
    • 0037087782 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress and cell death in astrocytes – requirement for stored Ca2+ and sustained opening of the permeability transition pore
    • Jacobson J, Duchen MR (2002) Mitochondrial oxidative stress and cell death in astrocytes – requirement for stored Ca2+ and sustained opening of the permeability transition pore. J Cell Sci 115:1175–1188
    • (2002) J Cell Sci , vol.115 , pp. 1175-1188
    • Jacobson, J.1    Duchen, M.R.2
  • 39
    • 0034604675 scopus 로고    scopus 로고
    • Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response
    • Pagani M, Fabbri M, Benedetti C, Fassio A, Pilati S, Bulleid NJ, Cabibbo A, Sitia R (2000) Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response. J Biol Chem 275:23685–23692
    • (2000) J Biol Chem , vol.275 , pp. 23685-23692
    • Pagani, M.1    Fabbri, M.2    Benedetti, C.3    Fassio, A.4    Pilati, S.5    Bulleid, N.J.6    Cabibbo, A.7    Sitia, R.8
  • 40
    • 34247098374 scopus 로고    scopus 로고
    • Accumulation of misfolded protein through nitrosative stress linked to neurodegenerative disorders
    • Uehara T (2007) Accumulation of misfolded protein through nitrosative stress linked to neurodegenerative disorders. Antioxid Redox Signal 9:597–601
    • (2007) Antioxid Redox Signal , vol.9 , pp. 597-601
    • Uehara, T.1
  • 43
    • 56349144637 scopus 로고    scopus 로고
    • Thirty years of protein translocation into mitochondria: Unexpectedly complex and still puzzling
    • Mokranjac D, Neupert W (2009) Thirty years of protein translocation into mitochondria: unexpectedly complex and still puzzling. Biochim Biophys Acta 1793:33–41
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 33-41
    • Mokranjac, D.1    Neupert, W.2
  • 44
    • 38549101188 scopus 로고    scopus 로고
    • Quality control of mitochondria: Protection against neurodegeneration and ageing
    • Tatsuta T, Langer T (2008) Quality control of mitochondria: protection against neurodegeneration and ageing. EMBO J 27:306–314
    • (2008) EMBO J , vol.27 , pp. 306-314
    • Tatsuta, T.1    Langer, T.2
  • 45
    • 53049099984 scopus 로고    scopus 로고
    • Short-and long-term alterations of mitochondrial morphology dynamics and mtDNA after transient oxidative stress
    • Jendrach M, Mai S, Pohl S, Voth M, Bereiter-Hahn J (2008) Short-and long-term alterations of mitochondrial morphology dynamics and mtDNA after transient oxidative stress. Mitochondrion 8:293–304
    • (2008) Mitochondrion , vol.8 , pp. 293-304
    • Jendrach, M.1    Mai, S.2    Pohl, S.3    Voth, M.4    Bereiter-Hahn, J.5
  • 46
    • 0024458504 scopus 로고
    • Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
    • Ostermann J, Horwich AL, Neupert W, Hartl FU (1989) Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature 341:125–130
    • (1989) Nature , vol.341 , pp. 125-130
    • Ostermann, J.1    Horwich, A.L.2    Neupert, W.3    Hartl, F.U.4
  • 47
    • 36549006049 scopus 로고    scopus 로고
    • Importance of the lon protease in mitochondrial maintenance and the significance of declining lon in aging
    • Ngo JK, Davies KJ (2007) Importance of the lon protease in mitochondrial maintenance and the significance of declining lon in aging. Ann NY Acad Sci 1119:78–87
    • (2007) Ann NY Acad Sci , vol.1119 , pp. 78-87
    • Ngo, J.K.1    Davies, K.J.2
  • 49
    • 0842330592 scopus 로고    scopus 로고
    • Genetic defects in fatty acid beta-oxidation and acyl-CoA dehydrogenases
    • Gregersen N, Bross P, Andresen BS (2004) Genetic defects in fatty acid beta-oxidation and acyl-CoA dehydrogenases. Eur J Biochem 271:470–482
    • (2004) Eur J Biochem , vol.271 , pp. 470-482
    • Gregersen, N.1    Bross, P.2    Andresen, B.S.3
  • 50
    • 24944456875 scopus 로고    scopus 로고
    • Protein misfolding, aggregation, and degradation in disease
    • Gregersen N, Bolund L, Bross P (2005) Protein misfolding, aggregation, and degradation in disease. Mol Biotechnol 31: 141–150
    • (2005) Mol Biotechnol , vol.31 , pp. 141-150
    • Gregersen, N.1    Bolund, L.2    Bross, P.3
  • 53
    • 34848861368 scopus 로고    scopus 로고
    • ClpP mediates activation of a mitochondrial unfolded protein response in C. Elegans
    • Haynes CM, Petrova K, Benedetti C, Yang Y, Ron D (2007) ClpP mediates activation of a mitochondrial unfolded protein response in C. elegans. Dev Cell 13:467–480
    • (2007) Dev Cell , vol.13 , pp. 467-480
    • Haynes, C.M.1    Petrova, K.2    Benedetti, C.3    Yang, Y.4    Ron, D.5
  • 54
    • 37849038317 scopus 로고    scopus 로고
    • The chop gene contains an element for the positive regulation of the mitochondrial unfolded protein response
    • Horibe T, Hoogenraad NJ (2007) The chop gene contains an element for the positive regulation of the mitochondrial unfolded protein response. PLoS One 2:e835
    • (2007) Plos One , vol.2
    • Horibe, T.1    Hoogenraad, N.J.2
  • 55
    • 0036314984 scopus 로고    scopus 로고
    • Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response
    • Ma Y, Brewer JW, Diehl JA, Hendershot LM (2002) Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response. J Mol Biol 318:1351–1365
    • (2002) J Mol Biol , vol.318 , pp. 1351-1365
    • Ma, Y.1    Brewer, J.W.2    Diehl, J.A.3    Hendershot, L.M.4
  • 56
    • 0029760957 scopus 로고    scopus 로고
    • Redox regulation of transcriptional activators
    • Sun Y, Oberley LW (1996) Redox regulation of transcriptional activators. Free Radic Biol Med 21:335–348
    • (1996) Free Radic Biol Med , vol.21 , pp. 335-348
    • Sun, Y.1    Oberley, L.W.2
  • 57
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
    • D’Autreaux B, Toledano MB (2007) ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nat Rev Mol Cell Biol 8:813–824
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 813-824
    • D’Autreaux, B.1    Toledano, M.B.2
  • 58
    • 67649840689 scopus 로고    scopus 로고
    • Regulation of superoxide dismutase genes: Implications in disease
    • Miao L, St Clair DK (2009) Regulation of superoxide dismutase genes: Implications in disease. Free Radic Biol Med 47:344–56
    • (2009) Free Radic Biol Med , vol.47 , pp. 344-356
    • Miao, L.1    St Clair, D.K.2
  • 59
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy MP (2009) How mitochondria produce reactive oxygen species. Biochem J 417:1–13
    • (2009) Biochem J , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 60
    • 57649233079 scopus 로고    scopus 로고
    • The role of mitochondria in reactive oxygen species metabolism and signaling
    • Starkov AA (2008) The role of mitochondria in reactive oxygen species metabolism and signaling. Ann NY Acad Sci 1147:37–52
    • (2008) Ann NY Acad Sci , vol.1147 , pp. 37-52
    • Starkov, A.A.1
  • 62
    • 0037160091 scopus 로고    scopus 로고
    • Topology of superoxide production from different sites in the mitochondrial electron transport chain
    • St-Pierre J, Buckingham JA, Roebuck SJ, Brand MD (2002) Topology of superoxide production from different sites in the mitochondrial electron transport chain. J Biol Chem 277:44784–44790
    • (2002) J Biol Chem , vol.277 , pp. 44784-44790
    • St-Pierre, J.1    Buckingham, J.A.2    Roebuck, S.J.3    Brand, M.D.4
  • 63
    • 4344630828 scopus 로고    scopus 로고
    • The role of oxidative damage in the neuropathology of organic acidurias: Insights from animal studies
    • Wajner M, Latini A, Wyse AT, Dutra-Filho CS (2004) The role of oxidative damage in the neuropathology of organic acidurias: insights from animal studies. J Inherit Metab Dis 27:427–448
    • (2004) J Inherit Metab Dis , vol.27 , pp. 427-448
    • Wajner, M.1    Latini, A.2    Wyse, A.T.3    Dutra-Filho, C.S.4
  • 64
    • 64049107461 scopus 로고    scopus 로고
    • Medium-chain fatty acids accumulating in MCAD deficiency elicit lipid and protein oxidative damage and decrease non-enzymatic antioxidant defenses in rat brain
    • Schuck PF, Ferreira GC, Moura AP, Busanello EN, Tonin AM, Dutra-Filho CS, Wajner M (2009) Medium-chain fatty acids accumulating in MCAD deficiency elicit lipid and protein oxidative damage and decrease non-enzymatic antioxidant defenses in rat brain. Neurochem Int 54:519–525
    • (2009) Neurochem Int , vol.54 , pp. 519-525
    • Schuck, P.F.1    Ferreira, G.C.2    Moura, A.P.3    Busanello, E.N.4    Tonin, A.M.5    Dutra-Filho, C.S.6    Wajner, M.7
  • 65
    • 57049138178 scopus 로고    scopus 로고
    • Disease-causing missense mutations affect enzymatic activity, stability and oligomerization of glutaryl-CoA dehydrogenase (GCDH)
    • Keyser B, Muhlhausen C, Dickmanns A, Christensen E, Muschol N, Ullrich K, Braulke T (2008) Disease-causing missense mutations affect enzymatic activity, stability and oligomerization of glutaryl-CoA dehydrogenase (GCDH). Hum Mol Genet 17:3854–3863
    • (2008) Hum Mol Genet , vol.17 , pp. 3854-3863
    • Keyser, B.1    Muhlhausen, C.2    Dickmanns, A.3    Christensen, E.4    Muschol, N.5    Ullrich, K.6    Braulke, T.7
  • 67
    • 0242268107 scopus 로고    scopus 로고
    • Stage-specific enhanced expression of mitochondrial fusion and fission factors during spermatogenesis in rat testis
    • Honda S, Hirose S (2003) Stage-specific enhanced expression of mitochondrial fusion and fission factors during spermatogenesis in rat testis. Biochem Biophys Res Commun 311:424–432
    • (2003) Biochem Biophys Res Commun , vol.311 , pp. 424-432
    • Honda, S.1    Hirose, S.2
  • 68
    • 27544466847 scopus 로고    scopus 로고
    • Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes
    • Okamoto K, Shaw JM (2005) Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes. Annu Rev Genet 39:503–536
    • (2005) Annu Rev Genet , vol.39 , pp. 503-536
    • Okamoto, K.1    Shaw, J.M.2
  • 70
    • 33751544005 scopus 로고    scopus 로고
    • Mitochondrial dynamics generate equal distribution but patchwork localization of respiratory complex I
    • Busch KB, Bereiter-Hahn J, Wittig I, Schagger H, Jendrach M (2006) Mitochondrial dynamics generate equal distribution but patchwork localization of respiratory complex I. Mol Membr Biol 23:509–520
    • (2006) Mol Membr Biol , vol.23 , pp. 509-520
    • Busch, K.B.1    Bereiter-Hahn, J.2    Wittig, I.3    Schagger, H.4    Jendrach, M.5
  • 73
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima N, Levine B, Cuervo AM, Klionsky DJ (2008) Autophagy fights disease through cellular self-digestion. Nature 451:1069–1075
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 74
    • 34848920863 scopus 로고    scopus 로고
    • ROS, mitochondria and the regulation of autophagy
    • Scherz-Shouval R, Elazar Z (2007) ROS, mitochondria and the regulation of autophagy. Trends Cell Biol 17:422–427
    • (2007) Trends Cell Biol , vol.17 , pp. 422-427
    • Scherz-Shouval, R.1    Elazar, Z.2
  • 76
    • 64249133725 scopus 로고    scopus 로고
    • S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury
    • Cho DH, Nakamura T, Fang J, Cieplak P, Godzik A, Gu Z, Lipton SA (2009) S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury. Science 324:102–105
    • (2009) Science , vol.324 , pp. 102-105
    • Cho, D.H.1    Nakamura, T.2    Fang, J.3    Cieplak, P.4    Godzik, A.5    Gu, Z.6    Lipton, S.A.7
  • 77
    • 34247464726 scopus 로고    scopus 로고
    • Identification of carbonylated proteins from enriched rat skeletal muscle mitochondria using affinity chromatography-stable isotope labeling and tandem mass spectrometry
    • Meany DL, Xie H, Thompson LV, Arriaga EA, Griffin TJ (2007) Identification of carbonylated proteins from enriched rat skeletal muscle mitochondria using affinity chromatography-stable isotope labeling and tandem mass spectrometry. Proteomics 7:1150–1163
    • (2007) Proteomics , vol.7 , pp. 1150-1163
    • Meany, D.L.1    Xie, H.2    Thompson, L.V.3    Arriaga, E.A.4    Griffin, T.J.5
  • 78
    • 0242606930 scopus 로고    scopus 로고
    • A unifying view of ageing and disease: The double-agent theory
    • Lane N (2003) A unifying view of ageing and disease: the double-agent theory. J Theor Biol 225:531–540
    • (2003) J Theor Biol , vol.225 , pp. 531-540
    • Lane, N.1
  • 79
    • 33750729203 scopus 로고    scopus 로고
    • Theories of biological aging: Genes, proteins, and free radicals
    • Rattan SI (2006) Theories of biological aging: genes, proteins, and free radicals. Free Radic Res 40:1230–1238
    • (2006) Free Radic Res , vol.40 , pp. 1230-1238
    • Rattan, S.I.1
  • 80
    • 0020365443 scopus 로고
    • Separation and characterization of the aldehydic products of lipid peroxidation stimulated by ADP-Fe2+ in rat liver microsomes
    • Esterbauer H, Cheeseman KH, Dianzani MU, Poli G, Slater TF (1982) Separation and characterization of the aldehydic products of lipid peroxidation stimulated by ADP-Fe2+ in rat liver microsomes. Biochem J 208:129–140
    • (1982) Biochem J , vol.208 , pp. 129-140
    • Esterbauer, H.1    Cheeseman, K.H.2    Dianzani, M.U.3    Poli, G.4    Slater, T.F.5
  • 81
    • 0033571012 scopus 로고    scopus 로고
    • Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose
    • Pt 1
    • Thornalley PJ, Langborg A, Minhas HS (1999) Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose. Biochem J 344(Pt 1):109–116
    • (1999) Biochem J , vol.344 , pp. 109-116
    • Thornalley, P.J.1    Langborg, A.2    Minhas, H.S.3
  • 82
    • 57149096282 scopus 로고    scopus 로고
    • Quantitative proteomic profiling of muscle type-dependent and age-dependent protein carbonylation in rat skeletal muscle mitochondria
    • Feng J, Xie H, Meany DL, Thompson LV, Arriaga EA, Griffin TJ (2008) Quantitative proteomic profiling of muscle type-dependent and age-dependent protein carbonylation in rat skeletal muscle mitochondria. J Gerontol A Biol Sci Med Sci 63:1137–1152
    • (2008) J Gerontol a Biol Sci Med Sci , vol.63 , pp. 1137-1152
    • Feng, J.1    Xie, H.2    Meany, D.L.3    Thompson, L.V.4    Arriaga, E.A.5    Griffin, T.J.6
  • 83
    • 0344084088 scopus 로고    scopus 로고
    • High-throughput proteomic-based identification of oxidatively induced protein carbonylation in mouse brain
    • Soreghan BA, Yang F, Thomas SN, Hsu J, Yang AJ (2003) High-throughput proteomic-based identification of oxidatively induced protein carbonylation in mouse brain. Pharm Res 20: 1713–1720
    • (2003) Pharm Res , vol.20 , pp. 1713-1720
    • Soreghan, B.A.1    Yang, F.2    Thomas, S.N.3    Hsu, J.4    Yang, A.J.5
  • 84
    • 20444400257 scopus 로고    scopus 로고
    • Redox redux: Revisiting PTPs and the control of cell signaling
    • Tonks NK (2005) Redox redux: revisiting PTPs and the control of cell signaling. Cell 121:667–670
    • (2005) Cell , vol.121 , pp. 667-670
    • Tonks, N.K.1
  • 85
    • 33947579630 scopus 로고    scopus 로고
    • Enzyme-catalyzed side reactions with molecular oxygen may contribute to cell signaling and neurodegenerative diseases
    • Bunik VI, Schloss JV, Pinto JT, Gibson GE, Cooper AJ (2007) Enzyme-catalyzed side reactions with molecular oxygen may contribute to cell signaling and neurodegenerative diseases. Neurochem Res 32:871–891
    • (2007) Neurochem Res , vol.32 , pp. 871-891
    • Bunik, V.I.1    Schloss, J.V.2    Pinto, J.T.3    Gibson, G.E.4    Cooper, A.J.5
  • 86
    • 33646948530 scopus 로고    scopus 로고
    • Parkinson’s disease brain mitochondrial complex I has oxidatively damaged sub- units and is functionally impaired and misassembled
    • Keeney PM, Xie J, Capaldi RA, Bennett JP Jr (2006) Parkinson’s disease brain mitochondrial complex I has oxidatively damaged sub- units and is functionally impaired and misassembled. J Neurosci 26:5256–5264
    • (2006) J Neurosci , vol.26 , pp. 5256-5264
    • Keeney, P.M.1    Xie, J.2    Capaldi, R.A.3    Bennett, J.P.4
  • 87
    • 77951978533 scopus 로고    scopus 로고
    • Misfolding of shortchain acyl-CoA dehydrogenase leads to mitochondrial fission and oxidative stress
    • Schmidt SP, Corydon TJ, Pedersen CB, Bross P, & Gregersen N. (2010) Misfolding of shortchain acyl-CoA dehydrogenase leads to mitochondrial fission and oxidative stress. Mol Genet Metab 100:155–162
    • (2010) Mol Genet Metab , vol.100 , pp. 155-162
    • Schmidt, S.P.1    Corydon, T.J.2    Pedersen, C.B.3    Bross, P.4    Gregersen, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.