메뉴 건너뛰기




Volumn 35, Issue 12, 2010, Pages 1880-1915

Cellular stress responses, mitostress and carnitine insufficiencies as critical determinants in aging and neurodegenerative disorders: Role of hormesis and vitagenes

Author keywords

Acetylcarnitine; Cellular stress response; Hormesis; Mitochondrial bioenergetics; Redox state; Vitagenes

Indexed keywords

ACETYLCARNITINE; ACYLCARNITINE; ADENOSINE TRIPHOSPHATASE (CALCIUM); CARNITINE; CATALASE; COPPER ZINC SUPEROXIDE DISMUTASE; HEAT SHOCK PROTEIN; ISOPROSTANE; MITOCHONDRIAL DNA; MITOFUSIN 2; OXYGEN RADICAL; REACTIVE OXYGEN METABOLITE; SIRTUIN; THIOREDOXIN; TRANSCRIPTION FACTOR;

EID: 78651324323     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11064-010-0307-z     Document Type: Article
Times cited : (68)

References (221)
  • 1
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • 1:CAS:528:DC%2BD1cXhslOmtLw%3D 18276881
    • WE Balch RI Morimoto A Dillin JW Kelly 2008 Adapting proteostasis for disease intervention Science 319 916 919 1:CAS:528:DC%2BD1cXhslOmtLw%3D 18276881
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 2
    • 77449098537 scopus 로고    scopus 로고
    • Cellular stress responses, the hormesis paradigm and vitagenes: Novel targets for therapeutic intervention in neurodegenerative disorders
    • 1:CAS:528:DC%2BC3cXos1Cntb8%3D
    • V Calabrese C Cornelius AT Dinkova-Kostova EJ Calabrese MP Mattson 2010 Cellular stress responses, the hormesis paradigm and vitagenes: novel targets for therapeutic intervention in neurodegenerative disorders Antioxid Redox Signal 610 285 308 1:CAS:528:DC%2BC3cXos1Cntb8%3D
    • (2010) Antioxid Redox Signal , vol.610 , pp. 285-308
    • Calabrese, V.1    Cornelius, C.2    Dinkova-Kostova, A.T.3    Calabrese, E.J.4    Mattson, M.P.5
  • 3
    • 67649213915 scopus 로고    scopus 로고
    • Vitagenes, cellular stress response and acetylcarnitine: Relevance to hormesis
    • 1:CAS:528:DC%2BD1MXnsVSlsrs%3D 19449442
    • V Calabrese C Cornelius AT Dinkova-Kostova EJ Calabrese 2009 Vitagenes, cellular stress response and acetylcarnitine: relevance to hormesis Biofactors 35 146 160 1:CAS:528:DC%2BD1MXnsVSlsrs%3D 19449442
    • (2009) Biofactors , vol.35 , pp. 146-160
    • Calabrese, V.1    Cornelius, C.2    Dinkova-Kostova, A.T.3    Calabrese, E.J.4
  • 4
    • 33645999557 scopus 로고
    • Oxygen poisoning and x-irradiation: A mechanism in common
    • 1:CAS:528:DyaG2cXlsl2huw%3D%3D 13156638
    • R Gerschman DL Gilbert SW Nye P Dwyer WO Fenn 1954 Oxygen poisoning and x-irradiation: a mechanism in common Science 119 623 626 1:CAS:528: DyaG2cXlsl2huw%3D%3D 13156638
    • (1954) Science , vol.119 , pp. 623-626
    • Gerschman, R.1    Gilbert, D.L.2    Nye, S.W.3    Dwyer, P.4    Fenn, W.O.5
  • 5
    • 34447340094 scopus 로고
    • Influence of x-irradiation on oxygen poisoning in mice
    • 1:CAS:528:DyaG2cXmtVKksQ%3D%3D 13177582
    • R Gerschman DL Gilbert SW Nye WO Fenn 1954 Influence of x-irradiation on oxygen poisoning in mice Proc Soc Exp Biol Med 86 27 29 1:CAS:528: DyaG2cXmtVKksQ%3D%3D 13177582
    • (1954) Proc Soc Exp Biol Med , vol.86 , pp. 27-29
    • Gerschman, R.1    Gilbert, D.L.2    Nye, S.W.3    Fenn, W.O.4
  • 6
    • 77049308856 scopus 로고
    • Aging: A theory based on free radical and radiation chemistry
    • 1:STN:280:DyaG28%2FosVygsw%3D%3D 13332224
    • D Harman 1956 Aging: a theory based on free radical and radiation chemistry J Gerontol 11 298 300 1:STN:280:DyaG28%2FosVygsw%3D%3D 13332224
    • (1956) J Gerontol , vol.11 , pp. 298-300
    • Harman, D.1
  • 7
    • 0015319592 scopus 로고
    • The biologic clock: The mitochondria?
    • 1:STN:280:DyaE387lsVCmug%3D%3D 5016631
    • D Harman 1972 The biologic clock: the mitochondria? J Am Geriatr Soc 20 145 147 1:STN:280:DyaE387lsVCmug%3D%3D 5016631
    • (1972) J Am Geriatr Soc , vol.20 , pp. 145-147
    • Harman, D.1
  • 8
    • 18944388449 scopus 로고    scopus 로고
    • Body size, energy metabolism and lifespan
    • 15855403
    • JR Speakman 2005 Body size, energy metabolism and lifespan J Exp Biol 208 1717 1730 15855403
    • (2005) J Exp Biol , vol.208 , pp. 1717-1730
    • Speakman, J.R.1
  • 10
    • 8344282655 scopus 로고    scopus 로고
    • The role of oxidative damage and stress in aging
    • 1:CAS:528:DC%2BD2cXpslGmsrw%3D 15541775
    • A Bokov A Chaudhuri A Richardson 2004 The role of oxidative damage and stress in aging Mech Ageing Dev 125 811 826 1:CAS:528:DC%2BD2cXpslGmsrw%3D 15541775
    • (2004) Mech Ageing Dev , vol.125 , pp. 811-826
    • Bokov, A.1    Chaudhuri, A.2    Richardson, A.3
  • 11
    • 0030038103 scopus 로고    scopus 로고
    • Oxidative stress, caloric restriction, and aging
    • 1:STN:280:DyaK283nsFGruw%3D%3D 8658196
    • R Sohal R Weindruch 1996 Oxidative stress, caloric restriction, and aging Science 273 59 63 1:STN:280:DyaK283nsFGruw%3D%3D 8658196
    • (1996) Science , vol.273 , pp. 59-63
    • Sohal, R.1    Weindruch, R.2
  • 13
    • 75149165994 scopus 로고    scopus 로고
    • Update on the oxidative stress theory of aging: Does oxidative stress play a role in aging or healthy aging?
    • 1:CAS:528:DC%2BC3cXhtlGhtbo%3D 20036736
    • AB Salmon A Richardson VI Pérez 2010 Update on the oxidative stress theory of aging: does oxidative stress play a role in aging or healthy aging? Free Radic Biol Med 48 642 655 1:CAS:528:DC%2BC3cXhtlGhtbo%3D 20036736
    • (2010) Free Radic Biol Med , vol.48 , pp. 642-655
    • Salmon, A.B.1    Richardson, A.2    Pérez, V.I.3
  • 14
    • 4544327666 scopus 로고    scopus 로고
    • Redox regulation in neurodegeneration and longevity: Role of the heme oxygenase and HSP70 systems in brain stress tolerance
    • 1:CAS:528:DC%2BD2cXntFCgsL8%3D 15345150
    • V Calabrese AM Giuffrida Stella DA Butterfield G Scapagnini 2004 Redox regulation in neurodegeneration and longevity: role of the heme oxygenase and HSP70 systems in brain stress tolerance Antioxid Redox Signal 6 895 913 1:CAS:528:DC%2BD2cXntFCgsL8%3D 15345150
    • (2004) Antioxid Redox Signal , vol.6 , pp. 895-913
    • Calabrese, V.1    Giuffrida Stella, A.M.2    Butterfield, D.A.3    Scapagnini, G.4
  • 15
    • 33646681219 scopus 로고    scopus 로고
    • Redox regulation of heat shock protein expression by signaling involving nitric oxide and carbon monoxide: Relevance to brain aging, neurodegenerative disorders, and longevity
    • 1:CAS:528:DC%2BD28Xkt12qsrw%3D 16677090
    • V Calabrese DA Butterfield G Scapagnini AM Stella MD Maines 2006 Redox regulation of heat shock protein expression by signaling involving nitric oxide and carbon monoxide: relevance to brain aging, neurodegenerative disorders, and longevity Antioxid Redox Signal 8 444 477 1:CAS:528:DC%2BD28Xkt12qsrw%3D 16677090
    • (2006) Antioxid Redox Signal , vol.8 , pp. 444-477
    • Calabrese, V.1    Butterfield, D.A.2    Scapagnini, G.3    Stella, A.M.4    Maines, M.D.5
  • 17
    • 46649104435 scopus 로고    scopus 로고
    • Age-related decrease in expression of mitochondrial DNA encoded subunits of cytochrome c oxidase in Drosophila melanogaster
    • 1:CAS:528:DC%2BD1cXosVOnsbs%3D 18538373
    • RS Sohal D Toroser C Brégère RJ Mockett WC Orr 2008 Age-related decrease in expression of mitochondrial DNA encoded subunits of cytochrome c oxidase in Drosophila melanogaster Mech Ageing Dev 129 558 561 1:CAS:528:DC%2BD1cXosVOnsbs%3D 18538373
    • (2008) Mech Ageing Dev , vol.129 , pp. 558-561
    • Sohal, R.S.1    Toroser, D.2    Brégère, C.3    Mockett, R.J.4    Orr, W.C.5
  • 18
    • 77954675024 scopus 로고    scopus 로고
    • Involvement of oxidatively damaged DNA and repair in cancer development and aging
    • 1:CAS:528:DC%2BC3cXms1Wls7s%3D 20589166
    • B Tudek A Winczura J Janik A Siomek M Foksinski R Oliński 2010 Involvement of oxidatively damaged DNA and repair in cancer development and aging Am J Transl Res 2 254 284 1:CAS:528:DC%2BC3cXms1Wls7s%3D 20589166
    • (2010) Am J Transl Res , vol.2 , pp. 254-284
    • Tudek, B.1    Winczura, A.2    Janik, J.3    Siomek, A.4    Foksinski, M.5    Oliński, R.6
  • 19
    • 78549237781 scopus 로고    scopus 로고
    • Oxidation in the nucleotide pool, the DNA Damage response and cellular senescence: Defective bricks build a defective house
    • Epub ahead of print
    • Rai P (2010) Oxidation in the nucleotide pool, the DNA Damage response and cellular senescence: defective bricks build a defective house. Mutat Res. [Epub ahead of print]
    • (2010) Mutat Res.
    • Rai, P.1
  • 20
    • 69049109744 scopus 로고    scopus 로고
    • Biomarkers of oxidative and nitrosative damage in Alzheimer's disease and mild cognitive impairment
    • 1:CAS:528:DC%2BD1MXht1GntLrE 19376275
    • F Mangialasche MC Polidori R Monastero S Ercolani C Camarda R Cecchetti P Mecocci 2009 Biomarkers of oxidative and nitrosative damage in Alzheimer's disease and mild cognitive impairment Ageing Res Rev 8 285 305 1:CAS:528:DC%2BD1MXht1GntLrE 19376275
    • (2009) Ageing Res Rev , vol.8 , pp. 285-305
    • Mangialasche, F.1    Polidori, M.C.2    Monastero, R.3    Ercolani, S.4    Camarda, C.5    Cecchetti, R.6    Mecocci, P.7
  • 21
    • 0032967445 scopus 로고    scopus 로고
    • Mitochondrial DNA 4977 bp deletion and OH8dG levels correlate in the brain of aged subjects but not Alzheimer's disease patients
    • 1:CAS:528:DyaK1MXjsVOlu7o%3D 10336891
    • AM Lezza P Mecocci A Cormio MF Beal A Cherubini P Cantatore U Senin MN Gadaleta 1999 Mitochondrial DNA 4977 bp deletion and OH8dG levels correlate in the brain of aged subjects but not Alzheimer's disease patients FASEB J 13 1083 1088 1:CAS:528:DyaK1MXjsVOlu7o%3D 10336891
    • (1999) FASEB J , vol.13 , pp. 1083-1088
    • Lezza, A.M.1    Mecocci, P.2    Cormio, A.3    Beal, M.F.4    Cherubini, A.5    Cantatore, P.6    Senin, U.7    Gadaleta, M.N.8
  • 22
    • 45449100900 scopus 로고    scopus 로고
    • DNA damage, DNA repair, ageing and age-related disease
    • 1:CAS:528:DC%2BD1cXns1Shtbg%3D 18420253
    • DM Wilson 3rd VA Bohr PJ McKinnon 2008 DNA damage, DNA repair, ageing and age-related disease Mech Ageing Dev 129 349 352 1:CAS:528:DC%2BD1cXns1Shtbg%3D 18420253
    • (2008) Mech Ageing Dev , vol.129 , pp. 349-352
    • Wilson III, D.M.1    Bohr, V.A.2    McKinnon, P.J.3
  • 23
    • 38049057905 scopus 로고    scopus 로고
    • DNA damage in telomeres and mitochondria during cellular senescence: Is there a connection?
    • 1:CAS:528:DC%2BD1cXisFyqsA%3D%3D 17986462
    • JF Passos G Saretzki T von Zglinicki 2007 DNA damage in telomeres and mitochondria during cellular senescence: is there a connection? Nucleic Acids Res 35 7505 7513 1:CAS:528:DC%2BD1cXisFyqsA%3D%3D 17986462
    • (2007) Nucleic Acids Res , vol.35 , pp. 7505-7513
    • Passos, J.F.1    Saretzki, G.2    Von Zglinicki, T.3
  • 25
    • 0027090431 scopus 로고
    • Relationship between antioxidants, prooxidants, and the aging process
    • 1:CAS:528:DyaK3sXhsVeqtbc%3D 1482104
    • RS Sohal WC Orr 1992 Relationship between antioxidants, prooxidants, and the aging process Ann N Y Acad Sci 663 74 84 1:CAS:528:DyaK3sXhsVeqtbc%3D 1482104
    • (1992) Ann N y Acad Sci , vol.663 , pp. 74-84
    • Sohal, R.S.1    Orr, W.C.2
  • 26
    • 33750710080 scopus 로고    scopus 로고
    • Protein oxidation and aging
    • 1:CAS:528:DC%2BD28XhtlGqs7jF 17090414
    • ER Stadtman 2006 Protein oxidation and aging Free Radic Res 40 1250 1258 1:CAS:528:DC%2BD28XhtlGqs7jF 17090414
    • (2006) Free Radic Res , vol.40 , pp. 1250-1258
    • Stadtman, E.R.1
  • 27
    • 76849104804 scopus 로고    scopus 로고
    • Differential proteomics analysis of specific carbonylated proteins in the temporal cortex of aged rats: The deterioration of antioxidant system
    • 19562484
    • Q Wang X Zhao S He Y Liu M An J Ji 2010 Differential proteomics analysis of specific carbonylated proteins in the temporal cortex of aged rats: the deterioration of antioxidant system Neurochem Res 35 13 21 19562484
    • (2010) Neurochem Res , vol.35 , pp. 13-21
    • Wang, Q.1    Zhao, X.2    He, S.3    Liu, Y.4    An, M.5    Ji, J.6
  • 28
    • 47649117452 scopus 로고    scopus 로고
    • The roles of the proteasome pathway in signal transduction and neurodegenerative diseases
    • 1:CAS:528:DC%2BD1MXntFOqtr8%3D 18500392
    • JJ Chen F Lin ZH Qin 2008 The roles of the proteasome pathway in signal transduction and neurodegenerative diseases Neurosci Bull 24 183 194 1:CAS:528:DC%2BD1MXntFOqtr8%3D 18500392
    • (2008) Neurosci Bull , vol.24 , pp. 183-194
    • Chen, J.J.1    Lin, F.2    Qin, Z.H.3
  • 29
    • 78651327805 scopus 로고    scopus 로고
    • Protein oxidative modifications in the ageing brain: Consequence for the onset of neurodegenerative disease
    • Epub ahead of print
    • Grimm S, Hoehn A, Davies KJ, Grune T (2010) Protein oxidative modifications in the ageing brain: Consequence for the onset of neurodegenerative disease. Free Radic Res. [Epub ahead of print]
    • (2010) Free Radic Res.
    • Grimm, S.1    Hoehn, A.2    Davies, K.J.3    Grune, T.4
  • 30
    • 33646687948 scopus 로고    scopus 로고
    • Friedreich's ataxia: From disease mechanisms to therapeutic interventions
    • 1:CAS:528:DC%2BD28Xkt12ru7w%3D 16677089
    • R Lodi C Tonon V Calabrese AH Schapira 2006 Friedreich's ataxia: from disease mechanisms to therapeutic interventions Antioxid Redox Signal 8 438 443 1:CAS:528:DC%2BD28Xkt12ru7w%3D 16677089
    • (2006) Antioxid Redox Signal , vol.8 , pp. 438-443
    • Lodi, R.1    Tonon, C.2    Calabrese, V.3    Schapira, A.H.4
  • 32
    • 34250886382 scopus 로고    scopus 로고
    • Highlight commentary on "redox proteomics analysis of oxidatively 3 modified proteins in G93A-SOD1 transgenic mice - A model of 4 familial amyotrophic lateral sclerosis"
    • 1:CAS:528:DC%2BD2sXntFaruro%3D 17603925
    • V Calabrese 2007 Highlight commentary on "redox proteomics analysis of oxidatively 3 modified proteins in G93A-SOD1 transgenic mice-a model of 4 familial amyotrophic lateral sclerosis" Free Radic Biol Med 43 160 162 1:CAS:528:DC%2BD2sXntFaruro%3D 17603925
    • (2007) Free Radic Biol Med , vol.43 , pp. 160-162
    • Calabrese, V.1
  • 33
    • 59249102083 scopus 로고    scopus 로고
    • The wanderings of a free radical
    • 1:CAS:528:DC%2BD1MXhs1ejs74%3D 19111608
    • B Halliwell 2009 The wanderings of a free radical Free Radic Biol Med 46 531 542 1:CAS:528:DC%2BD1MXhs1ejs74%3D 19111608
    • (2009) Free Radic Biol Med , vol.46 , pp. 531-542
    • Halliwell, B.1
  • 35
    • 33646699107 scopus 로고    scopus 로고
    • Proteomics analyses of specific protein oxidation and protein expression in aged rat brain and its modulation by l-acetylcarnitine: Insights into the mechanisms of action of this proposed therapeutic agent for CNS disorders associated with oxidative stress
    • 1:CAS:528:DC%2BD28Xkt12qsr8%3D 16677085
    • HF Poon V Calabrese M Calvani DA Butterfield 2006 Proteomics analyses of specific protein oxidation and protein expression in aged rat brain and its modulation by l-acetylcarnitine: insights into the mechanisms of action of this proposed therapeutic agent for CNS disorders associated with oxidative stress Antioxid Redox Signal 8 381 394 1:CAS:528:DC%2BD28Xkt12qsr8%3D 16677085
    • (2006) Antioxid Redox Signal , vol.8 , pp. 381-394
    • Poon, H.F.1    Calabrese, V.2    Calvani, M.3    Butterfield, D.A.4
  • 36
    • 77951216461 scopus 로고    scopus 로고
    • Identification of novel oxidized protein substrates and physiological partners of the mitochondrial ATP-dependent Lon-like protease Pim1
    • 1:CAS:528:DC%2BC3cXktFGltrc%3D 20150421
    • A Bayot M Gareil A Rogowska-Wrzesinska P Roepstorff B Friguet AL Bulteau 2010 Identification of novel oxidized protein substrates and physiological partners of the mitochondrial ATP-dependent Lon-like protease Pim1 J Biol Chem 285 11445 11457 1:CAS:528:DC%2BC3cXktFGltrc%3D 20150421
    • (2010) J Biol Chem , vol.285 , pp. 11445-11457
    • Bayot, A.1    Gareil, M.2    Rogowska-Wrzesinska, A.3    Roepstorff, P.4    Friguet, B.5    Bulteau, A.L.6
  • 37
    • 77954490419 scopus 로고    scopus 로고
    • Oxidized mitochondrial protein degradation and repair in aging and oxidative stress
    • 1:CAS:528:DC%2BC3cXot1aks7k%3D 19958171
    • N Ugarte I Petropoulos B Friguet 2010 Oxidized mitochondrial protein degradation and repair in aging and oxidative stress Antioxid Redox Signal 13 539 549 1:CAS:528:DC%2BC3cXot1aks7k%3D 19958171
    • (2010) Antioxid Redox Signal , vol.13 , pp. 539-549
    • Ugarte, N.1    Petropoulos, I.2    Friguet, B.3
  • 38
    • 75149161571 scopus 로고    scopus 로고
    • Redox proteomic analysis of carbonylated brain proteins in mild cognitive impairment and early Alzheimer's disease
    • 1:CAS:528:DC%2BC3cXitVahsLo%3D 19686046
    • R Sultana M Perluigi SF Newman WM Pierce C Cini R Coccia DA Butterfield 2010 Redox proteomic analysis of carbonylated brain proteins in mild cognitive impairment and early Alzheimer's disease Antioxid Redox Signal 12 327 336 1:CAS:528:DC%2BC3cXitVahsLo%3D 19686046
    • (2010) Antioxid Redox Signal , vol.12 , pp. 327-336
    • Sultana, R.1    Perluigi, M.2    Newman, S.F.3    Pierce, W.M.4    Cini, C.5    Coccia, R.6    Butterfield, D.A.7
  • 39
    • 34247326430 scopus 로고    scopus 로고
    • In vivo induction of heat shock proteins in the substantia nigra following l-DOPA administration is associated with increased activity of mitochondrial complex i and nitrosative stress in rats: Regulation by glutathione redox state
    • 1:CAS:528:DC%2BD2sXlsV2ksLw%3D 17241115
    • V Calabrese C Mancuso A Ravagna M Perluigi C Cini C De Marco DA Butterfield AM Giuffrida Stella 2007 In vivo induction of heat shock proteins in the substantia nigra following l-DOPA administration is associated with increased activity of mitochondrial complex I and nitrosative stress in rats: regulation by glutathione redox state J Neurochem 101 709 717 1:CAS:528:DC%2BD2sXlsV2ksLw%3D 17241115
    • (2007) J Neurochem , vol.101 , pp. 709-717
    • Calabrese, V.1    Mancuso, C.2    Ravagna, A.3    Perluigi, M.4    Cini, C.5    De Marco, C.6    Butterfield, D.A.7    Giuffrida Stella, A.M.8
  • 42
    • 52249099052 scopus 로고    scopus 로고
    • Practical approaches to investigate redox regulation of heat shock protein expression and intracellular glutathione redox state
    • 1:CAS:528:DC%2BD1cXhtFamsL7F 18554531
    • V Calabrese A Signorile C Cornelius C Mancuso G Scapagnini B Ventimiglia N Ragusa A Dinkova-Kostova 2008 Practical approaches to investigate redox regulation of heat shock protein expression and intracellular glutathione redox state Methods Enzymol 441 83 110 1:CAS:528:DC%2BD1cXhtFamsL7F 18554531
    • (2008) Methods Enzymol , vol.441 , pp. 83-110
    • Calabrese, V.1    Signorile, A.2    Cornelius, C.3    Mancuso, C.4    Scapagnini, G.5    Ventimiglia, B.6    Ragusa, N.7    Dinkova-Kostova, A.8
  • 43
    • 33646675336 scopus 로고    scopus 로고
    • Redox modulation of heat shock protein expression by acetylcarnitine in aging brain: Relationship to antioxidant status and mitochondrial function
    • 1:CAS:528:DC%2BD28Xkt12rurs%3D 16677087
    • V Calabrese C Colombrita R Sultana G Scapagnini M Calvani DA Butterfield AM Stella 2006 Redox modulation of heat shock protein expression by acetylcarnitine in aging brain: relationship to antioxidant status and mitochondrial function Antioxid Redox Signal 8 404 416 1:CAS:528: DC%2BD28Xkt12rurs%3D 16677087
    • (2006) Antioxid Redox Signal , vol.8 , pp. 404-416
    • Calabrese, V.1    Colombrita, C.2    Sultana, R.3    Scapagnini, G.4    Calvani, M.5    Butterfield, D.A.6    Stella, A.M.7
  • 44
    • 78049423686 scopus 로고    scopus 로고
    • Redox proteomics in aging rat brain: Involvement of mitochondrial GSH status and mitochondrial protein oxidation in the aging process
    • in press
    • Perluigi M, Di Domenico F, Butterfield DA, Giorgi A, Schininà ME, Coccia R, Cini C, Bellia F, Cambria MT, Cormelius C, Calabrese V (2010) Redox proteomics in aging rat brain: involvement of mitochondrial GSH status and mitochondrial protein oxidation in the aging process. J Neurosci Res (in press)
    • (2010) J Neurosci Res
    • Perluigi M, D.1
  • 45
    • 77952672909 scopus 로고    scopus 로고
    • Increased levels of 4-hydroxynonenal and acrolein in the brain in preclinical Alzheimer disease
    • 1:CAS:528:DC%2BC3cXlvVeitrg%3D 20171275
    • MA Bradley WR Markesbery MA Lovell 2010 Increased levels of 4-hydroxynonenal and acrolein in the brain in preclinical Alzheimer disease Free Radic Biol Med 48 1570 1576 1:CAS:528:DC%2BC3cXlvVeitrg%3D 20171275
    • (2010) Free Radic Biol Med , vol.48 , pp. 1570-1576
    • Bradley, M.A.1    Markesbery, W.R.2    Lovell, M.A.3
  • 46
    • 77449110410 scopus 로고    scopus 로고
    • Proteomics identification of carbonylated and HNE-bound brain proteins in Alzheimer's disease
    • R Sultana DA Butterfield 2010 Proteomics identification of carbonylated and HNE-bound brain proteins in Alzheimer's disease Methods Mol Biol 566 123 135
    • (2010) Methods Mol Biol , vol.566 , pp. 123-135
    • Sultana, R.1    Butterfield, D.A.2
  • 47
    • 0031678044 scopus 로고    scopus 로고
    • Decreased glutathione transferase activity in brain and ventricular fluid in Alzheimer's disease
    • 1:CAS:528:DyaK1MXhsVOntA%3D%3D 9855502
    • MA Lovell C Xie WR Markesbery 1998 Decreased glutathione transferase activity in brain and ventricular fluid in Alzheimer's disease Neurology 51 1562 1566 1:CAS:528:DyaK1MXhsVOntA%3D%3D 9855502
    • (1998) Neurology , vol.51 , pp. 1562-1566
    • Lovell, M.A.1    Xie, C.2    Markesbery, W.R.3
  • 48
    • 77955503270 scopus 로고    scopus 로고
    • Decreased energy metabolism extends life span in Caenorhabditis elegans without reducing oxidative damage
    • 20382831
    • JM Van Raamsdonk Y Meng D Camp W Yang X Jia C Bénard S Hekimi 2010 Decreased energy metabolism extends life span in Caenorhabditis elegans without reducing oxidative damage Genetics 185 559 571 20382831
    • (2010) Genetics , vol.185 , pp. 559-571
    • Van Raamsdonk, J.M.1    Meng, Y.2    Camp, D.3    Yang, W.4    Jia, X.5    Bénard, C.6    Hekimi, S.7
  • 49
    • 78149343508 scopus 로고    scopus 로고
    • Reactive oxygen species and aging in caenorhabditis elegans: Causal or casual relationship?
    • Van Raamsdonk JM, Hekimi S (2010) Reactive oxygen species and aging in caenorhabditis elegans: causal or casual relationship? Antioxid Redox Signal
    • (2010) Antioxid Redox Signal
    • Van Raamsdonk, J.M.1    Hekimi, S.2
  • 50
    • 0034864018 scopus 로고    scopus 로고
    • Mitocondrial involvement in brain function and dysfunction: Relevance to aging, neurodegenerative disordes and longevity
    • 1:CAS:528:DC%2BD3MXmtFKrtLY%3D 11519733
    • V Calabrese G Scapagnini AM Giuffrida Stella TE Bates JB Clark 2001 Mitocondrial involvement in brain function and dysfunction: relevance to aging, neurodegenerative disordes and longevity Neurochem Res 26 739 764 1:CAS:528:DC%2BD3MXmtFKrtLY%3D 11519733
    • (2001) Neurochem Res , vol.26 , pp. 739-764
    • Calabrese, V.1    Scapagnini, G.2    Giuffrida Stella, A.M.3    Bates, T.E.4    Clark, J.B.5
  • 51
    • 45449088101 scopus 로고    scopus 로고
    • Mitochondrial DNA repair in aging and disease
    • 1:CAS:528:DC%2BD1cXns1Shtbc%3D
    • NM Druzhyna GL Wilson SP LeDoux 2008 Mitochondrial DNA repair in aging and disease Mech Age Dev 129 383 390 1:CAS:528:DC%2BD1cXns1Shtbc%3D
    • (2008) Mech Age Dev , vol.129 , pp. 383-390
    • Druzhyna, N.M.1    Wilson, G.L.2    Ledoux, S.P.3
  • 52
    • 51249111704 scopus 로고    scopus 로고
    • Mitochondrial medicine and mitochondrion-based therapeutics
    • S Hamm-Alvarez E Cadenas 2009 Mitochondrial medicine and mitochondrion-based therapeutics Adv Drug Deliv Rev 60 1437 1438
    • (2009) Adv Drug Deliv Rev , vol.60 , pp. 1437-1438
    • Hamm-Alvarez, S.1    Cadenas, E.2
  • 53
    • 71549124934 scopus 로고    scopus 로고
    • Mitochondrial medicine and therapeutics, Part II
    • 1:CAS:528:DC%2BD1MXhsVWmu7nO 19835920
    • S Hamm-Alvarez E Cadenas 2009 Mitochondrial medicine and therapeutics, Part II Adv Drug Deliv Rev 61 1233 1:CAS:528:DC%2BD1MXhsVWmu7nO 19835920
    • (2009) Adv Drug Deliv Rev , vol.61 , pp. 1233
    • Hamm-Alvarez, S.1    Cadenas, E.2
  • 54
    • 71549131281 scopus 로고    scopus 로고
    • The energy-redox axis in aging and age-related neurodegeneration
    • 1:CAS:528:DC%2BD1MXhsVWmu7nK 19716388
    • LP Yap JV Garcia D Han E Cadenas 2009 The energy-redox axis in aging and age-related neurodegeneration Adv Drug Deliv Rev 61 1283 1298 1:CAS:528:DC%2BD1MXhsVWmu7nK 19716388
    • (2009) Adv Drug Deliv Rev , vol.61 , pp. 1283-1298
    • Yap, L.P.1    Garcia, J.V.2    Han, D.3    Cadenas, E.4
  • 55
    • 0035990290 scopus 로고    scopus 로고
    • Primary and secondary defects of the mitochondrial respiratory chain
    • 1:CAS:528:DC%2BD38XmtFShs7k%3D 12137229
    • AH Schapira 2002 Primary and secondary defects of the mitochondrial respiratory chain J Inherit Metab Dis 25 207 214 1:CAS:528:DC%2BD38XmtFShs7k%3D 12137229
    • (2002) J Inherit Metab Dis , vol.25 , pp. 207-214
    • Schapira, A.H.1
  • 56
    • 52249097807 scopus 로고    scopus 로고
    • Idebenone in Friedreich's ataxia
    • 1:CAS:528:DC%2BD1cXpvFygu7s%3D 18710357
    • C Tonon R Lodi 2008 Idebenone in Friedreich's ataxia Expert Opin Pharmacother 9 2327 2337 1:CAS:528:DC%2BD1cXpvFygu7s%3D 18710357
    • (2008) Expert Opin Pharmacother , vol.9 , pp. 2327-2337
    • Tonon, C.1    Lodi, R.2
  • 57
    • 0347991813 scopus 로고    scopus 로고
    • Redox regulation of heat shock protein expression in aging and neurodegenerative disorders associated with oxidative stress: A nutritional approach
    • 1:CAS:528:DC%2BD3sXpsFOntb8%3D 14661103
    • V Calabrese G Scapagnini C Colombrita A Ravagna G Pennisi AM Giuffrida Stella F Galli DA Butterfield 2003 Redox regulation of heat shock protein expression in aging and neurodegenerative disorders associated with oxidative stress: a nutritional approach Amino Acids 25 437 444 1:CAS:528: DC%2BD3sXpsFOntb8%3D 14661103
    • (2003) Amino Acids , vol.25 , pp. 437-444
    • Calabrese, V.1    Scapagnini, G.2    Colombrita, C.3    Ravagna, A.4    Pennisi, G.5    Giuffrida Stella, A.M.6    Galli, F.7    Butterfield, D.A.8
  • 58
    • 52049089147 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in rat brain with aging Involvement of complex I, reactive oxygen species and cardiolipin
    • 1:CAS:528:DC%2BD1cXhtFOltbvF 18657582
    • G Petrosillo M Matera G Casanova FM Ruggiero G Paradies 2008 Mitochondrial dysfunction in rat brain with aging Involvement of complex I, reactive oxygen species and cardiolipin Neurochem Int 53 126 131 1:CAS:528:DC%2BD1cXhtFOltbvF 18657582
    • (2008) Neurochem Int , vol.53 , pp. 126-131
    • Petrosillo, G.1    Matera, M.2    Casanova, G.3    Ruggiero, F.M.4    Paradies, G.5
  • 59
    • 10644232862 scopus 로고    scopus 로고
    • Delaying the mitochondrial decay of aging with acetylcarnitine
    • 1:CAS:528:DC%2BD2MXjvFOgtw%3D%3D 15591008
    • BN Ames J Liu 2004 Delaying the mitochondrial decay of aging with acetylcarnitine Ann N Y Acad Sci 1033 108 116 1:CAS:528:DC%2BD2MXjvFOgtw%3D%3D 15591008
    • (2004) Ann N y Acad Sci , vol.1033 , pp. 108-116
    • Ames, B.N.1    Liu, J.2
  • 60
    • 77249139160 scopus 로고    scopus 로고
    • The impact of acute caloric restriction on the metabolic phenotype in male C57BL/6 and DBA/2 mice
    • 1:CAS:528:DC%2BC3cXitVKjtrs%3D 20064544
    • S Hempenstall L Picchio SE Mitchell JR Speakman C Selman 2010 The impact of acute caloric restriction on the metabolic phenotype in male C57BL/6 and DBA/2 mice Mech Ageing Dev 131 111 118 1:CAS:528:DC%2BC3cXitVKjtrs%3D 20064544
    • (2010) Mech Ageing Dev , vol.131 , pp. 111-118
    • Hempenstall, S.1    Picchio, L.2    Mitchell, S.E.3    Speakman, J.R.4    Selman, C.5
  • 61
    • 37749037128 scopus 로고    scopus 로고
    • Dietary factors, hormesis and health
    • 17913594
    • MP Mattson 2008 Dietary factors, hormesis and health Ageing Res Rev 7 43 48 17913594
    • (2008) Ageing Res Rev , vol.7 , pp. 43-48
    • Mattson, M.P.1
  • 62
    • 77952548782 scopus 로고    scopus 로고
    • How increased oxidative stress promotes longevity and metabolic health: The concept of mitochondrial hormesis (mitohormesis)
    • 1:CAS:528:DC%2BC3cXlsV2kurc%3D 20350594
    • M Ristow K Zarse 2010 How increased oxidative stress promotes longevity and metabolic health: the concept of mitochondrial hormesis (mitohormesis) Exp Gerontol 45 410 418 1:CAS:528:DC%2BC3cXlsV2kurc%3D 20350594
    • (2010) Exp Gerontol , vol.45 , pp. 410-418
    • Ristow, M.1    Zarse, K.2
  • 64
    • 78651126508 scopus 로고
    • A case of severe hypermetabolism of nonthyroid origin with a defect in the maintenance of mitochondrial respiratory control: A correlated clinical, biochemical and morphological study
    • 1:CAS:528:DyaF38XkvVKgur8%3D 14467237
    • R Luft D Ikkos G Palmieri L Ernster A Afzelius 1962 A case of severe hypermetabolism of nonthyroid origin with a defect in the maintenance of mitochondrial respiratory control: a correlated clinical, biochemical and morphological study J Clin Invest 41 1776 1804 1:CAS:528:DyaF38XkvVKgur8%3D 14467237
    • (1962) J Clin Invest , vol.41 , pp. 1776-1804
    • Luft, R.1    Ikkos, D.2    Palmieri, G.3    Ernster, L.4    Afzelius, A.5
  • 65
    • 60549083568 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in neurodegenerative diseases
    • 1:CAS:528:DC%2BD1cXhtlCku77J 18998208
    • AH Schapira 2008 Mitochondrial dysfunction in neurodegenerative diseases Neurochem Res 33 2502 2509 1:CAS:528:DC%2BD1cXhtlCku77J 18998208
    • (2008) Neurochem Res , vol.33 , pp. 2502-2509
    • Schapira, A.H.1
  • 66
    • 0033525773 scopus 로고    scopus 로고
    • Mitochondrial diseases in man and mouse
    • 1:CAS:528:DyaK1MXhs1ygurk%3D 10066162
    • DC Wallace 1999 Mitochondrial diseases in man and mouse Science 283 1482 1488 1:CAS:528:DyaK1MXhs1ygurk%3D 10066162
    • (1999) Science , vol.283 , pp. 1482-1488
    • Wallace, D.C.1
  • 67
    • 49849088591 scopus 로고    scopus 로고
    • Mitochondria as Chi
    • 1:CAS:528:DC%2BD1cXos1arsbc%3D 18558648
    • DC Wallace 2008 Mitochondria as Chi Genetics 179 727 735 1:CAS:528:DC%2BD1cXos1arsbc%3D 18558648
    • (2008) Genetics , vol.179 , pp. 727-735
    • Wallace, D.C.1
  • 69
    • 0035282929 scopus 로고    scopus 로고
    • What do mitochondrial diseases teach us about normal mitochondrial functions that we already knew: Threshold expression of mitochondrial defects
    • 1:CAS:528:DC%2BD3MXhsFSit70%3D 11239482
    • J Mazat R Rossignol M Malgat C Rocher B Faustin T Letellier 2001 What do mitochondrial diseases teach us about normal mitochondrial functions that we already knew: threshold expression of mitochondrial defects Biochim Biophys Acta 1504 20 30 1:CAS:528:DC%2BD3MXhsFSit70%3D 11239482
    • (2001) Biochim Biophys Acta , vol.1504 , pp. 20-30
    • Mazat, J.1    Rossignol, R.2    Malgat, M.3    Rocher, C.4    Faustin, B.5    Letellier, T.6
  • 71
    • 0032557511 scopus 로고    scopus 로고
    • Energy thresholds in brain mitochondria
    • 1:CAS:528:DyaK1cXjsVertb4%3D 9582300
    • GP Davey S Peuchen JB Clark 1998 Energy thresholds in brain mitochondria J Biol Chem 273 12753 12757 1:CAS:528:DyaK1cXjsVertb4%3D 9582300
    • (1998) J Biol Chem , vol.273 , pp. 12753-12757
    • Davey, G.P.1    Peuchen, S.2    Clark, J.B.3
  • 72
    • 50949104833 scopus 로고    scopus 로고
    • Complex i and energy thresholds in the brain
    • 1:CAS:528:DC%2BD1cXnsFCmt74%3D 18519025
    • RU Pathak GP Davey 2008 Complex I and energy thresholds in the brain Biochim Biophys Acta 1777 777 782 1:CAS:528:DC%2BD1cXnsFCmt74%3D 18519025
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 777-782
    • Pathak, R.U.1    Davey, G.P.2
  • 75
    • 43049094751 scopus 로고    scopus 로고
    • Functional dynamic compartmentalization of respiratory chain intermediate substrates: Implications for the control of energy production and mitochondrial diseases
    • 1:CAS:528:DC%2BD1cXlslGqu70%3D 18207445
    • G Benard B Faustin A Galinier C Rocher N Bellance K Smolkova L Casteilla R Rossignol T Letellier 2008 Functional dynamic compartmentalization of respiratory chain intermediate substrates: implications for the control of energy production and mitochondrial diseases Int J Biochem Cell Biol 40 1543 1554 1:CAS:528:DC%2BD1cXlslGqu70%3D 18207445
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 1543-1554
    • Benard, G.1    Faustin, B.2    Galinier, A.3    Rocher, C.4    Bellance, N.5    Smolkova, K.6    Casteilla, L.7    Rossignol, R.8    Letellier, T.9
  • 76
    • 43249114934 scopus 로고    scopus 로고
    • Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease
    • 1:CAS:528:DC%2BD1cXlsFCmsrg%3D 18391962
    • JH Kordower Y Chu RA Hauser TB Freeman CW Olanow 2008 Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease Nat Med 14 504 506 1:CAS:528:DC%2BD1cXlsFCmsrg%3D 18391962
    • (2008) Nat Med , vol.14 , pp. 504-506
    • Kordower, J.H.1    Chu, Y.2    Hauser, R.A.3    Freeman, T.B.4    Olanow, C.W.5
  • 77
    • 46349098565 scopus 로고    scopus 로고
    • Partial inhibition of complex i activity increases Ca(2+)-independent glutamate release rates from depolarized synaptosomes
    • 1:CAS:528:DC%2BD1cXovFWgtbc%3D 18445136
    • SM Kilbride JE Telford KF Tipton GP Davey 2008 Partial inhibition of complex I activity increases Ca(2+)-independent glutamate release rates from depolarized synaptosomes J Neurochem 106 826 834 1:CAS:528:DC%2BD1cXovFWgtbc%3D 18445136
    • (2008) J Neurochem , vol.106 , pp. 826-834
    • Kilbride, S.M.1    Telford, J.E.2    Tipton, K.F.3    Davey, G.P.4
  • 78
    • 46349097650 scopus 로고    scopus 로고
    • 2 production and bioenergetics in rat brain synaptosomes
    • 1:CAS:528:DC%2BD1cXnsFCmt7w%3D 18515065
    • 2 production and bioenergetics in rat brain synaptosomes Biochim Biophys Acta 1777 783 788 1:CAS:528:DC%2BD1cXnsFCmt7w%3D 18515065
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 783-788
    • Kilbride, S.M.1    Telford, J.E.2    Davey, G.P.3
  • 79
    • 33646948530 scopus 로고    scopus 로고
    • Parkinson's disease brain mitochondrial complex i has oxidatively damaged subunits and is functionally impaired and misassembled
    • 1:CAS:528:DC%2BD28Xlt1Cisrk%3D 16687518
    • PM Keeney J Xie RA Capaldi JP Bennett Jr. 2006 Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled J Neurosci 26 5256 5264 1:CAS:528:DC%2BD28Xlt1Cisrk%3D 16687518
    • (2006) J Neurosci , vol.26 , pp. 5256-5264
    • Keeney, P.M.1    Xie, J.2    Capaldi, R.A.3    Bennett Jr., J.P.4
  • 80
    • 34848911639 scopus 로고    scopus 로고
    • Human mitochondrial complex i assembly: A dynamic and versatile process
    • 1:CAS:528:DC%2BD2sXhtFCjurbF 17854760
    • RO Vogel JA Smeitink LG Nijtmans 2007 Human mitochondrial complex I assembly: a dynamic and versatile process Biochim Biophys Acta 1767 1215 1227 1:CAS:528:DC%2BD2sXhtFCjurbF 17854760
    • (2007) Biochim Biophys Acta , vol.1767 , pp. 1215-1227
    • Vogel, R.O.1    Smeitink, J.A.2    Nijtmans, L.G.3
  • 82
    • 77953743759 scopus 로고    scopus 로고
    • Structure and function of mitochondrial supercomplexes
    • 1:CAS:528:DC%2BC3cXnvV2qs7s%3D 20036212
    • NV Dudkina R Kouřil K Peters HP Braun EJ Boekema 2010 Structure and function of mitochondrial supercomplexes Biochim Biophys Acta 1797 664 670 1:CAS:528:DC%2BC3cXnvV2qs7s%3D 20036212
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 664-670
    • Dudkina, N.V.1    Kouřil, R.2    Peters, K.3    Braun, H.P.4    Boekema, E.J.5
  • 83
    • 67349200007 scopus 로고    scopus 로고
    • Supramolecular organization of ATP synthase and respiratory chain in mitochondrial membranes
    • 1:CAS:528:DC%2BD1MXntVSitro%3D 19168025
    • I Wittig H Schägger 2009 Supramolecular organization of ATP synthase and respiratory chain in mitochondrial membranes Biochim Biophys Acta 1787 672 680 1:CAS:528:DC%2BD1MXntVSitro%3D 19168025
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 672-680
    • Wittig, I.1    Schägger, H.2
  • 84
    • 33845997803 scopus 로고    scopus 로고
    • Similar transition states mediate the Q-cycle and superoxide production by the cytochrome bc1 complex
    • 1:CAS:528:DC%2BD28Xht12msr%2FM 17008316
    • I Forquer R Covian MK Bowman BL Trumpower DM Kramer 2006 Similar transition states mediate the Q-cycle and superoxide production by the cytochrome bc1 complex J Biol Chem 281 38459 38465 1:CAS:528: DC%2BD28Xht12msr%2FM 17008316
    • (2006) J Biol Chem , vol.281 , pp. 38459-38465
    • Forquer, I.1    Covian, R.2    Bowman, M.K.3    Trumpower, B.L.4    Kramer, D.M.5
  • 85
    • 39849088049 scopus 로고    scopus 로고
    • Heme oxygenase and carbon monoxide initiate homeostatic signaling
    • 1:CAS:528:DC%2BD1cXitlGntbg%3D 18034222
    • M Bilban A Haschemi B Wegiel BY Chin O Wagner LE Otterbein 2008 Heme oxygenase and carbon monoxide initiate homeostatic signaling J Mol Med 86 267 279 1:CAS:528:DC%2BD1cXitlGntbg%3D 18034222
    • (2008) J Mol Med , vol.86 , pp. 267-279
    • Bilban, M.1    Haschemi, A.2    Wegiel, B.3    Chin, B.Y.4    Wagner, O.5    Otterbein, L.E.6
  • 88
    • 0036122601 scopus 로고    scopus 로고
    • Superoxide dismutase in aging and disease: An overview
    • 1:CAS:528:DC%2BD38XjsFajur0%3D 11912924
    • JM McCord 2002 Superoxide dismutase in aging and disease: an overview Methods Enzymol 349 331 341 1:CAS:528:DC%2BD38XjsFajur0%3D 11912924
    • (2002) Methods Enzymol , vol.349 , pp. 331-341
    • McCord, J.M.1
  • 89
    • 77957358299 scopus 로고    scopus 로고
    • Mitochondrial dynamics in cell death and neurodegeneration
    • 2010 Jun 25. [Epub ahead of print]
    • Cho DH, Nakamura T, Lipton SA (2010) Mitochondrial dynamics in cell death and neurodegeneration. Cell Mol Life Sci. 2010 Jun 25. [Epub ahead of print]
    • (2010) Cell Mol Life Sci
    • Cho, D.H.1    Nakamura, T.2    Lipton, S.A.3
  • 90
    • 77955432558 scopus 로고    scopus 로고
    • S-Nitrosylation of Drp1 links excessive mitochondrial fission to neuronal injury in neurodegeneration
    • 1:CAS:528:DC%2BC3cXpvFOnu7s%3D 20447471
    • T Nakamura P Cieplak DH Cho A Godzik SA Lipton 2010 S-Nitrosylation of Drp1 links excessive mitochondrial fission to neuronal injury in neurodegeneration Mitochondrion 10 573 578 1:CAS:528:DC%2BC3cXpvFOnu7s%3D 20447471
    • (2010) Mitochondrion , vol.10 , pp. 573-578
    • Nakamura, T.1    Cieplak, P.2    Cho, D.H.3    Godzik, A.4    Lipton, S.A.5
  • 91
    • 77955085868 scopus 로고    scopus 로고
    • Redox reactions induced by nitrosative stress mediate protein misfolding and mitochondrial dysfunction in neurodegenerative diseases
    • 1:CAS:528:DC%2BC3cXmsFSqsbo%3D 20333559
    • Z Gu T Nakamura SA Lipton 2010 Redox reactions induced by nitrosative stress mediate protein misfolding and mitochondrial dysfunction in neurodegenerative diseases Mol Neurobiol 41 55 72 1:CAS:528:DC%2BC3cXmsFSqsbo%3D 20333559
    • (2010) Mol Neurobiol , vol.41 , pp. 55-72
    • Gu, Z.1    Nakamura, T.2    Lipton, S.A.3
  • 92
    • 78649983205 scopus 로고    scopus 로고
    • Redox regulation of mitochondrial fission, protein misfolding, synaptic damage, and neuronal cell death: Potential implications for Alzheimer's and Parkinson's diseases
    • Epub ahead of print
    • Nakamura T, Lipton SA (2010) Redox regulation of mitochondrial fission, protein misfolding, synaptic damage, and neuronal cell death: potential implications for Alzheimer's and Parkinson's diseases. Apoptosis [Epub ahead of print]
    • (2010) Apoptosis
    • Nakamura, T.1    Lipton, S.A.2
  • 93
    • 78650017514 scopus 로고    scopus 로고
    • Mitochondrial dynamics, cell death and the pathogenesis of Parkinson's disease
    • Epub ahead of print
    • Büeler H (2010) Mitochondrial dynamics, cell death and the pathogenesis of Parkinson's disease. Apoptosis [Epub ahead of print]
    • (2010) Apoptosis
    • Büeler, H.1
  • 94
    • 45749117188 scopus 로고    scopus 로고
    • Mitochondrial fragmentation in neurodegeneration
    • 1:CAS:528:DC%2BD1cXnsFChu7c%3D 18568013
    • AB Knott G Perkins R Schwarzenbacher E Bossy-Wetzel 2008 Mitochondrial fragmentation in neurodegeneration Nat Rev Neurosci 9 505 518 1:CAS:528:DC%2BD1cXnsFChu7c%3D 18568013
    • (2008) Nat Rev Neurosci , vol.9 , pp. 505-518
    • Knott, A.B.1    Perkins, G.2    Schwarzenbacher, R.3    Bossy-Wetzel, E.4
  • 95
    • 77749326636 scopus 로고    scopus 로고
    • Mitochondrial dynamics in Alzheimer's disease: Opportunities for future treatment strategies
    • 1:CAS:528:DC%2BC3cXls1SksLs%3D 20210366
    • DJ Bonda X Wang G Perry MA Smith X Zhu 2010 Mitochondrial dynamics in Alzheimer's disease: opportunities for future treatment strategies Drugs Aging 27 181 192 1:CAS:528:DC%2BC3cXls1SksLs%3D 20210366
    • (2010) Drugs Aging , vol.27 , pp. 181-192
    • Bonda, D.J.1    Wang, X.2    Perry, G.3    Smith, M.A.4    Zhu, X.5
  • 96
    • 77955861146 scopus 로고    scopus 로고
    • Autophagy in health and disease. 5. Mitophagy as a way of life
    • 1:CAS:528:DC%2BC3cXhtVOht7jK 20357180
    • RA Gottlieb RS Carreira 2010 Autophagy in health and disease. 5. Mitophagy as a way of life Am J Physiol Cell Physiol 299 C203 210 1:CAS:528:DC%2BC3cXhtVOht7jK 20357180
    • (2010) Am J Physiol Cell Physiol , vol.299 , pp. 203-210
    • Gottlieb, R.A.1    Carreira, R.S.2
  • 97
    • 71549116704 scopus 로고    scopus 로고
    • Mitochondria in the elderly: Is acetylcarnitine a rejuvenator?
    • 1:CAS:528:DC%2BD1MXhsVWmu7bM 19720100
    • MG Rosca H Lemieux CL Hoppel 2009 Mitochondria in the elderly: is acetylcarnitine a rejuvenator? Adv Drug Deliv Rev 61 1332 1342 1:CAS:528:DC%2BD1MXhsVWmu7bM 19720100
    • (2009) Adv Drug Deliv Rev , vol.61 , pp. 1332-1342
    • Rosca, M.G.1    Lemieux, H.2    Hoppel, C.L.3
  • 98
    • 48549090696 scopus 로고    scopus 로고
    • Carbon monoxide, reactive oxygen signaling, and oxidative stress
    • 1:CAS:528:DC%2BD1cXpslWkur4%3D 18549826
    • CA Piantadosi 2008 Carbon monoxide, reactive oxygen signaling, and oxidative stress Free Radic Biol Med 45 562 569 1:CAS:528:DC%2BD1cXpslWkur4%3D 18549826
    • (2008) Free Radic Biol Med , vol.45 , pp. 562-569
    • Piantadosi, C.A.1
  • 99
    • 58149328569 scopus 로고    scopus 로고
    • Heme oxygenase-1 regulates cardiac mitochondrial biogenesis via Nrf2-mediated transcriptional control of nuclear respiratory factor-1
    • 1:CAS:528:DC%2BD1cXhtlKrt7fK 18845810
    • CA Piantadosi MS Carraway A Babiker HB Suliman 2008 Heme oxygenase-1 regulates cardiac mitochondrial biogenesis via Nrf2-mediated transcriptional control of nuclear respiratory factor-1 Circ Res 103 1232 1240 1:CAS:528:DC%2BD1cXhtlKrt7fK 18845810
    • (2008) Circ Res , vol.103 , pp. 1232-1240
    • Piantadosi, C.A.1    Carraway, M.S.2    Babiker, A.3    Suliman, H.B.4
  • 101
    • 0032994225 scopus 로고    scopus 로고
    • Evidence that hormesis represents an "overcompensation" response to a disruption in homeostasis
    • EJ Calabrese 1999 Evidence that hormesis represents an "overcompensation" response to a disruption in homeostasis Ecotoxicol Environ Safety 42 135 137
    • (1999) Ecotoxicol Environ Safety , vol.42 , pp. 135-137
    • Calabrese, E.J.1
  • 102
    • 36849079233 scopus 로고    scopus 로고
    • Low doses of radiation reduce risk in vivo
    • 1:CAS:528:DC%2BD2sXmsVOqu78%3D
    • REJ Mitchel 2007 Low doses of radiation reduce risk in vivo Dose Response 5 1 10 1:CAS:528:DC%2BD2sXmsVOqu78%3D
    • (2007) Dose Response , vol.5 , pp. 1-10
    • Mitchel, R.E.J.1
  • 103
    • 0343974179 scopus 로고
    • Induction of the carcinogenic action produced by a weakly carcinogenic hydrocarbon on a highly active carcinogenic hydrocarbon
    • 1:CAS:528:DyaH2MXitl2ktg%3D%3D
    • A Lacassagne NP Buu-Hoi G Rudali 1945 Induction of the carcinogenic action produced by a weakly carcinogenic hydrocarbon on a highly active carcinogenic hydrocarbon Br J Exp Pathol 26 5 12 1:CAS:528:DyaH2MXitl2ktg%3D%3D
    • (1945) Br J Exp Pathol , vol.26 , pp. 5-12
    • Lacassagne, A.1    Buu-Hoi, N.P.2    Rudali, G.3
  • 104
    • 33750618049 scopus 로고    scopus 로고
    • The pKZ1 recombination mutation assay: A sensitive assay for low dose studies
    • 1:CAS:528:DC%2BD2sXivVOgsr4%3D 18648582
    • PJ Sykes AA Morley AM Hooker 2006 The pKZ1 recombination mutation assay: a sensitive assay for low dose studies Dose Response 4 91 105 1:CAS:528:DC%2BD2sXivVOgsr4%3D 18648582
    • (2006) Dose Response , vol.4 , pp. 91-105
    • Sykes, P.J.1    Morley, A.A.2    Hooker, A.M.3
  • 105
    • 42149142784 scopus 로고    scopus 로고
    • The adaptive response and protection against heritable mutations and fetal malformation
    • 1:CAS:528:DC%2BD2sXivVOhu7w%3D 18648586
    • DR Boreham J-A Dolling C Somers J Quinn REJ Mitchel 2006 The adaptive response and protection against heritable mutations and fetal malformation Dose Response 4 317 326 1:CAS:528:DC%2BD2sXivVOhu7w%3D 18648586
    • (2006) Dose Response , vol.4 , pp. 317-326
    • Boreham, D.R.1    Dolling, J.-A.2    Somers, C.3    Quinn, J.4    Mitchel, R.E.J.5
  • 106
    • 33646062845 scopus 로고    scopus 로고
    • Radiation-induced bystander effects and the DNA paradigm: An "out of field" perspective
    • 1:CAS:528:DC%2BD28XjvVGls7Y%3D 16414088
    • C Mothersill CB Seymour 2006 Radiation-induced bystander effects and the DNA paradigm: an "out of field" perspective Mutat Res 597 5 10 1:CAS:528:DC%2BD28XjvVGls7Y%3D 16414088
    • (2006) Mutat Res , vol.597 , pp. 5-10
    • Mothersill, C.1    Seymour, C.B.2
  • 107
    • 41849123382 scopus 로고    scopus 로고
    • Enhancement of bio-protective functions by low dose/dose-rate radiation
    • 1:CAS:528:DC%2BD2sXivVOhu70%3D 18648588
    • K Sakai T Nomura Y Ina 2006 Enhancement of bio-protective functions by low dose/dose-rate radiation Dose Response 4 327 332 1:CAS:528: DC%2BD2sXivVOhu70%3D 18648588
    • (2006) Dose Response , vol.4 , pp. 327-332
    • Sakai, K.1    Nomura, T.2    Ina, Y.3
  • 108
    • 58149253547 scopus 로고    scopus 로고
    • Sparsely ionizing diagnostic and natural background radiations are likely preventing cancer and other genomic-instability-associated diseases
    • 18648608
    • BR Scott J DiPalma 2006 Sparsely ionizing diagnostic and natural background radiations are likely preventing cancer and other genomic-instability-associated diseases Dose Response 5 230 255 18648608
    • (2006) Dose Response , vol.5 , pp. 230-255
    • Scott, B.R.1    Dipalma, J.2
  • 109
    • 36849018353 scopus 로고    scopus 로고
    • Suppression of neoplastic transformation in vitro by low doses of low LET radiation
    • 1:CAS:528:DC%2BD2sXivVOhu74%3D 18648592
    • JL Redpath 2006 Suppression of neoplastic transformation in vitro by low doses of low LET radiation Dose Response 4 302 308 1:CAS:528: DC%2BD2sXivVOhu74%3D 18648592
    • (2006) Dose Response , vol.4 , pp. 302-308
    • Redpath, J.L.1
  • 110
    • 0033657377 scopus 로고    scopus 로고
    • Chemical hormesis: Its historical foundations as a biological hypothesis
    • 1:STN:280:DC%2BD3c3htFartQ%3D%3D 10745292
    • EJ Calabrese LA Baldwin 2000 Chemical hormesis: Its historical foundations as a biological hypothesis Hum Exp Toxicol 19 2 31 1:STN:280:DC%2BD3c3htFartQ%3D%3D 10745292
    • (2000) Hum Exp Toxicol , vol.19 , pp. 2-31
    • Calabrese, E.J.1    Baldwin, L.A.2
  • 111
    • 0033643737 scopus 로고    scopus 로고
    • The marginalization of hormesis
    • 1:STN:280:DC%2BD3c3htFarug%3D%3D 10745293
    • EJ Calabrese LA Baldwin 2000 The marginalization of hormesis Hum Exp Toxicol 19 32 40 1:STN:280:DC%2BD3c3htFarug%3D%3D 10745293
    • (2000) Hum Exp Toxicol , vol.19 , pp. 32-40
    • Calabrese, E.J.1    Baldwin, L.A.2
  • 112
    • 0034076363 scopus 로고    scopus 로고
    • Radiation hormesis: Its historical foundations as a biological hypothesis
    • 1:STN:280:DC%2BD3c3htFaruw%3D%3D 10745294
    • EJ Calabrese LA Baldwin 2000 Radiation hormesis: its historical foundations as a biological hypothesis Hum Exp Toxicol 19 41 75 1:STN:280:DC%2BD3c3htFaruw%3D%3D 10745294
    • (2000) Hum Exp Toxicol , vol.19 , pp. 41-75
    • Calabrese, E.J.1    Baldwin, L.A.2
  • 113
    • 0034076364 scopus 로고    scopus 로고
    • Radiation hormesis: The demise of a legitimate hypothesis
    • 1:STN:280:DC%2BD3c3htFaqsg%3D%3D 10745295
    • EJ Calabrese LA Baldwin 2000 Radiation hormesis: the demise of a legitimate hypothesis Hum Exp Toxicol 19 76 84 1:STN:280:DC%2BD3c3htFaqsg%3D%3D 10745295
    • (2000) Hum Exp Toxicol , vol.19 , pp. 76-84
    • Calabrese, E.J.1    Baldwin, L.A.2
  • 114
    • 0038015515 scopus 로고    scopus 로고
    • Ethanol and hormesis
    • 1:CAS:528:DC%2BD3sXkvVKkuro%3D 12809430
    • EJ Calabrese LA Baldwin 2003 Ethanol and hormesis Crit Rev Toxicol 33 407 424 1:CAS:528:DC%2BD3sXkvVKkuro%3D 12809430
    • (2003) Crit Rev Toxicol , vol.33 , pp. 407-424
    • Calabrese, E.J.1    Baldwin, L.A.2
  • 116
    • 62349109928 scopus 로고    scopus 로고
    • The road to linearity: Shy linearity at low doses became the basis for carcinogen risk assessment
    • 1:CAS:528:DC%2BD1MXisVWrur0%3D 19247635
    • EJ Calabrese 2009 The road to linearity: shy linearity at low doses became the basis for carcinogen risk assessment Arch Toxicol 83 203 225 1:CAS:528:DC%2BD1MXisVWrur0%3D 19247635
    • (2009) Arch Toxicol , vol.83 , pp. 203-225
    • Calabrese, E.J.1
  • 117
    • 0017061099 scopus 로고
    • Effects of low metal levels on a clonal hydroid
    • 1:CAS:528:DyaE2sXms1aqug%3D%3D
    • ARD Stebbing 1976 Effects of low metal levels on a clonal hydroid J Mar Biol Assoc UK 56 977 994 1:CAS:528:DyaE2sXms1aqug%3D%3D
    • (1976) J Mar Biol Assoc UK , vol.56 , pp. 977-994
    • Stebbing, A.R.D.1
  • 118
    • 0017652208 scopus 로고
    • Model of 2 functionally antagonistic receptor populations activated by same agonist
    • 1:CAS:528:DyaE1cXotlKquw%3D%3D 592862
    • E Szabadi 1977 Model of 2 functionally antagonistic receptor populations activated by same agonist J Theor Biol 69 101 112 1:CAS:528:DyaE1cXotlKquw%3D%3D 592862
    • (1977) J Theor Biol , vol.69 , pp. 101-112
    • Szabadi, E.1
  • 120
    • 0034115903 scopus 로고    scopus 로고
    • Tales of two similar hypotheses: The rise and fall of chemical and radiation hormesis
    • 1:STN:280:DC%2BD3c3htFaqsw%3D%3D 10745296
    • EJ Calabrese LA Baldwin 2000 Tales of two similar hypotheses: the rise and fall of chemical and radiation hormesis Hum Exp Toxicol 19 85 97 1:STN:280:DC%2BD3c3htFaqsw%3D%3D 10745296
    • (2000) Hum Exp Toxicol , vol.19 , pp. 85-97
    • Calabrese, E.J.1    Baldwin, L.A.2
  • 121
    • 12844251475 scopus 로고    scopus 로고
    • The occurrence of hormetic dose responses in the toxicological literature, the hormesis database: An overview
    • 1:CAS:528:DC%2BD2MXms1KitQ%3D%3D 15667834
    • EJ Calabrese R Blain 2005 The occurrence of hormetic dose responses in the toxicological literature, the hormesis database: an overview Toxicol Appl Pharmacol 202 289 301 1:CAS:528:DC%2BD2MXms1KitQ%3D%3D 15667834
    • (2005) Toxicol Appl Pharmacol , vol.202 , pp. 289-301
    • Calabrese, E.J.1    Blain, R.2
  • 122
    • 34548436740 scopus 로고    scopus 로고
    • Low doses of radiation are protective in vitro and in vivo: Evolutionary origins
    • 1:CAS:528:DC%2BD2sXivVOhu7c%3D 18648638
    • REJ Mitchel 2006 Low doses of radiation are protective in vitro and in vivo: evolutionary origins Dose Response 4 75 90 1:CAS:528:DC%2BD2sXivVOhu7c%3D 18648638
    • (2006) Dose Response , vol.4 , pp. 75-90
    • Mitchel, R.E.J.1
  • 123
    • 70349305206 scopus 로고    scopus 로고
    • Hormesis [biological effects of low level exposure (BELLE)] and dermatology
    • 1:CAS:528:DC%2BD1cXntV2ktbo%3D 18648574
    • H-Y Thong HI Maibach 2008 Hormesis [biological effects of low level exposure (BELLE)] and dermatology Dose Response 6 1 15 1:CAS:528: DC%2BD1cXntV2ktbo%3D 18648574
    • (2008) Dose Response , vol.6 , pp. 1-15
    • Thong, H.-Y.1    Maibach, H.I.2
  • 125
    • 77958128472 scopus 로고    scopus 로고
    • Hormesis in environmental health: How hormesis will change the risk assessment process
    • in press
    • Calabrese EJ, Ricci PF (2010) Hormesis in environmental health: how hormesis will change the risk assessment process. Encycl Environ Health (in press)
    • (2010) Encycl Environ Health
    • Calabrese, E.J.1    Ricci, P.F.2
  • 126
    • 0032994225 scopus 로고    scopus 로고
    • Evidence that hormesis represents an "overcompensation" response to a disruption in homeostasis
    • EJ Calabrese 1999 Evidence that hormesis represents an "overcompensation" response to a disruption in homeostasis Ecotoxicol Environ Saf 42 135 137
    • (1999) Ecotoxicol Environ Saf , vol.42 , pp. 135-137
    • Calabrese, E.J.1
  • 127
    • 56749158033 scopus 로고    scopus 로고
    • Hormesis and plant biology
    • 1:CAS:528:DC%2BD1cXhsVGgsbjO
    • EJ Calabrese RB Blain 2009 Hormesis and plant biology Environ Poll. 157 42 48 1:CAS:528:DC%2BD1cXhsVGgsbjO
    • (2009) Environ Poll. , vol.157 , pp. 42-48
    • Calabrese, E.J.1    Blain, R.B.2
  • 128
    • 0038692031 scopus 로고    scopus 로고
    • Inorganics and hormesis
    • 1:CAS:528:DC%2BD3sXkvVKkur4%3D 12809427
    • EJ Calabrese LA Baldwin 2003 Inorganics and hormesis Crit Rev Toxicol 33 215 304 1:CAS:528:DC%2BD3sXkvVKkur4%3D 12809427
    • (2003) Crit Rev Toxicol , vol.33 , pp. 215-304
    • Calabrese, E.J.1    Baldwin, L.A.2
  • 129
    • 0038015520 scopus 로고    scopus 로고
    • Chemotherapeutics and hormesis
    • 1:CAS:528:DC%2BD3sXkvVKkurw%3D 12809428
    • EJ Calabrese LA Baldwin 2003 Chemotherapeutics and hormesis Crit Rev Toxicol 33 305 354 1:CAS:528:DC%2BD3sXkvVKkurw%3D 12809428
    • (2003) Crit Rev Toxicol , vol.33 , pp. 305-354
    • Calabrese, E.J.1    Baldwin, L.A.2
  • 130
    • 0037677608 scopus 로고    scopus 로고
    • Peptides and hormesis
    • 1:CAS:528:DC%2BD3sXkvVKkur0%3D 12809429
    • EJ Calabrese LA Baldwin 2003 Peptides and hormesis Crit Rev Toxicol 33 355 406 1:CAS:528:DC%2BD3sXkvVKkur0%3D 12809429
    • (2003) Crit Rev Toxicol , vol.33 , pp. 355-406
    • Calabrese, E.J.1    Baldwin, L.A.2
  • 132
    • 77949899311 scopus 로고
    • Memory retention-enhancement by cholinergic drug-combinations in mice
    • JF Flood GE Smith A Cherkin 1982 Memory retention-enhancement by cholinergic drug-combinations in mice Gerontologist 22 230 231
    • (1982) Gerontologist , vol.22 , pp. 230-231
    • Flood, J.F.1    Smith, G.E.2    Cherkin, A.3
  • 133
    • 0020955530 scopus 로고
    • Memory retention-potentiation of cholinergic drug-combinations in mice
    • 1:CAS:528:DyaL3sXks1Ciu70%3D 6877486
    • JF Flood GE Smith A Cherkin 1983 Memory retention-potentiation of cholinergic drug-combinations in mice Neurobiol Aging 4 37 43 1:CAS:528:DyaL3sXks1Ciu70%3D 6877486
    • (1983) Neurobiol Aging , vol.4 , pp. 37-43
    • Flood, J.F.1    Smith, G.E.2    Cherkin, A.3
  • 134
    • 77949899853 scopus 로고
    • Memory retention-enhancement by synergistic oral cholinergic drug-combination in mice
    • JF Flood GE Smith A Cherkin 1984 Memory retention-enhancement by synergistic oral cholinergic drug-combination in mice Gerontologist 24 149 158
    • (1984) Gerontologist , vol.24 , pp. 149-158
    • Flood, J.F.1    Smith, G.E.2    Cherkin, A.3
  • 135
    • 0021848533 scopus 로고
    • Memory enhancement-supra-additive effect of subcutaneous chlolinergic drug-combinations in mice
    • 1:CAS:528:DyaL2MXksVyis7c%3D 3927367
    • JF Flood GE Smith A Cherkin 1985 Memory enhancement-supra-additive effect of subcutaneous chlolinergic drug-combinations in mice Psychopharmacology 86 61 67 1:CAS:528:DyaL2MXksVyis7c%3D 3927367
    • (1985) Psychopharmacology , vol.86 , pp. 61-67
    • Flood, J.F.1    Smith, G.E.2    Cherkin, A.3
  • 136
    • 42449084179 scopus 로고    scopus 로고
    • Neuroscience and hormesis: Overview and general findings
    • 1:CAS:528:DC%2BD1cXltFCmt7c%3D 18432418
    • EJ Calabrese 2008 Neuroscience and hormesis: overview and general findings Crit Rev Toxicol 38 249 252 1:CAS:528:DC%2BD1cXltFCmt7c%3D 18432418
    • (2008) Crit Rev Toxicol , vol.38 , pp. 249-252
    • Calabrese, E.J.1
  • 138
    • 30744469267 scopus 로고    scopus 로고
    • Cancer biology and hormesis: Human tumor cell lines commonly display hormetic (biphasic) dose responses
    • 1:CAS:528:DC%2BD2MXht1elt7fJ 16422392
    • EJ Calabrese 2005 Cancer biology and hormesis: human tumor cell lines commonly display hormetic (biphasic) dose responses Crit Rev Toxicol 35 463 582 1:CAS:528:DC%2BD2MXht1elt7fJ 16422392
    • (2005) Crit Rev Toxicol , vol.35 , pp. 463-582
    • Calabrese, E.J.1
  • 139
    • 62349085355 scopus 로고
    • Demonstration of hormesis (increase in fatality rate) by penicillin
    • 18016510
    • WA Randall CW Price H Welch 1947 Demonstration of hormesis (increase in fatality rate) by penicillin Am J Pub Health 37 421 425 18016510
    • (1947) Am J Pub Health , vol.37 , pp. 421-425
    • Randall, W.A.1    Price, C.W.2    Welch, H.3
  • 140
    • 62349091239 scopus 로고
    • Increase in fatality rate of E. Typhosa for white mice by streptomycin
    • 1:CAS:528:DyaH28XjsVantA%3D%3D
    • H Welch CW Price WA Randall 1946 Increase in fatality rate of E. Typhosa for white mice by streptomycin J Am Pharm 35 155 158 1:CAS:528: DyaH28XjsVantA%3D%3D
    • (1946) J Am Pharm , vol.35 , pp. 155-158
    • Welch, H.1    Price, C.W.2    Randall, W.A.3
  • 141
    • 0347625839 scopus 로고    scopus 로고
    • Ouabain- and marinobufagenin-induced proliferation of human umbilical vein smooth muscle cells and a rat vascular smooth muscle cell lines, A7r5
    • 1:CAS:528:DC%2BD3sXps1SitLc%3D 14638550
    • J Abramowitz C Dai KK Hirschi RI Dmitieva PA Doris L Liu JC Allen 2003 Ouabain- and marinobufagenin-induced proliferation of human umbilical vein smooth muscle cells and a rat vascular smooth muscle cell lines, A7r5 Circulation 108 3048 3053 1:CAS:528:DC%2BD3sXps1SitLc%3D 14638550
    • (2003) Circulation , vol.108 , pp. 3048-3053
    • Abramowitz, J.1    Dai, C.2    Hirschi, K.K.3    Dmitieva, R.I.4    Doris, P.A.5    Liu, L.6    Allen, J.C.7
  • 142
    • 0034977171 scopus 로고    scopus 로고
    • Dual effects of ouabain on the regulation of proliferation and apoptosis in human prostatic smooth muscle cells
    • 1:CAS:528:DC%2BD3MXkvFemsL0%3D 11435898
    • S-C Chueh J-H Guh J Chen M-K Lai C-M Teng 2001 Dual effects of ouabain on the regulation of proliferation and apoptosis in human prostatic smooth muscle cells J Urol 166 347 353 1:CAS:528:DC%2BD3MXkvFemsL0%3D 11435898
    • (2001) J Urol , vol.166 , pp. 347-353
    • Chueh, S.-C.1    Guh, J.-H.2    Chen, J.3    Lai, M.-K.4    Teng, C.-M.5
  • 143
    • 68149154783 scopus 로고    scopus 로고
    • 2-mediated modulation of cytosolic signaling and organelle function in rat hippocampus
    • 1:CAS:528:DC%2BD1MXptlamsb4%3D 19430810
    • 2-mediated modulation of cytosolic signaling and organelle function in rat hippocampus Pflugers Arch 458 937 952 1:CAS:528:DC%2BD1MXptlamsb4%3D 19430810
    • (2009) Pflugers Arch , vol.458 , pp. 937-952
    • Gerich, F.J.1    Funke, F.2    Hildebrandt, B.3    Fahauer, M.4    Müller, M.5
  • 144
    • 40949119810 scopus 로고    scopus 로고
    • Superoxide-induced potentiation in the hippocampus requires activation of ryanodine receptor type 3 and ERK
    • 1:CAS:528:DC%2BD1cXksVGls7Y%3D 18199822
    • AT Huddleston W Tang H Takeshima SL Hamilton E Klann 2008 Superoxide-induced potentiation in the hippocampus requires activation of ryanodine receptor type 3 and ERK J Neurophysiol 99 1565 1571 1:CAS:528:DC%2BD1cXksVGls7Y%3D 18199822
    • (2008) J Neurophysiol , vol.99 , pp. 1565-1571
    • Huddleston, A.T.1    Tang, W.2    Takeshima, H.3    Hamilton, S.L.4    Klann, E.5
  • 145
    • 47249122974 scopus 로고    scopus 로고
    • A direct redox regulation of protein kinase C isoenzymes mediates oxidant-induced neuritogenesis in PC12 cells
    • 1:CAS:528:DC%2BD1cXlvFyjs7s%3D 18375950
    • R Gopalakrishna U Gundimeda JE Schiffman TH McNeill 2008 A direct redox regulation of protein kinase C isoenzymes mediates oxidant-induced neuritogenesis in PC12 cells J Biol Chem 283 14430 14444 1:CAS:528: DC%2BD1cXlvFyjs7s%3D 18375950
    • (2008) J Biol Chem , vol.283 , pp. 14430-14444
    • Gopalakrishna, R.1    Gundimeda, U.2    Schiffman, J.E.3    McNeill, T.H.4
  • 146
    • 33748466565 scopus 로고    scopus 로고
    • Specificity in reactive oxidant signaling: Think globally, act locally
    • 1:CAS:528:DC%2BD28XptV2jtLo%3D 16923830
    • LS Terada 2006 Specificity in reactive oxidant signaling: think globally, act locally J Cell Biol 174 615 623 1:CAS:528:DC%2BD28XptV2jtLo%3D 16923830
    • (2006) J Cell Biol , vol.174 , pp. 615-623
    • Terada, L.S.1
  • 147
    • 0030611750 scopus 로고    scopus 로고
    • Activation of NF-kappaB protects hippocampal neurons against oxidative stress-induced apoptosis: Evidence for induction of manganese superoxide dismutase and suppression of peroxynitrite production and protein tyrosine nitration
    • 1:CAS:528:DyaK2sXmtl2itLs%3D 9335256
    • MP Mattson Y Goodman H Luo W Fu K Furukawa 1997 Activation of NF-kappaB protects hippocampal neurons against oxidative stress-induced apoptosis: evidence for induction of manganese superoxide dismutase and suppression of peroxynitrite production and protein tyrosine nitration J Neurosci Res 49 681 697 1:CAS:528:DyaK2sXmtl2itLs%3D 9335256
    • (1997) J Neurosci Res , vol.49 , pp. 681-697
    • Mattson, M.P.1    Goodman, Y.2    Luo, H.3    Fu, W.4    Furukawa, K.5
  • 149
    • 59349110661 scopus 로고    scopus 로고
    • Brain inflammation and adult neurogenesis: The dual role of microglia
    • 1:CAS:528:DC%2BD1MXhsFKrtL4%3D 18662748
    • CT Ekdahl Z Kokaia O Lindvall 2009 Brain inflammation and adult neurogenesis: the dual role of microglia Neuroscience 158 1021 1029 1:CAS:528:DC%2BD1MXhsFKrtL4%3D 18662748
    • (2009) Neuroscience , vol.158 , pp. 1021-1029
    • Ekdahl, C.T.1    Kokaia, Z.2    Lindvall, O.3
  • 151
    • 73649130269 scopus 로고    scopus 로고
    • Pathogenesis of Parkinson's disease: Emerging role of molecular chaperones
    • 1:CAS:528:DC%2BC3cXjslCntA%3D%3D 20036196
    • R Bandopadhyay J de Belleroche 2010 Pathogenesis of Parkinson's disease: emerging role of molecular chaperones Trends Mol Med 16 27 36 1:CAS:528:DC%2BC3cXjslCntA%3D%3D 20036196
    • (2010) Trends Mol Med , vol.16 , pp. 27-36
    • Bandopadhyay, R.1    De Belleroche, J.2
  • 152
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • 1:CAS:528:DC%2BD1cXnsVOlurY%3D 18519635
    • RI Morimoto 2008 Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging Genes Dev 22 1427 1438 1:CAS:528: DC%2BD1cXnsVOlurY%3D 18519635
    • (2008) Genes Dev , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 153
    • 84934436352 scopus 로고    scopus 로고
    • Chaperones as parts of cellular networks
    • 17205675
    • P Csermely C Söti GL Blatch 2007 Chaperones as parts of cellular networks Adv Exp Med Biol 594 55 63 17205675
    • (2007) Adv Exp Med Biol , vol.594 , pp. 55-63
    • Csermely, P.1    Söti, C.2    Blatch, G.L.3
  • 154
    • 70349305183 scopus 로고    scopus 로고
    • Inhibitors of protein aggregation and toxicity
    • 1:CAS:528:DC%2BD1MXovVOjtL0%3D 19614577
    • H Amijee J Madine DA Middleton AJ Doig 2009 Inhibitors of protein aggregation and toxicity Biochem Soc Trans 37 692 696 1:CAS:528: DC%2BD1MXovVOjtL0%3D 19614577
    • (2009) Biochem Soc Trans , vol.37 , pp. 692-696
    • Amijee, H.1    Madine, J.2    Middleton, D.A.3    Doig, A.J.4
  • 155
    • 33645299025 scopus 로고    scopus 로고
    • Ageing and neuronal vulnerability
    • 1:CAS:528:DC%2BD28Xis1GksrY%3D 16552414
    • MP Mattson T Magnus 2006 Ageing and neuronal vulnerability Nat Rev Neurosci 7 278 294 1:CAS:528:DC%2BD28Xis1GksrY%3D 16552414
    • (2006) Nat Rev Neurosci , vol.7 , pp. 278-294
    • Mattson, M.P.1    Magnus, T.2
  • 156
    • 39149143645 scopus 로고    scopus 로고
    • Chaperone machines in action
    • 1:CAS:528:DC%2BD1cXitVGitrc%3D 18242075
    • HR Saibil 2008 Chaperone machines in action Curr Opin Struct Biol 18 35 42 1:CAS:528:DC%2BD1cXitVGitrc%3D 18242075
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 35-42
    • Saibil, H.R.1
  • 157
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • 1:CAS:528:DC%2BD1cXht1ynt7rK 18723507
    • CG Glabe 2008 Structural classification of toxic amyloid oligomers J Biol Chem 283 29639 29643 1:CAS:528:DC%2BD1cXht1ynt7rK 18723507
    • (2008) J Biol Chem , vol.283 , pp. 29639-29643
    • Glabe, C.G.1
  • 158
    • 68649113747 scopus 로고    scopus 로고
    • The role of molecular chaperones in human misfolding diseases
    • 1:CAS:528:DC%2BD1MXhtVent7nP 19393652
    • SA Broadley FU Hartl 2009 The role of molecular chaperones in human misfolding diseases FEBS Lett 583 2647 2653 1:CAS:528:DC%2BD1MXhtVent7nP 19393652
    • (2009) FEBS Lett , vol.583 , pp. 2647-2653
    • Broadley, S.A.1    Hartl, F.U.2
  • 159
    • 77749319656 scopus 로고    scopus 로고
    • A cellular perspective on conformational disease: The role of genetic background and proteostasis networks
    • 1:CAS:528:DC%2BC3cXit1OgsLg%3D 20053547
    • T Gidalevitz EA Kikis RI Morimoto 2010 A cellular perspective on conformational disease: the role of genetic background and proteostasis networks Curr Opin Struct Biol 20 23 32 1:CAS:528:DC%2BC3cXit1OgsLg%3D 20053547
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 23-32
    • Gidalevitz, T.1    Kikis, E.A.2    Morimoto, R.I.3
  • 160
    • 78149339310 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis pathogenesis: A journey through the secretory pathway
    • Epub ahead of print
    • Nassif M, Matus S, Castillo K, Hetz C (2010) Amyotrophic lateral sclerosis pathogenesis: a journey through the secretory pathway. Antioxid Redox Signal. [Epub ahead of print]
    • (2010) Antioxid Redox Signal
    • Nassif, M.1    Matus, S.2    Castillo, K.3    Hetz, C.4
  • 161
    • 39149104320 scopus 로고    scopus 로고
    • The role for endoplasmic reticulum stress in diabetes mellitus
    • 1:CAS:528:DC%2BD1cXivFGqs7s%3D 18048764
    • DL Eizirik AK Cardozo M Cnop 2008 The role for endoplasmic reticulum stress in diabetes mellitus Endocr Rev 29 42 61 1:CAS:528:DC%2BD1cXivFGqs7s%3D 18048764
    • (2008) Endocr Rev , vol.29 , pp. 42-61
    • Eizirik, D.L.1    Cardozo, A.K.2    Cnop, M.3
  • 162
    • 65349093893 scopus 로고    scopus 로고
    • The unfolded protein response is activated in pretangle neurons in Alzheimer's disease hippocampus
    • 1:CAS:528:DC%2BD1MXksVOkt74%3D 19264902
    • JJ Hoozemans ES van Haastert DA Nijholt AJ Rozemuller P Eikelenboom W Scheper 2009 The unfolded protein response is activated in pretangle neurons in Alzheimer's disease hippocampus Am J Pathol 174 1241 1251 1:CAS:528: DC%2BD1MXksVOkt74%3D 19264902
    • (2009) Am J Pathol , vol.174 , pp. 1241-1251
    • Hoozemans, J.J.1    Van Haastert, E.S.2    Nijholt, D.A.3    Rozemuller, A.J.4    Eikelenboom, P.5    Scheper, W.6
  • 163
    • 63149175877 scopus 로고    scopus 로고
    • Endoplasmic reticulum protein quality control in neurodegenerative disease: The good, the bad and the therapy
    • 1:CAS:528:DC%2BD1MXjsFGqsbs%3D 19199926
    • W Scheper JJ Hoozemans 2009 Endoplasmic reticulum protein quality control in neurodegenerative disease: the good, the bad and the therapy Curr Med Chem 16 615 626 1:CAS:528:DC%2BD1MXjsFGqsbs%3D 19199926
    • (2009) Curr Med Chem , vol.16 , pp. 615-626
    • Scheper, W.1    Hoozemans, J.J.2
  • 164
    • 67349217063 scopus 로고    scopus 로고
    • ER and aging-protein folding and the ER stress response
    • 1:CAS:528:DC%2BD1MXptVKrtL4%3D 19491040
    • N Naidoo 2009 ER and aging-protein folding and the ER stress response Ageing Res Rev 8 150 159 1:CAS:528:DC%2BD1MXptVKrtL4%3D 19491040
    • (2009) Ageing Res Rev , vol.8 , pp. 150-159
    • Naidoo, N.1
  • 165
    • 43249109174 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress responses
    • 18038217
    • M Schröder 2008 Endoplasmic reticulum stress responses Cell Mol Life Sci 65 862 894 18038217
    • (2008) Cell Mol Life Sci , vol.65 , pp. 862-894
    • Schröder, M.1
  • 166
    • 26044431774 scopus 로고    scopus 로고
    • Endoplasmic reticulum calcium signaling in nerve cells
    • 15709699
    • A Verkhratsky 2004 Endoplasmic reticulum calcium signaling in nerve cells Biol Res 37 693 699 15709699
    • (2004) Biol Res , vol.37 , pp. 693-699
    • Verkhratsky, A.1
  • 167
    • 16344364156 scopus 로고    scopus 로고
    • Bcl-2 enhances Ca(2+) signaling to support the intrinsic regenerative capacity of CNS axons
    • 1:CAS:528:DC%2BD2MXitV2itrg%3D 15719013
    • J Jiao X Huang RA Feit-Leithman RL Neve W Snider DA Dartt DF Chen 2005 Bcl-2 enhances Ca(2+) signaling to support the intrinsic regenerative capacity of CNS axons EMBO J 24 1068 1078 1:CAS:528:DC%2BD2MXitV2itrg%3D 15719013
    • (2005) EMBO J , vol.24 , pp. 1068-1078
    • Jiao, J.1    Huang, X.2    Feit-Leithman, R.A.3    Neve, R.L.4    Snider, W.5    Dartt, D.A.6    Chen, D.F.7
  • 169
    • 54049126512 scopus 로고    scopus 로고
    • Exercise training acts as a therapeutic strategy for reduction of the pathogenic phenotypes for Alzheimer's disease in an NSE=APPsw-transgenic model
    • 1:CAS:528:DC%2BD1cXht1KrurfO 18813861
    • HS Um EB Kang YH Leem IH Cho CH Yang KR Chae DY Hwang JY Cho 2008 Exercise training acts as a therapeutic strategy for reduction of the pathogenic phenotypes for Alzheimer's disease in an NSE=APPsw-transgenic model Int J Mol Med 22 529 539 1:CAS:528:DC%2BD1cXht1KrurfO 18813861
    • (2008) Int J Mol Med , vol.22 , pp. 529-539
    • Um, H.S.1    Kang, E.B.2    Leem, Y.H.3    Cho, I.H.4    Yang, C.H.5    Chae, K.R.6    Hwang, D.Y.7    Cho, J.Y.8
  • 170
    • 45549091524 scopus 로고    scopus 로고
    • The stress rheostat: An interplay between the unfolded protein response (UPR) and autophagy in neurodegeneration
    • 1:CAS:528:DC%2BD1cXktlWgsb4%3D 18473817
    • S Matus F Lisbona M Torres C León P Thielen C Hetz 2008 The stress rheostat: an interplay between the unfolded protein response (UPR) and autophagy in neurodegeneration Curr Mol Med 8 157 172 1:CAS:528: DC%2BD1cXktlWgsb4%3D 18473817
    • (2008) Curr Mol Med , vol.8 , pp. 157-172
    • Matus, S.1    Lisbona, F.2    Torres, M.3    León, C.4    Thielen, P.5    Hetz, C.6
  • 172
    • 70349612498 scopus 로고    scopus 로고
    • Autophagy for the avoidance of neurodegeneration
    • 1:CAS:528:DC%2BD1MXht12qtbbL 19797764
    • F Madeo T Eisenberg G Kroemer 2009 Autophagy for the avoidance of neurodegeneration Genes Dev 23 2253 2259 1:CAS:528:DC%2BD1MXht12qtbbL 19797764
    • (2009) Genes Dev , vol.23 , pp. 2253-2259
    • Madeo, F.1    Eisenberg, T.2    Kroemer, G.3
  • 173
    • 38749104284 scopus 로고    scopus 로고
    • Ablation of the UPR-mediator CHOP restores motor function and reduces demyelination in Charcot-Marie-Tooth 1B mice
    • 1:CAS:528:DC%2BD1cXit1Snsb0%3D 18255032
    • M Pennuto E Tinelli M Malaguti U Del Carro M D'Antonio D Ron A Quattrini ML Feltri L Wrabetz 2008 Ablation of the UPR-mediator CHOP restores motor function and reduces demyelination in Charcot-Marie-Tooth 1B mice Neuron 57 393 405 1:CAS:528:DC%2BD1cXit1Snsb0%3D 18255032
    • (2008) Neuron , vol.57 , pp. 393-405
    • Pennuto, M.1    Tinelli, E.2    Malaguti, M.3    Del Carro, U.4    D'Antonio, M.5    Ron, D.6    Quattrini, A.7    Feltri, M.L.8    Wrabetz, L.9
  • 174
    • 47249157360 scopus 로고    scopus 로고
    • Protein kinase Cu is required for autophagy in response to stress in the endoplasmic reticulum
    • 1:CAS:528:DC%2BD1cXmtlynu7k%3D 18356160
    • K Sakaki J Wu RJ Kaufman 2008 Protein kinase Cu is required for autophagy in response to stress in the endoplasmic reticulum J Biol Chem 283 15370 15380 1:CAS:528:DC%2BD1cXmtlynu7k%3D 18356160
    • (2008) J Biol Chem , vol.283 , pp. 15370-15380
    • Sakaki, K.1    Wu, J.2    Kaufman, R.J.3
  • 175
    • 34748850786 scopus 로고    scopus 로고
    • Glucose restriction extends Caenorhabditis elegans life span by inducing mitochondrial respiration and increasing oxidative stress
    • 1:CAS:528:DC%2BD2sXht1Sjsr3J 17908557
    • TJ Schulz K Zarse A Voigt N Urban M Birringer M Ristow 2007 Glucose restriction extends Caenorhabditis elegans life span by inducing mitochondrial respiration and increasing oxidative stress Cell Metab 6 280 293 1:CAS:528:DC%2BD2sXht1Sjsr3J 17908557
    • (2007) Cell Metab , vol.6 , pp. 280-293
    • Schulz, T.J.1    Zarse, K.2    Voigt, A.3    Urban, N.4    Birringer, M.5    Ristow, M.6
  • 176
    • 60749108379 scopus 로고    scopus 로고
    • Regulation of autophagy by reactive oxygen species (ROS): Implications for cancer progression and treatment
    • 1:CAS:528:DC%2BD1MXitlWiu7Y%3D 18828708
    • MB Azad Y Chen SB Gibson 2009 Regulation of autophagy by reactive oxygen species (ROS): implications for cancer progression and treatment Antioxid Redox Signal 11 777 790 1:CAS:528:DC%2BD1MXitlWiu7Y%3D 18828708
    • (2009) Antioxid Redox Signal , vol.11 , pp. 777-790
    • Azad, M.B.1    Chen, Y.2    Gibson, S.B.3
  • 177
    • 74049140368 scopus 로고    scopus 로고
    • Dimeric coiled-coil structure of Saccharomyces cerevisiae Atg16 and its functional significance in autophagy
    • 1:CAS:528:DC%2BC3cXkvFCn 19889643
    • Y Fujioka NN Noda H Nakatogawa Y Ohsumi F Inagaki 2010 Dimeric coiled-coil structure of Saccharomyces cerevisiae Atg16 and its functional significance in autophagy J Biol Chem 285 1508 1515 1:CAS:528:DC%2BC3cXkvFCn 19889643
    • (2010) J Biol Chem , vol.285 , pp. 1508-1515
    • Fujioka, Y.1    Noda, N.N.2    Nakatogawa, H.3    Ohsumi, Y.4    Inagaki, F.5
  • 179
    • 77950228149 scopus 로고    scopus 로고
    • Jun proteins are starvation-regulated inhibitors of autophagy
    • 1:CAS:528:DC%2BC3cXjtFygt7c%3D 20197466
    • O Yogev R Goldberg S Anzi O Yogev E Shaulian 2010 Jun proteins are starvation-regulated inhibitors of autophagy Cancer Res 70 2318 2327 1:CAS:528:DC%2BC3cXjtFygt7c%3D 20197466
    • (2010) Cancer Res , vol.70 , pp. 2318-2327
    • Yogev, O.1    Goldberg, R.2    Anzi, S.3    Yogev, O.4    Shaulian, E.5
  • 180
    • 56749117866 scopus 로고    scopus 로고
    • Interactions between Hsp70 and the hydrophobic core of alpha-synuclein inhibit fibril assembly
    • 1:CAS:528:DC%2BD1cXhtlWqtLjJ 18975920
    • KC Luk IP Mills JQ Trojanowski VM Lee 2008 Interactions between Hsp70 and the hydrophobic core of alpha-synuclein inhibit fibril assembly Biochemistry 47 12614 12625 1:CAS:528:DC%2BD1cXhtlWqtLjJ 18975920
    • (2008) Biochemistry , vol.47 , pp. 12614-12625
    • Luk, K.C.1    Mills, I.P.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 182
    • 30544442097 scopus 로고    scopus 로고
    • Acetylcarnitine and cellular stress response: Roles in nutritional redox homeostasis andregulation of longevity genes
    • 1:CAS:528:DC%2BD28XksVaksA%3D%3D 16413418
    • V Calabrese AMG Stella M Calvani DA Butterfield 2006 Acetylcarnitine and cellular stress response: roles in nutritional redox homeostasis andregulation of longevity genes J Nutr Biochem 17 73 88 1:CAS:528:DC%2BD28XksVaksA%3D%3D 16413418
    • (2006) J Nutr Biochem , vol.17 , pp. 73-88
    • Calabrese, V.1    Stella, A.M.G.2    Calvani, M.3    Butterfield, D.A.4
  • 184
    • 0032860171 scopus 로고    scopus 로고
    • Formation of propionate after short-term ethanol treatment and its interaction with the carnitine pool in rat
    • 1:CAS:528:DyaK1MXmsFaqur8%3D 10548162
    • V Calabrese V Rizza 1999 Formation of propionate after short-term ethanol treatment and its interaction with the carnitine pool in rat Alcohol 19 169 176 1:CAS:528:DyaK1MXmsFaqur8%3D 10548162
    • (1999) Alcohol , vol.19 , pp. 169-176
    • Calabrese, V.1    Rizza, V.2
  • 185
    • 5644229645 scopus 로고    scopus 로고
    • Increased formation of short-chain organic acids after chronic ethanol administration and its interaction with the carnitine pool in rat
    • 1:CAS:528:DC%2BD2cXos1Klsrg%3D 15488476
    • V Calabrese M Calvani DA Butterfield 2004 Increased formation of short-chain organic acids after chronic ethanol administration and its interaction with the carnitine pool in rat Arch Biochem Biophys 431 271 278 1:CAS:528:DC%2BD2cXos1Klsrg%3D 15488476
    • (2004) Arch Biochem Biophys , vol.431 , pp. 271-278
    • Calabrese, V.1    Calvani, M.2    Butterfield, D.A.3
  • 186
    • 69249113803 scopus 로고    scopus 로고
    • Carnitine insufficiency caused by aging and overnutrition compromises mitochondrial performance and metabolic control
    • 1:CAS:528:DC%2BD1MXpvFKitLc%3D 19553674
    • RC Noland TR Koves SE Seiler H Lum RM Lust O Ilkayeva RD Stevens FG Hegardt DM Muoio 2009 Carnitine insufficiency caused by aging and overnutrition compromises mitochondrial performance and metabolic control J Biol Chem 284 22840 22852 1:CAS:528:DC%2BD1MXpvFKitLc%3D 19553674
    • (2009) J Biol Chem , vol.284 , pp. 22840-22852
    • Noland, R.C.1    Koves, T.R.2    Seiler, S.E.3    Lum, H.4    Lust, R.M.5    Ilkayeva, O.6    Stevens, R.D.7    Hegardt, F.G.8    Muoio, D.M.9
  • 188
    • 0012738864 scopus 로고    scopus 로고
    • Pharmacokinetics of l-carnitine
    • 1:CAS:528:DC%2BD3sXnslGms74%3D 12908852
    • AM Evans G Fornasini 2003 Pharmacokinetics of l-carnitine Clin Pharmacokinet 42 941 967 1:CAS:528:DC%2BD3sXnslGms74%3D 12908852
    • (2003) Clin Pharmacokinet , vol.42 , pp. 941-967
    • Evans, A.M.1    Fornasini, G.2
  • 189
    • 10644229056 scopus 로고    scopus 로고
    • Kinetics, pharmacokinetics, and regulation of l-carnitine and acetyl-l-carnitine metabolism
    • 1:CAS:528:DC%2BD2MXjvFOhug%3D%3D 15591001
    • CJ Rebouche 2004 Kinetics, pharmacokinetics, and regulation of l-carnitine and acetyl-l-carnitine metabolism Ann N Y Acad Sci 1033 30 41 1:CAS:528:DC%2BD2MXjvFOhug%3D%3D 15591001
    • (2004) Ann N y Acad Sci , vol.1033 , pp. 30-41
    • Rebouche, C.J.1
  • 190
    • 4444315751 scopus 로고    scopus 로고
    • Carnitine: A nutritional, biosynthetic, and functional perspective
    • 1:CAS:528:DC%2BD2cXnsVyrurs%3D 15363636
    • A Steiber J Kerner CL Hoppel 2004 Carnitine: a nutritional, biosynthetic, and functional perspective Mol Aspects Med 25 455 473 1:CAS:528: DC%2BD2cXnsVyrurs%3D 15363636
    • (2004) Mol Aspects Med , vol.25 , pp. 455-473
    • Steiber, A.1    Kerner, J.2    Hoppel, C.L.3
  • 192
    • 0024313361 scopus 로고
    • Carnitine status of lactoovovegetarians and strict vegetarian adults and children
    • 1:STN:280:DyaL1MzjtlGgsA%3D%3D 2756917
    • KA Lombard AL Olson SE Nelson CJ Rebouche 1989 Carnitine status of lactoovovegetarians and strict vegetarian adults and children Am J Clin Nutr 50 301 306 1:STN:280:DyaL1MzjtlGgsA%3D%3D 2756917
    • (1989) Am J Clin Nutr , vol.50 , pp. 301-306
    • Lombard, K.A.1    Olson, A.L.2    Nelson, S.E.3    Rebouche, C.J.4
  • 193
    • 0028222594 scopus 로고
    • Effect of intravenous l-carnitine on carnitine homeostasis and fuel metabolism during exercise in humans
    • 1:CAS:528:DyaK2cXmt1Wls7c%3D 8004884
    • EP Brass CL Hoppel WR Hiatt 1994 Effect of intravenous l-carnitine on carnitine homeostasis and fuel metabolism during exercise in humans Clin Pharmacol Ther 55 681 692 1:CAS:528:DyaK2cXmt1Wls7c%3D 8004884
    • (1994) Clin Pharmacol Ther , vol.55 , pp. 681-692
    • Brass, E.P.1    Hoppel, C.L.2    Hiatt, W.R.3
  • 194
    • 0030983840 scopus 로고    scopus 로고
    • The effect of starvation on brain carnitine concentration in neonatal rats
    • 1:CAS:528:DyaK2sXmslOqsbc%3D 9327367
    • R Murakami A Tanaka H Nakamura 1997 The effect of starvation on brain carnitine concentration in neonatal rats J Pediatr Gastroenterol Nutr 25 385 387 1:CAS:528:DyaK2sXmslOqsbc%3D 9327367
    • (1997) J Pediatr Gastroenterol Nutr , vol.25 , pp. 385-387
    • Murakami, R.1    Tanaka, A.2    Nakamura, H.3
  • 195
    • 0021024932 scopus 로고
    • Carnitine-metabolism and functions
    • 1:CAS:528:DyaL2cXmsFGgsQ%3D%3D 6361812
    • J Bremer 1983 Carnitine-metabolism and functions Physiol Rev 63 1420 1480 1:CAS:528:DyaL2cXmsFGgsQ%3D%3D 6361812
    • (1983) Physiol Rev , vol.63 , pp. 1420-1480
    • Bremer, J.1
  • 198
    • 33745557847 scopus 로고    scopus 로고
    • Nucleocytosolic acetylcoenzyme a synthetase is required for histone acetylation and global transcription
    • 1:CAS:528:DC%2BD28XotVCjurk%3D 16857587
    • H Takahashi JM McCaffery RA Irizarry JD Boeke 2006 Nucleocytosolic acetylcoenzyme a synthetase is required for histone acetylation and global transcription Mol Cell 23 207 217 1:CAS:528:DC%2BD28XotVCjurk%3D 16857587
    • (2006) Mol Cell , vol.23 , pp. 207-217
    • Takahashi, H.1    McCaffery, J.M.2    Irizarry, R.A.3    Boeke, J.D.4
  • 199
    • 34247634168 scopus 로고    scopus 로고
    • Post-translational modifications of rat liver mitochondrial outer membrane proteins identified by mass spectrometry
    • 1:CAS:528:DC%2BD2sXkvFOrsrs%3D 17478130
    • AM Distler J Kerner CL Hoppel 2007 Post-translational modifications of rat liver mitochondrial outer membrane proteins identified by mass spectrometry Biochim Biophys Acta 1774 628 636 1:CAS:528:DC%2BD2sXkvFOrsrs%3D 17478130
    • (2007) Biochim Biophys Acta , vol.1774 , pp. 628-636
    • Distler, A.M.1    Kerner, J.2    Hoppel, C.L.3
  • 200
    • 0033955887 scopus 로고    scopus 로고
    • Secondary carnitine deficiency and impaired docosahexaenoic [22:6n-3] acid synthesis: A common denominator in thepathophysiology of diseases of oxidative phosphorylation and beta-oxidation
    • 1:CAS:528:DC%2BD3cXhtFamt70%3D 10683429
    • JP Infante VA Huszagh 2000 Secondary carnitine deficiency and impaired docosahexaenoic [22:6n-3] acid synthesis: a common denominator in thepathophysiology of diseases of oxidative phosphorylation and beta-oxidation FEBS Lett 468 1 5 1:CAS:528:DC%2BD3cXhtFamt70%3D 10683429
    • (2000) FEBS Lett , vol.468 , pp. 1-5
    • Infante, J.P.1    Huszagh, V.A.2
  • 201
    • 14144255699 scopus 로고    scopus 로고
    • Acetylcarnitine induces heme oxygenase in rat astrocytes and protects against oxidative stress: Involvement of the transcription factor Nrf2
    • 1:CAS:528:DC%2BD2MXhtFOmt70%3D 15641110
    • V Calabrese A Ravagna C Colombrita G Scapagnini E Guagliano M Calvani DA Butterfield AM Giuffrida Stella 2005 Acetylcarnitine induces heme oxygenase in rat astrocytes and protects against oxidative stress: involvement of the transcription factor Nrf2 J Neurosci Res 79 509 521 1:CAS:528: DC%2BD2MXhtFOmt70%3D 15641110
    • (2005) J Neurosci Res , vol.79 , pp. 509-521
    • Calabrese, V.1    Ravagna, A.2    Colombrita, C.3    Scapagnini, G.4    Guagliano, E.5    Calvani, M.6    Butterfield, D.A.7    Giuffrida Stella, A.M.8
  • 202
    • 0242580631 scopus 로고    scopus 로고
    • "Brain-specific" nutrients: A memory cure?
    • 1:CAS:528:DC%2BD3sXptVWmu7Y%3D 14624946
    • MA McDaniel SF Maier GO Einstein 2003 "Brain-specific" nutrients: a memory cure? Nutrition 19 957 975 1:CAS:528:DC%2BD3sXptVWmu7Y%3D 14624946
    • (2003) Nutrition , vol.19 , pp. 957-975
    • McDaniel, M.A.1    Maier, S.F.2    Einstein, G.O.3
  • 203
    • 66149090372 scopus 로고    scopus 로고
    • Cytoprotective effect of cetyl-l-carnitine evidenced by analysis of gene expression in the rat brain
    • 1:CAS:528:DC%2BD1MXivFylt7k%3D 19199082
    • G Traina G Federighi M Brunelli R Scuri 2009 Cytoprotective effect of cetyl-l-carnitine evidenced by analysis of gene expression in the rat brain Mol Neurobiol 39 101 106 1:CAS:528:DC%2BD1MXivFylt7k%3D 19199082
    • (2009) Mol Neurobiol , vol.39 , pp. 101-106
    • Traina, G.1    Federighi, G.2    Brunelli, M.3    Scuri, R.4
  • 204
    • 1842525777 scopus 로고    scopus 로고
    • Increased expression of heat shock proteins in rat brain during aging: Relationship with mitochondrial function and glutathione redox state
    • 1:CAS:528:DC%2BD2cXivVWmurk%3D 15063109
    • V Calabrese G Scapagnini A Ravagna C Colombrita F Spadaro DA Butterfield AM Giuffrida Stella 2004 Increased expression of heat shock proteins in rat brain during aging: relationship with mitochondrial function and glutathione redox state Mech Ageing Dev 125 325 335 1:CAS:528:DC%2BD2cXivVWmurk%3D 15063109
    • (2004) Mech Ageing Dev , vol.125 , pp. 325-335
    • Calabrese, V.1    Scapagnini, G.2    Ravagna, A.3    Colombrita, C.4    Spadaro, F.5    Butterfield, D.A.6    Giuffrida Stella, A.M.7
  • 205
    • 8844286158 scopus 로고    scopus 로고
    • Identification of differentially expressed genes induced in the rat brain by acetyl-l-carnitine as evidenced by suppression subtractive hybridisation
    • 1:CAS:528:DC%2BD2cXhtVSktr3K 15548429
    • G Traina S Valleggi R Bernardi 2004 Identification of differentially expressed genes induced in the rat brain by acetyl-l-carnitine as evidenced by suppression subtractive hybridisation Mol Brain Res 132 57 63 1:CAS:528:DC%2BD2cXhtVSktr3K 15548429
    • (2004) Mol Brain Res , vol.132 , pp. 57-63
    • Traina, G.1    Valleggi, S.2    Bernardi, R.3
  • 206
    • 33746223208 scopus 로고    scopus 로고
    • Acetyl-l-carnitine up-regulates expression of voltage-dependent anion channel in the rat brain
    • 1:CAS:528:DC%2BD28XjvVWmtb0%3D 16527372
    • G Traina R Bernardi M Rizzo M Calvani M Durante M Brunelli 2006 Acetyl-l-carnitine up-regulates expression of voltage-dependent anion channel in the rat brain Neurochem Int 48 673 678 1:CAS:528:DC%2BD28XjvVWmtb0%3D 16527372
    • (2006) Neurochem Int , vol.48 , pp. 673-678
    • Traina, G.1    Bernardi, R.2    Rizzo, M.3    Calvani, M.4    Durante, M.5    Brunelli, M.6
  • 207
    • 4344617955 scopus 로고    scopus 로고
    • Neuroprotective effect of l-carnitine in the 3-nitropropionic acid [3-NPA]-evoked neurotoxicity in rats
    • 1:CAS:528:DC%2BD2cXntFWqt7k%3D 15331167
    • Z Binienda A Virmani B Przybyla-Zawislak L Schmued 2004 Neuroprotective effect of l-carnitine in the 3-nitropropionic acid [3-NPA]-evoked neurotoxicity in rats Neurosci Lett 367 264 267 1:CAS:528:DC%2BD2cXntFWqt7k%3D 15331167
    • (2004) Neurosci Lett , vol.367 , pp. 264-267
    • Binienda, Z.1    Virmani, A.2    Przybyla-Zawislak, B.3    Schmued, L.4
  • 208
    • 33845664452 scopus 로고    scopus 로고
    • Reversal of mitochondrial defects before ischemia protects the aged heart
    • 1:CAS:528:DC%2BD28XmvV2itbk%3D 16793872
    • EJ Lesnefsky D He S Moghaddas CL Hoppel 2006 Reversal of mitochondrial defects before ischemia protects the aged heart FASEB J 20 1543 1545 1:CAS:528:DC%2BD28XmvV2itbk%3D 16793872
    • (2006) FASEB J , vol.20 , pp. 1543-1545
    • Lesnefsky, E.J.1    He, D.2    Moghaddas, S.3    Hoppel, C.L.4
  • 209
    • 33747270685 scopus 로고    scopus 로고
    • L-acetylcarnitine: A proposed therapeutic agent for painful peripheral neuropathies
    • 1:CAS:528:DC%2BD28Xpt1ejurw%3D 18615142
    • S Chiechio A Copani F Nicoletti RW Gereau 4th 2006 l-acetylcarnitine: a proposed therapeutic agent for painful peripheral neuropathies Curr Neuropharmacol 4 233 237 1:CAS:528:DC%2BD28Xpt1ejurw%3D 18615142
    • (2006) Curr Neuropharmacol , vol.4 , pp. 233-237
    • Chiechio, S.1    Copani, A.2    Nicoletti, F.3    Gereau IV, R.W.4
  • 210
    • 77950537328 scopus 로고    scopus 로고
    • Transcriptional regulation of type-2 metabotropic glutamate receptors: An epigenetic path to novel treatments for chronic pain
    • 1:CAS:528:DC%2BC3cXjvFKksbs%3D 20064669
    • S Chiechio A Copani M Zammataro G Battaglia RW Gereau 4th F Nicoletti 2010 Transcriptional regulation of type-2 metabotropic glutamate receptors: an epigenetic path to novel treatments for chronic pain Trends Pharmacol Sci 31 153 160 1:CAS:528:DC%2BC3cXjvFKksbs%3D 20064669
    • (2010) Trends Pharmacol Sci , vol.31 , pp. 153-160
    • Chiechio, S.1    Copani, A.2    Zammataro, M.3    Battaglia, G.4    Gereau IV, R.W.5    Nicoletti, F.6
  • 212
    • 37449016478 scopus 로고    scopus 로고
    • Fluxing the mitochondria to insulin resistance
    • 1:CAS:528:DC%2BD1cXnsFSgug%3D%3D 18177719
    • MJ Watt AL Hevener 2008 Fluxing the mitochondria to insulin resistance Cell Metab 7 5 6 1:CAS:528:DC%2BD1cXnsFSgug%3D%3D 18177719
    • (2008) Cell Metab , vol.7 , pp. 5-6
    • Watt, M.J.1    Hevener, A.L.2
  • 213
    • 66749094133 scopus 로고    scopus 로고
    • Plasma acylcarnitine profiles suggest incomplete long-chain fatty acid beta-oxidation and altered tricarboxylic acid cycle activity in type 2 diabetic African-American women
    • 1:CAS:528:DC%2BD1MXhtlWrtrfN 19369366
    • SH Adams CL Hoppel KH Lok L Zhao SW Wong PE Minkler DH Hwang JW Newman WT Garvey 2009 Plasma acylcarnitine profiles suggest incomplete long-chain fatty acid beta-oxidation and altered tricarboxylic acid cycle activity in type 2 diabetic African-American women J Nutr 139 1073 1081 1:CAS:528: DC%2BD1MXhtlWrtrfN 19369366
    • (2009) J Nutr , vol.139 , pp. 1073-1081
    • Adams, S.H.1    Hoppel, C.L.2    Lok, K.H.3    Zhao, L.4    Wong, S.W.5    Minkler, P.E.6    Hwang, D.H.7    Newman, J.W.8    Garvey, W.T.9
  • 214
    • 34249724327 scopus 로고    scopus 로고
    • New insights concerning the role of carnitine in the regulation of fuel metabolism in skeletal muscle
    • 17331998
    • FB Stephens D Constantin-Teodosiu PL Greenhaff 2007 New insights concerning the role of carnitine in the regulation of fuel metabolism in skeletal muscle J Physiol 581 431 444 17331998
    • (2007) J Physiol , vol.581 , pp. 431-444
    • Stephens, F.B.1    Constantin-Teodosiu, D.2    Greenhaff, P.L.3
  • 215
    • 0035212367 scopus 로고    scopus 로고
    • L-carnitine changes the levels of insulin-like growth factors (IGFs) and IGF binding proteins in streptozotocin-induced diabetic rat
    • 1:CAS:528:DC%2BD3MXovVOktLk%3D
    • YR Heo CW Kang S Cha 2001 l-carnitine changes the levels of insulin-like growth factors (IGFs) and IGF binding proteins in streptozotocin-induced diabetic rat J Nutr Sci Vitaminol (Tokyo) 47 329 334 1:CAS:528: DC%2BD3MXovVOktLk%3D
    • (2001) J Nutr Sci Vitaminol (Tokyo) , vol.47 , pp. 329-334
    • Heo, Y.R.1    Kang, C.W.2    Cha, S.3
  • 216
    • 50549202600 scopus 로고
    • The glucose fatty-acid cycle. Its role in insulin sensitivity and the metabolic disturbances of diabetes mellitus
    • 1:STN:280:DyaF387ot1KhsQ%3D%3D 13990765
    • PJ Randle PB Garland CN Hales EA Newsholme 1963 The glucose fatty-acid cycle. Its role in insulin sensitivity and the metabolic disturbances of diabetes mellitus Lancet 1 785 789 1:STN:280:DyaF387ot1KhsQ%3D%3D 13990765
    • (1963) Lancet , vol.1 , pp. 785-789
    • Randle, P.J.1    Garland, P.B.2    Hales, C.N.3    Newsholme, E.A.4
  • 217
    • 33746468121 scopus 로고    scopus 로고
    • Acetyl-l-carnitine-induced up-regulation of heat shock proteins protects cortical neurons against amyloid-beta peptide 1-42-mediated oxidative stress and neurotoxicity: Implications for Alzheimer's disease
    • 1:CAS:528:DC%2BD28XnvFaiu7k%3D 16634066
    • HM Abdul V Calabrese M Calvani DA Butterfield 2006 Acetyl-l-carnitine- induced up-regulation of heat shock proteins protects cortical neurons against amyloid-beta peptide 1-42-mediated oxidative stress and neurotoxicity: implications for Alzheimer's disease J Neurosci Res 84 398 408 1:CAS:528:DC%2BD28XnvFaiu7k%3D 16634066
    • (2006) J Neurosci Res , vol.84 , pp. 398-408
    • Abdul, H.M.1    Calabrese, V.2    Calvani, M.3    Butterfield, D.A.4
  • 218
    • 77955891911 scopus 로고    scopus 로고
    • The epigenome and the mitochondrion: Bioenergetics and the environment
    • 1:CAS:528:DC%2BC3cXhtVeitrvO 20679390
    • DC Wallace 2010 The epigenome and the mitochondrion: bioenergetics and the environment Genes Dev 24 1571 1573 1:CAS:528:DC%2BC3cXhtVeitrvO 20679390
    • (2010) Genes Dev , vol.24 , pp. 1571-1573
    • Wallace, D.C.1
  • 220
    • 34548614520 scopus 로고    scopus 로고
    • Why do we still have a maternally inherited mitochondrial DNA? Insights from evolutionary medicine
    • 1:CAS:528:DC%2BD2sXhtVehtb3M 17506638
    • DC Wallace 2007 Why do we still have a maternally inherited mitochondrial DNA? Insights from evolutionary medicine Annu Rev Biochem 76 781 821 1:CAS:528:DC%2BD2sXhtVehtb3M 17506638
    • (2007) Annu Rev Biochem , vol.76 , pp. 781-821
    • Wallace, D.C.1
  • 221
    • 77953507107 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations in disease and aging
    • 1:CAS:528:DC%2BC3cXnsVWgtL8%3D 20544884
    • DC Wallace 2010 Mitochondrial DNA mutations in disease and aging Environ Mol Mutagen 51 440 450 1:CAS:528:DC%2BC3cXnsVWgtL8%3D 20544884
    • (2010) Environ Mol Mutagen , vol.51 , pp. 440-450
    • Wallace, D.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.