메뉴 건너뛰기




Volumn 39, Issue 3, 2012, Pages 256-264

Mitochondrial decay in ageing: 'Qi-invigorating' schisandrin B as a hormetic agent for mitigating age-related diseases

Author keywords

Glutathione anti oxidant response; Heat shock response; Hormesis; Mitochondria; Schisandrin B

Indexed keywords

ADENYLATE KINASE; CYTOCHROME P450; FORKHEAD TRANSCRIPTION FACTOR; HEAT SHOCK PROTEIN 25; HEAT SHOCK PROTEIN 70; HEAT SHOCK TRANSCRIPTION FACTOR 1; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LOW DENSITY LIPOPROTEIN; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; REACTIVE OXYGEN METABOLITE; SCHISANDRA CHINENSIS EXTRACT; SCHIZANDRIN B; SOMATOMEDIN C; TARGET OF RAPAMYCIN KINASE; TRANSCRIPTION FACTOR NRF2;

EID: 84857394665     PISSN: 03051870     EISSN: 14401681     Source Type: Journal    
DOI: 10.1111/j.1440-1681.2011.05600.x     Document Type: Article
Times cited : (15)

References (112)
  • 1
    • 0032434055 scopus 로고    scopus 로고
    • How and why we age
    • Hayflick L. How and why we age. Exp. Gerontol. 1998; 33: 639-53.
    • (1998) Exp. Gerontol. , vol.33 , pp. 639-653
    • Hayflick, L.1
  • 2
    • 77049308856 scopus 로고
    • Aging: A theory based on free radical and radiation chemistry
    • Harman D. Aging: A theory based on free radical and radiation chemistry. J. Gerontol. 1956; 11: 298-300.
    • (1956) J. Gerontol. , vol.11 , pp. 298-300
    • Harman, D.1
  • 3
    • 0015383617 scopus 로고
    • Free radical theory of aging: Dietary implications
    • Harman D. Free radical theory of aging: Dietary implications. Am. J. Clin. Nutr. 1972; 25: 839-43.
    • (1972) Am. J. Clin. Nutr. , vol.25 , pp. 839-843
    • Harman, D.1
  • 4
    • 0033369476 scopus 로고    scopus 로고
    • Mitochondrial oxygen radical generation and leak: Sites of production in states 4 and 3, organ specificity, and relation to aging and longevity
    • Barja G. Mitochondrial oxygen radical generation and leak: Sites of production in states 4 and 3, organ specificity, and relation to aging and longevity. J. Bioenerg. Biomembr. 1999; 31: 347-66.
    • (1999) J. Bioenerg. Biomembr. , vol.31 , pp. 347-366
    • Barja, G.1
  • 5
    • 0035872902 scopus 로고    scopus 로고
    • A reliable assessment of 8-oxo-2-deoxyguanosine levels in nuclear and mitochondrial DNA using the sodium iodide method to isolate DNA
    • Hamilton ML, Guo Z, Fuller CDet al.A reliable assessment of 8-oxo-2-deoxyguanosine levels in nuclear and mitochondrial DNA using the sodium iodide method to isolate DNA. Nucleic Acids Res. 2001; 29: 2117-26.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2117-2126
    • Hamilton, M.L.1    Guo, Z.2    Fuller, C.D.3
  • 6
    • 0032541401 scopus 로고    scopus 로고
    • The mtDNA-encoded ND6 subunit of mitochondrial NADH dehydrogenase is essential for the assembly of the membrane arm and respiratory function of the enzyme
    • Bai Y, Attardi G. The mtDNA-encoded ND6 subunit of mitochondrial NADH dehydrogenase is essential for the assembly of the membrane arm and respiratory function of the enzyme. EMBO J. 1998; 17: 4848-58.
    • (1998) EMBO J. , vol.17 , pp. 4848-4858
    • Bai, Y.1    Attardi, G.2
  • 7
    • 0023029883 scopus 로고
    • Cytochorome b is necessary for the effective processing of core protein I and the iron-sulfur protein of complex III in the mitochondria
    • Sen K, Beattie DS. Cytochorome b is necessary for the effective processing of core protein I and the iron-sulfur protein of complex III in the mitochondria. Arch. Biochem. Biophys. 1986; 251: 239-49.
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 239-249
    • Sen, K.1    Beattie, D.S.2
  • 8
    • 0036236939 scopus 로고    scopus 로고
    • The reductive hotspot hypothesis of mammalian aging: Membrane metabolism magnifies mutant mitochondrial mischief
    • de Grey ADNJ. The reductive hotspot hypothesis of mammalian aging: Membrane metabolism magnifies mutant mitochondrial mischief. Eur. J. Biochem. 2002; 269: 2003-9.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2003-2009
    • de Grey, A.D.N.J.1
  • 9
    • 0038010637 scopus 로고    scopus 로고
    • A hypothesis for the minimal overall structure of the mammalian plasma membrane redox system
    • de Grey ADNJ. A hypothesis for the minimal overall structure of the mammalian plasma membrane redox system. Protoplasma 2003; 221: 3-9.
    • (2003) Protoplasma , vol.221 , pp. 3-9
    • de Grey, A.D.N.J.1
  • 10
    • 0030799043 scopus 로고    scopus 로고
    • Low density lipoprotein oxidation and its pathobiological significance
    • Steinberg D. Low density lipoprotein oxidation and its pathobiological significance. J. Biol. Chem. 1997; 272: 20963-6.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20963-20966
    • Steinberg, D.1
  • 11
    • 0027990590 scopus 로고
    • Toxicity of mildly modified low-density lipoproteins to cultured retinal capillary endothelial cells and pericytes
    • Lyons TJ, Li W, Wells-Knecht MC, Jokl R. Toxicity of mildly modified low-density lipoproteins to cultured retinal capillary endothelial cells and pericytes. Diabetes 1994; 43: 1090-5.
    • (1994) Diabetes , vol.43 , pp. 1090-1095
    • Lyons, T.J.1    Li, W.2    Wells-Knecht, M.C.3    Jokl, R.4
  • 14
    • 66149135335 scopus 로고    scopus 로고
    • Reversal of the mitochondrial phenotype and slow development of oxidative biomarkers of aging in long-lived Mclk1+/- mice
    • Lapointe J, Stepanyan Z, Bigras E, Hekimi S. Reversal of the mitochondrial phenotype and slow development of oxidative biomarkers of aging in long-lived Mclk1+/- mice. J. Biol. Chem. 2009; 284: 20364-74.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20364-20374
    • Lapointe, J.1    Stepanyan, Z.2    Bigras, E.3    Hekimi, S.4
  • 15
    • 54449091329 scopus 로고    scopus 로고
    • Early mitochondrial dysfunction in long-lived Mclk1+/- mice
    • Lapointe J, Hekimi S. Early mitochondrial dysfunction in long-lived Mclk1+/- mice. J. Biol. Chem. 2008; 283: 26217-27.
    • (2008) J. Biol. Chem. , vol.283 , pp. 26217-26227
    • Lapointe, J.1    Hekimi, S.2
  • 16
    • 77952548782 scopus 로고    scopus 로고
    • How increased oxidative stress promotes longevity and metabolic health: The concept of mitochondrial hormesis (mitohormesis)
    • Ristow M, Zarse K. How increased oxidative stress promotes longevity and metabolic health: The concept of mitochondrial hormesis (mitohormesis). Exp. Gerontol. 2010; 45: 410-8.
    • (2010) Exp. Gerontol. , vol.45 , pp. 410-418
    • Ristow, M.1    Zarse, K.2
  • 17
    • 77953357982 scopus 로고    scopus 로고
    • Impaired quality control of mitochondria: Aging from a new perspective
    • Weber TA, Reichert AS. Impaired quality control of mitochondria: Aging from a new perspective. Exp. Gerontol. 2010; 45: 503-11.
    • (2010) Exp. Gerontol. , vol.45 , pp. 503-511
    • Weber, T.A.1    Reichert, A.S.2
  • 18
    • 38849156952 scopus 로고    scopus 로고
    • Heart mitochondria: Gates of life and death
    • Gustafsson AB, Gottlieb RA. Heart mitochondria: Gates of life and death. Cardiovasc. Res. 2008; 77: 334-43.
    • (2008) Cardiovasc. Res. , vol.77 , pp. 334-343
    • Gustafsson, A.B.1    Gottlieb, R.A.2
  • 19
    • 34948881208 scopus 로고    scopus 로고
    • Mitochondria: A hub of redox activities and cellular distress
    • Kakkar P, Singh BK. Mitochondria: A hub of redox activities and cellular distress. Mol. Cell. Biochem. 2007; 305: 235-53.
    • (2007) Mol. Cell. Biochem. , vol.305 , pp. 235-253
    • Kakkar, P.1    Singh, B.K.2
  • 21
    • 0034705129 scopus 로고    scopus 로고
    • The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases
    • Landry J, Sutton A, Tafrov ST et al. The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases. Proc. Natl Acad. Sci. USA 2000; 97: 5807-11.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 5807-5811
    • Landry, J.1    Sutton, A.2    Tafrov, S.T.3
  • 22
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • Kaeberlein M, McVey M, Guarente L. The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev. 1999; 13: 2570-80.
    • (1999) Genes Dev. , vol.13 , pp. 2570-2580
    • Kaeberlein, M.1    McVey, M.2    Guarente, L.3
  • 23
    • 0035826271 scopus 로고    scopus 로고
    • Increaased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • Tissenbaum HA, Guarente L. Increaased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature 2001; 410: 227-30.
    • (2001) Nature , vol.410 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 24
    • 3943071801 scopus 로고    scopus 로고
    • Sirtuin activators mimic caloric restriction and delay ageing in metazoans
    • Wood JG, Rogina B, Lavu S et al. Sirtuin activators mimic caloric restriction and delay ageing in metazoans. Nature 2004; 430: 686-9.
    • (2004) Nature , vol.430 , pp. 686-689
    • Wood, J.G.1    Rogina, B.2    Lavu, S.3
  • 25
    • 33845868198 scopus 로고    scopus 로고
    • Sirtuin as potential targets for metabolic syndrome
    • Guarente L. Sirtuin as potential targets for metabolic syndrome. Nature 2006; 444: 868-74.
    • (2006) Nature , vol.444 , pp. 868-874
    • Guarente, L.1
  • 26
    • 0347128279 scopus 로고    scopus 로고
    • Calorie restriction extends yeast life span by lowering the level of NADH
    • Lin SJ, Ford E, Haigis M, Liszt G, Guarente L. Calorie restriction extends yeast life span by lowering the level of NADH. Genes Dev. 2004; 18: 12-6.
    • (2004) Genes Dev. , vol.18 , pp. 12-16
    • Lin, S.J.1    Ford, E.2    Haigis, M.3    Liszt, G.4    Guarente, L.5
  • 27
    • 3142740860 scopus 로고    scopus 로고
    • Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
    • Cohen HY, Miller C, Bitterman KG et al. Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase. Science 2004; 305: 390-2.
    • (2004) Science , vol.305 , pp. 390-392
    • Cohen, H.Y.1    Miller, C.2    Bitterman, K.G.3
  • 28
    • 1542373685 scopus 로고    scopus 로고
    • Transcriptional regulatory circuits controlling mitochondrial biogenesis and function
    • Kelly DP, Scarpulla RC. Transcriptional regulatory circuits controlling mitochondrial biogenesis and function. Gene Dev. 2004; 18: 357-68.
    • (2004) Gene Dev. , vol.18 , pp. 357-368
    • Kelly, D.P.1    Scarpulla, R.C.2
  • 29
    • 5344247243 scopus 로고    scopus 로고
    • PGC-1alpha: Turbocharging mitochondria
    • Houten SM, Auwerx J. PGC-1alpha: Turbocharging mitochondria. Cell 2004; 119: 5-7.
    • (2004) Cell , vol.119 , pp. 5-7
    • Houten, S.M.1    Auwerx, J.2
  • 30
    • 68149137896 scopus 로고    scopus 로고
    • Implications of mitochondrial DNA mutations and mitochondrial dysfunction in tumorigenesis
    • Lu J, Sharma LK, Bai Y. Implications of mitochondrial DNA mutations and mitochondrial dysfunction in tumorigenesis. Cell Res. 2009; 19: 802-15.
    • (2009) Cell Res. , vol.19 , pp. 802-815
    • Lu, J.1    Sharma, L.K.2    Bai, Y.3
  • 31
    • 0030761388 scopus 로고    scopus 로고
    • Dihydroorotatubiquinone oxidoreductase links mitochondria in the biosynthesis of pyrimidine nucleotides
    • Loffler M, Jockel J, Schuster G, Becker C. Dihydroorotatubiquinone oxidoreductase links mitochondria in the biosynthesis of pyrimidine nucleotides. Mol. Cell. Biochem. 1997; 174: 125-9.
    • (1997) Mol. Cell. Biochem. , vol.174 , pp. 125-129
    • Loffler, M.1    Jockel, J.2    Schuster, G.3    Becker, C.4
  • 32
    • 0028143584 scopus 로고
    • Physiological concentrations of purines and pyrimidines
    • Traut TW. Physiological concentrations of purines and pyrimidines. Mol. Cell. Biochem. 1994; 140: 1-22.
    • (1994) Mol. Cell. Biochem. , vol.140 , pp. 1-22
    • Traut, T.W.1
  • 33
    • 0024505072 scopus 로고
    • The molecular basis of mutations induced by deoxyribonucleoside triphosphate pool imbalances in mammalian cells
    • Meuth M. The molecular basis of mutations induced by deoxyribonucleoside triphosphate pool imbalances in mammalian cells. Exp. Cell Res. 1989; 181: 305-16.
    • (1989) Exp. Cell Res. , vol.181 , pp. 305-316
    • Meuth, M.1
  • 35
    • 0026093495 scopus 로고
    • An overview of the relationship between oxidative stress and chemical carcinogenesis
    • Trush MA, Kensler TW. An overview of the relationship between oxidative stress and chemical carcinogenesis. Free Radic. Biol. Med. 1991; 10: 201-9.
    • (1991) Free Radic. Biol. Med. , vol.10 , pp. 201-209
    • Trush, M.A.1    Kensler, T.W.2
  • 36
    • 23744471140 scopus 로고    scopus 로고
    • Mitochondria and ischemia/reperfusion injury
    • Honda HM, Korge P, Weiss JN. Mitochondria and ischemia/reperfusion injury. Ann. NY Acad. Sci. 2005; 1047: 248-58.
    • (2005) Ann. NY Acad. Sci. , vol.1047 , pp. 248-258
    • Honda, H.M.1    Korge, P.2    Weiss, J.N.3
  • 37
    • 33644877068 scopus 로고    scopus 로고
    • Nitric oxide and oxidative stress in cardiovascular aging
    • online). Available from
    • Raju SV, Barouch LA, Hare JM. Nitric oxide and oxidative stress in cardiovascular aging. Sci. Aging Knowledge Environ. 2005; 2005 (online). Available from:.
    • (2005) Sci. Aging Knowledge Environ. , vol.2005
    • Raju, S.V.1    Barouch, L.A.2    Hare, J.M.3
  • 38
    • 80051541139 scopus 로고    scopus 로고
    • Regulatory role of mitochondria in oxidative stress and atherosclerosis
    • Chang J, Kou S, Lin W, Liu C. Regulatory role of mitochondria in oxidative stress and atherosclerosis. World J. Cardiol. 2010; 2: 150-9.
    • (2010) World J. Cardiol. , vol.2 , pp. 150-159
    • Chang, J.1    Kou, S.2    Lin, W.3    Liu, C.4
  • 41
    • 33646948530 scopus 로고    scopus 로고
    • Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled
    • Keeney PM, Xie J, Capaldi RA, Bennett JP Jr. Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled. J. Neurosci. 2006; 26: 5256-64.
    • (2006) J. Neurosci. , vol.26 , pp. 5256-5264
    • Keeney, P.M.1    Xie, J.2    Capaldi, R.A.3    Bennett Jr., J.P.4
  • 42
  • 43
    • 0035500510 scopus 로고    scopus 로고
    • Amyloid-beta: An antioxidant that becomes a prooxidant and critically contributes to Alzheimer's diseases
    • Kontush A. Amyloid-beta: An antioxidant that becomes a prooxidant and critically contributes to Alzheimer's diseases. Free Radic. Biol. Med. 2001; 31: 1120-31.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 1120-1131
    • Kontush, A.1
  • 44
    • 70449411818 scopus 로고    scopus 로고
    • Oxidatively modified, mitochondria-relevant brain proteins in subjects with Alzheimer disease and mild cognitive impairment
    • Sultana R, Butterfield DA. Oxidatively modified, mitochondria-relevant brain proteins in subjects with Alzheimer disease and mild cognitive impairment. J. Bioenerg. Biomembr. 2009; 41: 441-6.
    • (2009) J. Bioenerg. Biomembr. , vol.41 , pp. 441-446
    • Sultana, R.1    Butterfield, D.A.2
  • 45
    • 0020685951 scopus 로고
    • Decreased pyruvate dehydrogenase complex activity in Huntington and Alzheimer brain
    • Sorbi S, Bird ED, Blass JP. Decreased pyruvate dehydrogenase complex activity in Huntington and Alzheimer brain. Ann. Neurol. 1983; 13: 72-8.
    • (1983) Ann. Neurol. , vol.13 , pp. 72-78
    • Sorbi, S.1    Bird, E.D.2    Blass, J.P.3
  • 46
    • 0026718966 scopus 로고
    • Brain cytochrome oxidase in Alzheimer's disease
    • Kish SJ, Bergeron C, Rajput A et al. Brain cytochrome oxidase in Alzheimer's disease. J. Neurochem. 1992; 59: 776-9.
    • (1992) J. Neurochem. , vol.59 , pp. 776-779
    • Kish, S.J.1    Bergeron, C.2    Rajput, A.3
  • 47
    • 36248988467 scopus 로고    scopus 로고
    • Insights into amyloid-beta-induced mitochondrial dysfunction in Alzheimer disease
    • Wang X, Su B, Perry G, Smith MA, Zhu X. Insights into amyloid-beta-induced mitochondrial dysfunction in Alzheimer disease. Free Radic. Biol. Med. 2007; 43: 1569-73.
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 1569-1573
    • Wang, X.1    Su, B.2    Perry, G.3    Smith, M.A.4    Zhu, X.5
  • 50
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct
    • Conway KA, Rochet JC, Bieganski RM, Lansbury PT Jr. Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct. Science 2001; 294: 1346-9.
    • (2001) Science , vol.294 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.C.2    Bieganski, R.M.3    Lansbury Jr., P.T.4
  • 51
    • 44049099669 scopus 로고    scopus 로고
    • Mitochondrial import and accumulation of alpha-synuclein impair complex I in human dopamineric neuronal cultures and Parkinson disase brain
    • Devi L, Raghavendran V, Prabhu BM, Avadhani NG, Anadatheerthavarada HK. Mitochondrial import and accumulation of alpha-synuclein impair complex I in human dopamineric neuronal cultures and Parkinson disase brain. J. Biol. Chem. 2008; 283: 9089-100.
    • (2008) J. Biol. Chem. , vol.283 , pp. 9089-9100
    • Devi, L.1    Raghavendran, V.2    Prabhu, B.M.3    Avadhani, N.G.4    Anadatheerthavarada, H.K.5
  • 52
    • 0036415838 scopus 로고    scopus 로고
    • Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils
    • Lashuel HA, Petre BM, Wall J et al. Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. J. Mol. Biol. 2002; 322: 1089-102.
    • (2002) J. Mol. Biol. , vol.322 , pp. 1089-1102
    • Lashuel, H.A.1    Petre, B.M.2    Wall, J.3
  • 53
    • 29644434199 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity
    • Smith WW, Jiang H, Pei Z et al. Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity. Hum. Mol. Genet. 2005; 14: 3801-11.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 3801-3811
    • Smith, W.W.1    Jiang, H.2    Pei, Z.3
  • 55
    • 23244458906 scopus 로고    scopus 로고
    • The exicitoprotective effect of N-methyl-d-aspartate receptors is mediated by a brain-derived neurotrophic factor autocrine loop in cultured hippocampal neurons
    • Jian X, Tian F, Mearow K, Okagaki P, Lipsky RH, Marini AM. The exicitoprotective effect of N-methyl-d-aspartate receptors is mediated by a brain-derived neurotrophic factor autocrine loop in cultured hippocampal neurons. J. Neurochem. 2005; 94: 713-22.
    • (2005) J. Neurochem. , vol.94 , pp. 713-722
    • Jian, X.1    Tian, F.2    Mearow, K.3    Okagaki, P.4    Lipsky, R.H.5    Marini, A.M.6
  • 56
    • 31844439407 scopus 로고    scopus 로고
    • Sublethal mitochondrial stress with an attendant stoichiometric augmentation of reactive oxygen species may precipitate many of the beneficial alterations in cellular physiology produced by caloric restriction, intermittent fasting, exercise and dietary phytonutrients. 'Mitohormesis' for health and vitality
    • Tapia PC. Sublethal mitochondrial stress with an attendant stoichiometric augmentation of reactive oxygen species may precipitate many of the beneficial alterations in cellular physiology produced by caloric restriction, intermittent fasting, exercise and dietary phytonutrients. 'Mitohormesis' for health and vitality. Med. Hypotheses 2006; 66: 832-43.
    • (2006) Med. Hypotheses , vol.66 , pp. 832-843
    • Tapia, P.C.1
  • 57
    • 77952543118 scopus 로고    scopus 로고
    • Mitochondrial redox metabolism: Aging, longevity and dietary effects
    • Page MM, Robb EL, Salway KD, Stuart JA. Mitochondrial redox metabolism: Aging, longevity and dietary effects. Mech. Ageing Dev. 2010; 131: 242-52.
    • (2010) Mech. Ageing Dev. , vol.131 , pp. 242-252
    • Page, M.M.1    Robb, E.L.2    Salway, K.D.3    Stuart, J.A.4
  • 58
    • 41549135942 scopus 로고    scopus 로고
    • FoxO transcription factors in the maintenance of cellular homeostasis during aging
    • Salih DA, Brunet A. FoxO transcription factors in the maintenance of cellular homeostasis during aging. Curr. Opin. Cell Biol. 2008; 20: 126-36.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 126-136
    • Salih, D.A.1    Brunet, A.2
  • 59
    • 78649635403 scopus 로고    scopus 로고
    • Nrf2, a guardian of healthspan and gatekeeper of species longevity
    • Lewis KN, Mele J, Hayes JD, Buffenstein R. Nrf2, a guardian of healthspan and gatekeeper of species longevity. Integr. Comp. Biol. 2010; 50: 829-43.
    • (2010) Integr. Comp. Biol. , vol.50 , pp. 829-843
    • Lewis, K.N.1    Mele, J.2    Hayes, J.D.3    Buffenstein, R.4
  • 60
    • 79951787452 scopus 로고    scopus 로고
    • Lifespan extension induced by AMPK and calcineurin is mediated by CRTC-1 and CREB
    • Mair W, Morantte I, Rodrigues AP et al. Lifespan extension induced by AMPK and calcineurin is mediated by CRTC-1 and CREB. Nature 2011; 470: 404-8.
    • (2011) Nature , vol.470 , pp. 404-408
    • Mair, W.1    Morantte, I.2    Rodrigues, A.P.3
  • 63
    • 33750909999 scopus 로고    scopus 로고
    • Reactive oxygen species-induced activation of the MAP kinase signaling pathways
    • McCubrey JA, Lahair MM, Franklin RA. Reactive oxygen species-induced activation of the MAP kinase signaling pathways. Antioxid. Redox Signal. 2006; 8: 1775-89.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 1775-1789
    • McCubrey, J.A.1    Lahair, M.M.2    Franklin, R.A.3
  • 64
    • 0142043984 scopus 로고    scopus 로고
    • Redox signaling and the MAP kinase pathways
    • Torres M, Forman HJ. Redox signaling and the MAP kinase pathways. Biofactors 2003; 17: 287-96.
    • (2003) Biofactors , vol.17 , pp. 287-296
    • Torres, M.1    Forman, H.J.2
  • 65
    • 0037032817 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases
    • Johnson GL, Lapadat R. Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases. Science 2002; 298: 1911-2.
    • (2002) Science , vol.298 , pp. 1911-1912
    • Johnson, G.L.1    Lapadat, R.2
  • 67
    • 21444439970 scopus 로고    scopus 로고
    • Phosphorylation of c-Fos by members of the p38 MAPK family. Role in the AP-1 response to UV light
    • Tanos T, Marinissen MJ, Leskow FC et al. Phosphorylation of c-Fos by members of the p38 MAPK family. Role in the AP-1 response to UV light. J. Biol. Chem. 2005; 280: 18842-52.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18842-18852
    • Tanos, T.1    Marinissen, M.J.2    Leskow, F.C.3
  • 68
    • 40049088820 scopus 로고    scopus 로고
    • The Nrf2-Keap1 defence pathway: Role in protection against drug-induced toxicity
    • Copple IM, Goldring CE, Kitteringham NR, Park BK. The Nrf2-Keap1 defence pathway: Role in protection against drug-induced toxicity. Toxicology 2008; 246: 24-33.
    • (2008) Toxicology , vol.246 , pp. 24-33
    • Copple, I.M.1    Goldring, C.E.2    Kitteringham, N.R.3    Park, B.K.4
  • 69
    • 33748358379 scopus 로고    scopus 로고
    • Mechanism of action of isothiocyanates: The induction of ARE-regulated genes is associated with activation of ERK and JNK and the phosphorylation and nuclear translocation of Nrf2
    • Xu C, Yuan X, Pan Z et al. Mechanism of action of isothiocyanates: The induction of ARE-regulated genes is associated with activation of ERK and JNK and the phosphorylation and nuclear translocation of Nrf2. Mol. Cancer Ther. 2006; 5: 1918-26.
    • (2006) Mol. Cancer Ther. , vol.5 , pp. 1918-1926
    • Xu, C.1    Yuan, X.2    Pan, Z.3
  • 70
    • 67649402187 scopus 로고    scopus 로고
    • The Nrf2-antioxidant response element signaling pathway and its activation by oxidative stress
    • Nguyen T, Nioi P, Pickett CB. The Nrf2-antioxidant response element signaling pathway and its activation by oxidative stress. J. Biol. Chem. 2009; 284: 13291-5.
    • (2009) J. Biol. Chem. , vol.284 , pp. 13291-13295
    • Nguyen, T.1    Nioi, P.2    Pickett, C.B.3
  • 72
    • 12344305246 scopus 로고    scopus 로고
    • Glutathione metabolism in long-living Ames dwarf mice
    • Brown-Borg HM, Rakoczy SG. Glutathione metabolism in long-living Ames dwarf mice. Exp. Gerontol. 2005; 40: 115-20.
    • (2005) Exp. Gerontol. , vol.40 , pp. 115-120
    • Brown-Borg, H.M.1    Rakoczy, S.G.2
  • 73
    • 3542995049 scopus 로고    scopus 로고
    • Stress-inducible responses and heat shock proteins: New pharmacologic targets for cytoprotection
    • Morimoto RI, Santoro MG. Stress-inducible responses and heat shock proteins: New pharmacologic targets for cytoprotection. Nat. Biotechnol. 1998; 16: 833-8.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 833-838
    • Morimoto, R.I.1    Santoro, M.G.2
  • 74
    • 0031031148 scopus 로고    scopus 로고
    • Nitric oxide protects cultured rat hepatocytes from tumor necrosis factor-alpha-induced apoptosis by inducing heat shock protein 70 expression
    • Kim YM, de Vera ME, Watkins SC, Billiar TR. Nitric oxide protects cultured rat hepatocytes from tumor necrosis factor-alpha-induced apoptosis by inducing heat shock protein 70 expression. J. Biol. Chem. 1997; 272: 1402-11.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1402-1411
    • Kim, Y.M.1    de Vera, M.E.2    Watkins, S.C.3    Billiar, T.R.4
  • 75
    • 0031962486 scopus 로고    scopus 로고
    • Small stress proteins: Chaperones that act as regulators of intracellular redox state and programmed cell death
    • Arrigo AP. Small stress proteins: Chaperones that act as regulators of intracellular redox state and programmed cell death. Biol. Chem. 1998; 379: 19-26.
    • (1998) Biol. Chem. , vol.379 , pp. 19-26
    • Arrigo, A.P.1
  • 76
    • 0345410965 scopus 로고    scopus 로고
    • Mammalian small stress proteins protect against oxidative stress through their ability to increase glucose-6-phosphate dehdrogenase activity and by maintaining optimal cellular detoxifying machinery
    • Preville X, Salvemini F, Giraud S et al. Mammalian small stress proteins protect against oxidative stress through their ability to increase glucose-6-phosphate dehdrogenase activity and by maintaining optimal cellular detoxifying machinery. Exp. Cell Res. 1999; 247: 61-78.
    • (1999) Exp. Cell Res. , vol.247 , pp. 61-78
    • Preville, X.1    Salvemini, F.2    Giraud, S.3
  • 78
    • 25844494542 scopus 로고    scopus 로고
    • Sick chaperones, cellular stress, and disease
    • Macario AJ, Conway de Macario E. Sick chaperones, cellular stress, and disease. N. Engl. J. Med. 2005; 353: 1489-501.
    • (2005) N. Engl. J. Med. , vol.353 , pp. 1489-1501
    • Macario, A.J.1    Conway de Macario, E.2
  • 79
    • 57749195944 scopus 로고    scopus 로고
    • Insulin exhibits short-term anti-inflammatory but long-term proinflammatory effects in vitro
    • Iwasaki Y, Nishiyama M, Tagucchi T et al. Insulin exhibits short-term anti-inflammatory but long-term proinflammatory effects in vitro. Mol. Cell. Endocrinol. 2009; 298: 25-32.
    • (2009) Mol. Cell. Endocrinol. , vol.298 , pp. 25-32
    • Iwasaki, Y.1    Nishiyama, M.2    Tagucchi, T.3
  • 80
    • 40949123149 scopus 로고    scopus 로고
    • Activation of innate immunity system during aging: NF-kB signaling is the molecular culprit of inflamm-aging
    • Salminen A, Huuskonen J, Ojala J, Kauppinen A, Kaarniranta K, Suuronen T. Activation of innate immunity system during aging: NF-kB signaling is the molecular culprit of inflamm-aging. Ageing Res. Rev. 2008; 7: 83-105.
    • (2008) Ageing Res. Rev. , vol.7 , pp. 83-105
    • Salminen, A.1    Huuskonen, J.2    Ojala, J.3    Kauppinen, A.4    Kaarniranta, K.5    Suuronen, T.6
  • 81
    • 65549139675 scopus 로고    scopus 로고
    • Regulation of the aging process by autophagy
    • Salminen A, Kaarniranta K. Regulation of the aging process by autophagy. Trends Mol. Med. 2009; 15: 217-24.
    • (2009) Trends Mol. Med. , vol.15 , pp. 217-224
    • Salminen, A.1    Kaarniranta, K.2
  • 82
    • 74449090245 scopus 로고    scopus 로고
    • Insulin/IGF-1 paradox of aging: Regulation via AKT/IKK/NF-κB signaling
    • Salminen A, Kaarniranta K. Insulin/IGF-1 paradox of aging: Regulation via AKT/IKK/NF-κB signaling. Cell. Signal. 2010; 22: 573-7.
    • (2010) Cell. Signal. , vol.22 , pp. 573-577
    • Salminen, A.1    Kaarniranta, K.2
  • 83
    • 79951912532 scopus 로고    scopus 로고
    • Four faces of cellular senescence
    • Rodier F, Campisi J. Four faces of cellular senescence. J. Cell Biol. 2011; 192: 547-56.
    • (2011) J. Cell Biol. , vol.192 , pp. 547-556
    • Rodier, F.1    Campisi, J.2
  • 84
    • 43049084732 scopus 로고    scopus 로고
    • 2+-induced mitochondrial permeability transition and mitochondrial membrane potential in H9c2 cardiomyocytes
    • 2+-induced mitochondrial permeability transition and mitochondrial membrane potential in H9c2 cardiomyocytes. Life Sci. 2008; 82: 1092-101.
    • (2008) Life Sci. , vol.82 , pp. 1092-1101
    • Chiu, P.Y.1    Luk, K.F.2    Leung, H.Y.3    Ng, K.M.4    Ko, K.M.5
  • 85
    • 33645047393 scopus 로고    scopus 로고
    • Biochemical basis of the 'Qi-invigorating' action of Schisandra berry (Wu-Wei-Zi) in Chinese medicine
    • Ko KM, Chiu PY. Biochemical basis of the 'Qi-invigorating' action of Schisandra berry (Wu-Wei-Zi) in Chinese medicine. Am. J. Chin. Med. 2006; 34: 171-6.
    • (2006) Am. J. Chin. Med. , vol.34 , pp. 171-176
    • Ko, K.M.1    Chiu, P.Y.2
  • 86
    • 33747319849 scopus 로고    scopus 로고
    • Chronic schisandrin B treatment improves mitochondrial antioxidant status and tissue heat shock protein production in various tissues of young adult and middle-aged rats
    • Chiu PY, Leung HY, Poon MK, Ko KM. Chronic schisandrin B treatment improves mitochondrial antioxidant status and tissue heat shock protein production in various tissues of young adult and middle-aged rats. Biogerontology 2006; 7: 199-210.
    • (2006) Biogerontology , vol.7 , pp. 199-210
    • Chiu, P.Y.1    Leung, H.Y.2    Poon, M.K.3    Ko, K.M.4
  • 87
    • 33744815331 scopus 로고    scopus 로고
    • Effects of schisandrin B enantiomers on cellular glutathione and menadione toxicity in AML12 hepatocytes
    • Chiu PY, Leung HY, Poon MK, Mak DH, Ko KM. Effects of schisandrin B enantiomers on cellular glutathione and menadione toxicity in AML12 hepatocytes. Pharmacology 2006; 77: 63-70.
    • (2006) Pharmacology , vol.77 , pp. 63-70
    • Chiu, P.Y.1    Leung, H.Y.2    Poon, M.K.3    Mak, D.H.4    Ko, K.M.5
  • 88
    • 4644289319 scopus 로고    scopus 로고
    • Down-modulation of heat shock protein 70 and up-modulation of caspase-3 during schisandrin B-induced apoptosis in human hepatoma SMMC-7721 cells
    • Wu YF, Cao MF, Gao YP et al. Down-modulation of heat shock protein 70 and up-modulation of caspase-3 during schisandrin B-induced apoptosis in human hepatoma SMMC-7721 cells. World J. Gastroenterol. 2004; 10: 2944-8.
    • (2004) World J. Gastroenterol. , vol.10 , pp. 2944-2948
    • Wu, Y.F.1    Cao, M.F.2    Gao, Y.P.3
  • 90
    • 0036715310 scopus 로고    scopus 로고
    • Schisandrin B protects against tert-butylhydroperoxide induced cerebral toxicity by enhancing glutathione antioxidant status in mouse brain
    • Ko KM, Lam BY. Schisandrin B protects against tert-butylhydroperoxide induced cerebral toxicity by enhancing glutathione antioxidant status in mouse brain. Mol. Cell. Biochem. 2002; 238: 181-6.
    • (2002) Mol. Cell. Biochem. , vol.238 , pp. 181-186
    • Ko, K.M.1    Lam, B.Y.2
  • 91
    • 76449098446 scopus 로고    scopus 로고
    • Long-term schisandrin B treatment mitigates age-related impairments in mitochondrial antioxidant status and functional ability in various tissues, and improves the survival of aging C57BL/6J mice
    • Ko KM, Chen N, Leung HY, Leong EP, Poon MK, Chiu PY. Long-term schisandrin B treatment mitigates age-related impairments in mitochondrial antioxidant status and functional ability in various tissues, and improves the survival of aging C57BL/6J mice. Biofactors 2008; 34: 331-42.
    • (2008) Biofactors , vol.34 , pp. 331-342
    • Ko, K.M.1    Chen, N.2    Leung, H.Y.3    Leong, E.P.4    Poon, M.K.5    Chiu, P.Y.6
  • 92
    • 46449093978 scopus 로고    scopus 로고
    • Schisandrin B enhances cerebral mitochondrial antioxidant status and structural integrity, and protects against cerebral ischemia/reperfusion injury in rats
    • Chen N, Chiu PY, Ko KM. Schisandrin B enhances cerebral mitochondrial antioxidant status and structural integrity, and protects against cerebral ischemia/reperfusion injury in rats. Biol. Pharm. Bull. 2008; 31: 1387-91.
    • (2008) Biol. Pharm. Bull. , vol.31 , pp. 1387-1391
    • Chen, N.1    Chiu, P.Y.2    Ko, K.M.3
  • 93
    • 0347286640 scopus 로고    scopus 로고
    • Time-dependent enhancement in mitochondrial glutathione status and ATP generation capacity by schisandrin B treatment decreases the susceptibility of rat hearts to ischemia-reperfusion injury
    • Chiu PY, Ko KM. Time-dependent enhancement in mitochondrial glutathione status and ATP generation capacity by schisandrin B treatment decreases the susceptibility of rat hearts to ischemia-reperfusion injury. Biofactors 2003; 19: 43-51.
    • (2003) Biofactors , vol.19 , pp. 43-51
    • Chiu, P.Y.1    Ko, K.M.2
  • 94
    • 41849109537 scopus 로고    scopus 로고
    • Schisandrin B enhances renal mitochondrial antioxidant status, functional and structural integrity, and protects against gentamicin-induced nephrotoxicity in rats
    • Chiu PY, Leung HY, Ko KM. Schisandrin B enhances renal mitochondrial antioxidant status, functional and structural integrity, and protects against gentamicin-induced nephrotoxicity in rats. Biol. Pharm. Bull. 2008; 31: 602-5.
    • (2008) Biol. Pharm. Bull. , vol.31 , pp. 602-605
    • Chiu, P.Y.1    Leung, H.Y.2    Ko, K.M.3
  • 95
    • 0142011656 scopus 로고    scopus 로고
    • Hepatoprotective mechanism of schisandrin B. Role of mitochondrial glutathione antioxidant status and heat shock proteins
    • Chiu PY, Tang MH, Mak DH, Poon MK, Ko KM. Hepatoprotective mechanism of schisandrin B. Role of mitochondrial glutathione antioxidant status and heat shock proteins. Free Radic. Biol. Med. 2003; 35: 368-80.
    • (2003) Free Radic. Biol. Med. , vol.35 , pp. 368-380
    • Chiu, P.Y.1    Tang, M.H.2    Mak, D.H.3    Poon, M.K.4    Ko, K.M.5
  • 96
    • 79951674293 scopus 로고    scopus 로고
    • Schisandrin B protects against solar irradiation-induced oxidative stress in rat skin tissue
    • Lam PY, Yan CW, Chiu PY, Leung HY, Ko KM. Schisandrin B protects against solar irradiation-induced oxidative stress in rat skin tissue. Fitoterapia 2011; 82: 393-400.
    • (2011) Fitoterapia , vol.82 , pp. 393-400
    • Lam, P.Y.1    Yan, C.W.2    Chiu, P.Y.3    Leung, H.Y.4    Ko, K.M.5
  • 97
    • 34250018342 scopus 로고    scopus 로고
    • Schisandrin B decreases the sensitivity of mitochondria to calcium ion-induced permeability transition and protects against carbon tetrachloride toxicity in mouse livers
    • Chiu PY, Leung HY, Siu AH, Poon MK, Ko KM. Schisandrin B decreases the sensitivity of mitochondria to calcium ion-induced permeability transition and protects against carbon tetrachloride toxicity in mouse livers. Biol. Pharm. Bull. 2007; 30: 1108-12.
    • (2007) Biol. Pharm. Bull. , vol.30 , pp. 1108-1112
    • Chiu, P.Y.1    Leung, H.Y.2    Siu, A.H.3    Poon, M.K.4    Ko, K.M.5
  • 98
    • 34848924275 scopus 로고    scopus 로고
    • Schisandrin B decreases the sensitivity of mitochondria to calcium ion-induced permeability transition and protects against ischemia-reperfusion injury in rat hearts
    • Chiu PY, Leung HY, Siu AH, Poon MK, Ko KM. Schisandrin B decreases the sensitivity of mitochondria to calcium ion-induced permeability transition and protects against ischemia-reperfusion injury in rat hearts. Acta Pharmacol. Sin. 2007; 28: 1559-65.
    • (2007) Acta Pharmacol. Sin. , vol.28 , pp. 1559-1565
    • Chiu, P.Y.1    Leung, H.Y.2    Siu, A.H.3    Poon, M.K.4    Ko, K.M.5
  • 99
    • 70349251736 scopus 로고    scopus 로고
    • Schisandrin B protects rat cortical neurons against Abeta1-42-induced neurotoxicity
    • Wang B, Wang XM. Schisandrin B protects rat cortical neurons against Abeta1-42-induced neurotoxicity. Pharmazie 2009; 64: 450-4.
    • (2009) Pharmazie , vol.64 , pp. 450-454
    • Wang, B.1    Wang, X.M.2
  • 100
    • 79951662032 scopus 로고    scopus 로고
    • (-)Schisandrin B ameliorates paraquat-induced oxidative stress by suppressing glutathione depletion and enhancing glutathione recovery in differentiated PC12 cells
    • Lam PY, Ko KM. (-)Schisandrin B ameliorates paraquat-induced oxidative stress by suppressing glutathione depletion and enhancing glutathione recovery in differentiated PC12 cells. Biofactors 2001; 37: 51-7.
    • (2001) Biofactors , vol.37 , pp. 51-57
    • Lam, P.Y.1    Ko, K.M.2
  • 101
    • 69249203689 scopus 로고    scopus 로고
    • Gomisin N isolated from Schisandra chinensis significantly induces anti-proliferative and pro-apototic effects in hepatic carcinoma
    • Yim SY, Lee YJ, Lee YK et al. Gomisin N isolated from Schisandra chinensis significantly induces anti-proliferative and pro-apototic effects in hepatic carcinoma. Mol. Med. Report 2009; 2: 725-32.
    • (2009) Mol. Med. Report , vol.2 , pp. 725-732
    • Yim, S.Y.1    Lee, Y.J.2    Lee, Y.K.3
  • 102
    • 76749131100 scopus 로고    scopus 로고
    • Apoptosis induction of human leukemia U937 cells by gomisin N, a dibenzocyclootadiene lignin, isolated from Schizandra chinensis Baill
    • Kim JH, Choi YW, Park C et al. Apoptosis induction of human leukemia U937 cells by gomisin N, a dibenzocyclootadiene lignin, isolated from Schizandra chinensis Baill. Food Chem. Toxicol. 2010; 48: 807-13.
    • (2010) Food Chem. Toxicol. , vol.48 , pp. 807-813
    • Kim, J.H.1    Choi, Y.W.2    Park, C.3
  • 103
    • 73149106613 scopus 로고    scopus 로고
    • Inhibition of ATR protein kinase activity by schisandrin B in DNA damage response
    • Nishida H, Tatewaki N, Nakajima Y et al. Inhibition of ATR protein kinase activity by schisandrin B in DNA damage response. Nucleic Acids Res. 2009; 37: 5678-89.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 5678-5689
    • Nishida, H.1    Tatewaki, N.2    Nakajima, Y.3
  • 104
    • 80755143829 scopus 로고    scopus 로고
    • Gomisin N has anti-allergic effect and inhibits inflammatory cytokine expression in mouse bone marrow-derived mast cells
    • Epub 14 March 2011; doi:
    • Chae HS, Kang OH, Oh YC et al. Gomisin N has anti-allergic effect and inhibits inflammatory cytokine expression in mouse bone marrow-derived mast cells. Immunopharmacol. Immunotoxicol. 2011; 33: 709-13. Epub 14 March 2011; doi:.
    • (2011) Immunopharmacol. Immunotoxicol. , vol.33 , pp. 709-713
    • Chae, H.S.1    Kang, O.H.2    Oh, Y.C.3
  • 105
    • 33846385587 scopus 로고    scopus 로고
    • Mammlian cytochromes P450: Importance of tissue specificity
    • Seliskar M, Rozman D. Mammlian cytochromes P450: Importance of tissue specificity. Biochim. Biophys. Acta 2006; 1770: 458-66.
    • (2006) Biochim. Biophys. Acta , vol.1770 , pp. 458-466
    • Seliskar, M.1    Rozman, D.2
  • 106
    • 0035059625 scopus 로고    scopus 로고
    • Metabolism of dimethyl-4,4′-dimethoxy-5,6,5′,6′-dimethylene dioxybiphenyl-2,2′-dicarboxylate (DDB) by human liver microsomes: Characterization of metabolic pathways and of cytochrome P450 isoforms involved
    • Baek MS, Kim JY, Myung SW, Yim YH, Jeong JH, Kim DH. Metabolism of dimethyl-4, 4′-dimethoxy-5, 6, 5′, 6′-dimethylene dioxybiphenyl-2, 2′-dicarboxylate (DDB) by human liver microsomes: Characterization of metabolic pathways and of cytochrome P450 isoforms involved. Drug Metab. Dispos. 2007; 29: 381-8.
    • (2007) Drug Metab. Dispos. , vol.29 , pp. 381-388
    • Baek, M.S.1    Kim, J.Y.2    Myung, S.W.3    Yim, Y.H.4    Jeong, J.H.5    Kim, D.H.6
  • 107
    • 77952365301 scopus 로고    scopus 로고
    • Schisandrin B-induced glutathione antioxidant response and cardioprotection are mediated by reactive oxidant species production in rat hearts
    • Chen N, Ko KM. Schisandrin B-induced glutathione antioxidant response and cardioprotection are mediated by reactive oxidant species production in rat hearts. Biol. Pharm. Bull. 2010; 33: 825-9.
    • (2010) Biol. Pharm. Bull. , vol.33 , pp. 825-829
    • Chen, N.1    Ko, K.M.2
  • 108
    • 84857431178 scopus 로고    scopus 로고
    • Cytochrome P-450-catalyzed reactive oxygen species production mediates the (-)Schisandrin B-induced glutathione and heat shock responses in AML12 hepatocytes
    • Leong PK, Chiu PY, Leung HY, Ko KM. Cytochrome P-450-catalyzed reactive oxygen species production mediates the (-)Schisandrin B-induced glutathione and heat shock responses in AML12 hepatocytes. Cell Biol. Int. 2012; 36: 321-6.
    • (2012) Cell Biol. Int. , vol.36 , pp. 321-326
    • Leong, P.K.1    Chiu, P.Y.2    Leung, H.Y.3    Ko, K.M.4
  • 109
    • 79952432864 scopus 로고    scopus 로고
    • Schisandrin B elicits a glutathione antioxidant response and protects against apoptosis via the redox-sensitive ERK/Nrf2 pathway in AML12 hepatocytes
    • Leong PK, Chiu PY, Chen N, Leung H, Ko KM. Schisandrin B elicits a glutathione antioxidant response and protects against apoptosis via the redox-sensitive ERK/Nrf2 pathway in AML12 hepatocytes. Free Radic. Res. 2011; 45: 483-95.
    • (2011) Free Radic. Res. , vol.45 , pp. 483-495
    • Leong, P.K.1    Chiu, P.Y.2    Chen, N.3    Leung, H.4    Ko, K.M.5
  • 110
    • 79953674467 scopus 로고    scopus 로고
    • Schisandrin B elicits a glutathione antioxidant response and protects against apoptosis via the redox-sensitive ERK/Nrf2 pathway in H9c2 cells
    • Chiu PY, Chen N, Leong PK, Leung HY, Ko KM. Schisandrin B elicits a glutathione antioxidant response and protects against apoptosis via the redox-sensitive ERK/Nrf2 pathway in H9c2 cells. Mol. Cell. Biochem. 2011; 350: 237-50.
    • (2011) Mol. Cell. Biochem. , vol.350 , pp. 237-250
    • Chiu, P.Y.1    Chen, N.2    Leong, P.K.3    Leung, H.Y.4    Ko, K.M.5
  • 111
    • 79953683977 scopus 로고    scopus 로고
    • Gomisin N enhances TNF-α-induced apoptosis via inhibition of the NF-κB and EGFR survival pathways
    • Waiwut P, Shin MS, Inujima A et al. Gomisin N enhances TNF-α-induced apoptosis via inhibition of the NF-κB and EGFR survival pathways. Mol. Cell. Biochem. 2011; 350: 169-75.
    • (2011) Mol. Cell. Biochem. , vol.350 , pp. 169-175
    • Waiwut, P.1    Shin, M.S.2    Inujima, A.3
  • 112
    • 33750159449 scopus 로고    scopus 로고
    • Neurohormetic phytochemicals: Low-dose toxins that induce adaptive neuronal stress responses
    • Mattson MP, Chen A. Neurohormetic phytochemicals: Low-dose toxins that induce adaptive neuronal stress responses. Trends Neurosci. 2006; 29: 632-9.
    • (2006) Trends Neurosci. , vol.29 , pp. 632-639
    • Mattson, M.P.1    Chen, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.