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Volumn 46, Issue 5, 2008, Pages 273-309

Free radicals and low-level photon emission in human pathogenesis: State of the art

Author keywords

Antioxidants; Chaperones; Chronic disease; Free radicals; Heat shock proteins; Photon count distribution; Ultraweak photon emission

Indexed keywords

ANTIOXIDANT; CHAPERONE; FREE RADICAL; HEAT SHOCK PROTEIN; HYDROGEN PEROXIDE; OXYGEN; REACTIVE OXYGEN METABOLITE;

EID: 50649099701     PISSN: 00195189     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (91)

References (442)
  • 1
    • 24944559333 scopus 로고
    • Historical introduction to the "free radical theory" of oxygen toxicity
    • edited by DL Gilbert (Springer, New York, USA)
    • Gerschman R, Historical introduction to the "free radical theory" of oxygen toxicity, in: Oxygen and living processes, an interdisciplinary approach, edited by DL Gilbert (Springer, New York, USA) 1981, 44.
    • (1981) Oxygen and Living Processes, an Interdisciplinary Approach , vol.44
    • Gerschman, R.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.Geronto, 11 (1956) 298.
    • (1956) J. Geronto , vol.11 , pp. 298
    • Harman, D.1
  • 3
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord J M & Fridovich I, Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein), J Biol Chem, 224 (1969) 6049.
    • (1969) J Biol Chem , vol.224 , pp. 6049
    • McCord, J.M.1    Fridovich, I.2
  • 4
    • 0020427486 scopus 로고
    • Biology of disease: Free radicals and tissue injury
    • Freeman B A & Crapo J D, Biology of disease: free radicals and tissue injury, Lab Invest, 47 (1982) 412.
    • (1982) Lab Invest , vol.47 , pp. 412
    • Freeman, B.A.1    Crapo, J.D.2
  • 5
    • 0020334058 scopus 로고
    • Free radical biology: Xenobiotics, cancer and aging
    • Pryor W A, Free radical biology: xenobiotics, cancer and aging, Ann NY Acad Sci, 393 (1982) 1.
    • (1982) Ann NY Acad Sci , vol.393 , pp. 1
    • Pryor, W.A.1
  • 6
    • 0004198354 scopus 로고
    • (Academic Press, New York, USA)
    • Sies H, Oxidative stress (Academic Press, New York, USA) 1985.
    • (1985) Oxidative Stress
    • Sies, H.1
  • 8
    • 0009495930 scopus 로고
    • Lipid peroxidation and myocardial ischaemic damage: Cause or consequence?
    • edited by H Stam H, G J Vusse (Steinkhoff Verlag, Darmstadt)
    • Koster J F, Biemand P & Stam H, Lipid peroxidation and myocardial ischaemic damage: cause or consequence? in Lipid metabolism in the normoxic and alchemic heart, edited by H Stam H, G J Vusse (Steinkhoff Verlag, Darmstadt) 1986, 253.
    • (1986) Lipid Metabolism in the Normoxic and Alchemic Heart , vol.253
    • Koster, J.F.1    Biemand, P.2    Stam, H.3
  • 10
    • 0024950154 scopus 로고
    • Free radical pathology and medicine: A review
    • Dormandi T L, Free radical pathology and medicine: a review, J R Coll Physic (London), 23 (1989) 221.
    • (1989) J R Coll Physic (London) , vol.23 , pp. 221
    • Dormandi, T.L.1
  • 12
    • 70349461920 scopus 로고
    • Glazer, Methods in enzymology: Oxygen radicals in biological systems, Part B
    • (Academic Press, New York, NY)
    • Packer L, Glazer, Methods in enzymology: oxygen radicals in biological systems, Part B: Oxygen radicals and antioxidants, (Academic Press, New York, NY), Vol.186, 1990.
    • (1990) Oxygen Radicals and Antioxidants , vol.186
    • Packer, L.1
  • 13
    • 0026712171 scopus 로고
    • Lipid peroxidation - A common pathogenetic mechanism?
    • Dargel R, Lipid peroxidation - a common pathogenetic mechanism? Exp. Toxic. Pathol, 44 (1992) 169.
    • (1992) Exp. Toxic. Pathol , vol.44 , pp. 169
    • Dargel, R.1
  • 14
    • 0002090036 scopus 로고
    • Origin and evolution of bioluminescence
    • edited by M Kasha and B Pullman (Academic Press, New York)
    • McElroy W D & Seliger H H, Origin and evolution of bioluminescence, in Horizons in biochemistry, edited by M Kasha and B Pullman (Academic Press, New York) 1962, 91.
    • (1962) Horizons in Biochemistry , pp. 91
    • McElroy, W.D.1    Seliger, H.H.2
  • 16
    • 0016838374 scopus 로고
    • The origin of bioluminescence
    • Seliger H H, The origin of bioluminescence, Photochem.Photobiol,21 (1975) 355.
    • (1975) Photochem.Photobiol , vol.21 , pp. 355
    • Seliger, H.H.1
  • 17
    • 78651142389 scopus 로고
    • Study on ultraweak spontaneous luminescence of animal cells
    • Tarusov B N, Polidova A I & Zhuravlev A I, Study on ultraweak spontaneous luminescence of animal cells, Biofizika, 6 (1961) 490.
    • (1961) Biofizika , vol.6 , pp. 490
    • Tarusov, B.N.1    Polidova, A.I.2    Zhuravlev, A.I.3
  • 20
    • 0014110844 scopus 로고
    • Chemoluminescence of mitochondria
    • Stauff J & Ostrowski J, Chemoluminescence of mitochondria, Z. Naturforsch B, 22 (1967) 743.
    • (1967) Z. Naturforsch B , vol.22 , pp. 743
    • Stauff, J.1    Ostrowski, J.2
  • 21
    • 0015087417 scopus 로고
    • Microsomal ( S) chemiluminescence (CL) induced by NADPH and its relation to lipid peroxidation
    • Howes R M & Steele R H, Microsomal ( S) chemiluminescence (CL) induced by NADPH and its relation to lipid peroxidation, Res. Commun. Chem. Pathol. Pharmacol, 2 (1971) 619.
    • (1971) Res. Commun. Chem. Pathol. Pharmacol , vol.2 , pp. 619
    • Howes, R.M.1    Steele, R.H.2
  • 22
    • 0015311231 scopus 로고
    • Microsomal (muS) chemiluminescence (CL) induced by NADPH and its relation to aryl-hydroxylations
    • Howes R M & Steele R H, Microsomal (muS) chemiluminescence (CL) induced by NADPH and its relation to aryl-hydroxylations, Res. Commun. Chem. Pathol. Pharmacol, 3 (1972) 349.
    • (1972) Res. Commun. Chem. Pathol. Pharmacol , vol.3 , pp. 349
    • Howes, R.M.1    Steele, R.H.2
  • 23
    • 70349450634 scopus 로고
    • Ultraweak emission in the visible and ultra-violet regions in oxidation of solutions of glycine by hydrogen peroxide
    • Gurwitsch A A, Eremeyev V F & Karabchievsky Y A, Ultraweak emission in the visible and ultra-violet regions in oxidation of solutions of glycine by hydrogen peroxide, Nature, 3 (1965) 206.
    • (1965) Nature , vol.3 , pp. 206
    • Gurwitsch, A.A.1    Eremeyev, V.F.2    Karabchievsky, Y.A.3
  • 25
    • 0014202862 scopus 로고
    • Mitogenetic radiation
    • Metcalf W S & Quickenden T I, Mitogenetic radiation, Nature, 216(5111) (1967) 169.
    • (1967) Nature , vol.216 , Issue.5111 , pp. 169
    • Metcalf, W.S.1    Quickenden, T.I.2
  • 26
    • 0022394280 scopus 로고
    • The importance of free radicals and catalytic metal ions in human disease
    • Halliwell B & Gutteridge J M C, The importance of free radicals and catalytic metal ions in human disease, Mol asp Med, 8 (1985) 89.
    • (1985) Mol Asp Med , vol.8 , pp. 89
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 27
    • 0001837912 scopus 로고
    • Superoxide radical and hydrogen peroxide in mitochondria
    • (Academic Press, Inc., New York)
    • Forman H J & Boveris A, Superoxide radical and hydrogen peroxide in mitochondria, in Free radicals in biology (Academic Press, Inc., New York) 1982, 65.
    • (1982) Free Radicals in Biology , vol.65
    • Forman, H.J.1    Boveris, A.2
  • 28
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B, Sies H & Boveris A, Hydroperoxide metabolism in mammalian organs, Physiol Rev, 59 (1979) 527.
    • (1979) Physiol Rev , vol.59 , pp. 527
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 29
    • 0016719209 scopus 로고
    • Superoxide, hydrogen peroxide, and singlet oxygen in lipid peroxidation by a xanthine oxidase system
    • Kellogg E W & Fridovich I, Superoxide, hydrogen peroxide, and singlet oxygen in lipid peroxidation by a xanthine oxidase system, J Biol Chem, 250 (1975) 8812.
    • (1975) J Biol Chem , vol.250 , pp. 8812
    • Kellogg, E.W.1    Fridovich, I.2
  • 30
    • 0021984681 scopus 로고
    • Oxygen-derived free radicals in postischemic tissue injury
    • McCord J M, Oxygen-derived free radicals in postischemic tissue injury, N Engl J Med, 312 (1985) 159.
    • (1985) N Engl J Med , vol.312 , pp. 159
    • McCord, J.M.1
  • 31
    • 0022394280 scopus 로고
    • The importance of free radicals and catalytic metal ions in human diseases
    • Halliwell B & Gutteridge J M, The importance of free radicals and catalytic metal ions in human diseases, Mol Aspects Med, 8 (1985) 89.
    • (1985) Mol Aspects Med , vol.8 , pp. 89
    • Halliwell, B.1    Gutteridge, J.M.2
  • 32
    • 0000162325 scopus 로고
    • The catalytic decomposition of hydrogen peroxide by iron salts
    • Haber F & Weiss J, The catalytic decomposition of hydrogen peroxide by iron salts, Proc R Soc London A, (1934) 332.
    • (1934) Proc R Soc London A , vol.332
    • Haber, F.1    Weiss, J.2
  • 33
    • 0018247918 scopus 로고
    • Antioxidants and lipid peroxidation in experimental atherosclerosis of rabbits
    • Wilson R B, Middleton C C & Sun G Y, Vitamin E, antioxidants and lipid peroxidation in experimental atherosclerosis of rabbits, J Nutr, 108 (1978) 1858.
    • (1978) J Nutr , vol.108 , pp. 1858
    • Wilson, R.B.1    Middleton, C.C.2    Sun, G.Y.3    Vitamin, E.4
  • 37
    • 0027209389 scopus 로고
    • Strategies of antioxidant defense
    • Sies H, Strategies of antioxidant defense, Eur J Biochem, 215 (1993) 213
    • (1993) Eur J Biochem , vol.215 , pp. 213
    • Sies, H.1
  • 38
    • 0027327373 scopus 로고
    • Biology of free radical scavengers
    • Rose R & Bode A, Biology of free radical scavengers, FASEB Journal, 7 (1993) 1135.
    • (1993) FASEB Journal , vol.7 , pp. 1135
    • Rose, R.1    Bode, A.2
  • 41
    • 0024512739 scopus 로고
    • Hypoxia, reactive oxygen and cell injury
    • DeGroot H & Littauer A, Hypoxia, reactive oxygen and cell injury, Free Radical Biol Med, 6 (1989) 541.
    • (1989) Free Radical Biol Med , vol.6 , pp. 541
    • DeGroot, H.1    Littauer, A.2
  • 42
    • 0024520513 scopus 로고
    • Central nervous system trauma and stroke: I. Biochemical considerations for oxygen radical formation and lipid peroxidation
    • Braughler J M & Hall E D, Central nervous system trauma and stroke: I. Biochemical considerations for oxygen radical formation and lipid peroxidation, Free Radic Biol Med, 6 (1989) 289.
    • (1989) Free Radic Biol Med , vol.6 , pp. 289
    • Braughler, J.M.1    Hall, E.D.2
  • 43
    • 0024589421 scopus 로고
    • Central nervous system trauma and stroke. II. Physiological and pharmacological evidence for involvement of oxygen radicals and lipid peroxidation
    • Hall E D & Braughler J M, Central nervous system trauma and stroke. II. Physiological and pharmacological evidence for involvement of oxygen radicals and lipid peroxidation, Free Radic Biol Med, 9 (1989) 303.
    • (1989) Free Radic Biol Med , vol.9 , pp. 303
    • Hall, E.D.1    Braughler, J.M.2
  • 44
    • 0024376770 scopus 로고
    • Lipid peroxidation and its significance for (post) ischemic cardiovascular injury
    • Van der Kraaij A M, Schoonderwood K & Koster J F et al., Lipid peroxidation and its significance for (post) ischemic cardiovascular injury, Prog Clin Biol Res, 301 (1989) 61.
    • (1989) Prog Clin Biol Res , vol.301 , pp. 61
    • Van Der Kraaij, A.M.1    Schoonderwood, K.2    Koster, J.F.3
  • 47
    • 0024504126 scopus 로고
    • Intracellular pH during "chemical hypoxia"in cultured rat hepatocytes by intracellular acidosis against theonset of cell death
    • Gores, G K, Nieminen A-L, Wray B E, Herman B & Lemasters J J, Intracellular pH during "chemical hypoxia"in cultured rat hepatocytes by intracellular acidosis against theonset of cell death, J Clin Invest, 83 (1989) 386.
    • (1989) J Clin Invest , vol.83 , pp. 386
    • Gores, G.K.1    Nieminen, A.-L.2    Wray, B.E.3    Herman, B.4    Lemasters, J.J.5
  • 50
    • 0027418625 scopus 로고
    • Mitochondria as a source of reactive oxygen species during reductive stress in rat hepatocytes
    • Dawson T L, Gores G J, Nieminen A-L, Herman B & Lemasters J J, Mitochondria as a source of reactive oxygen species during reductive stress in rat hepatocytes, Am J Physiol, 264 (1993) 961.
    • (1993) Am J Physiol , vol.264 , pp. 961
    • Dawson, T.L.1    Gores, G.J.2    Nieminen, A.-L.3    Herman, B.4    Lemasters, J.J.5
  • 52
    • 0024573661 scopus 로고
    • Transplantation
    • Starzl T E, Transplantation, JAMA, 261(19) (1989) 2894.
    • (1989) JAMA , vol.261 , Issue.19 , pp. 2894
    • Starzl, T.E.1
  • 53
    • 0003023897 scopus 로고
    • The role of oxygen concentration in oxidative stress: Hypoxic and hyperoxic models
    • edited by H. Sies (Academic Press, London)
    • Jones D P, The role of oxygen concentration in oxidative stress: hypoxic and hyperoxic models. In: Oxidative Stress, edited by H. Sies (Academic Press, London) 1985, 152.
    • (1985) Oxidative Stress , vol.152
    • Jones, D.P.1
  • 54
    • 0024210442 scopus 로고
    • Evaluation of free radical and lipid peroxide formation during global ischemia and reperfusion in isolated perfused rat heart
    • Maupoil V & Rochette L, Evaluation of free radical and lipid peroxide formation during global ischemia and reperfusion in isolated perfused rat heart. Cardiovasc, Drugs Ther, 2 (1988) 615.
    • (1988) Cardiovasc Drugs Ther , vol.2 , pp. 615
    • Maupoil, V.1    Rochette, L.2
  • 55
  • 56
    • 0024456743 scopus 로고
    • Effects of iloprost (ZK 36374) on glutathione status during ischaemia and reperfusion of rabbit isolated hearts
    • Ferrari R, Cargnoni A, Curello S, Boffa G M & Ceconi C, Effects of iloprost (ZK 36374) on glutathione status during ischaemia and reperfusion of rabbit isolated hearts, Br J Pharmacol, 98 (1989) 678.
    • (1989) Br J Pharmacol , vol.98 , pp. 678
    • Ferrari, R.1    Cargnoni, A.2    Curello, S.3    Boffa, G.M.4    Ceconi, C.5
  • 60
    • 0000098037 scopus 로고
    • Direct measurement of free radical generation following reperfusion of ischemic myocardium
    • Zweier J L, Flaherty J T & Weisefeldt ML, Direct measurement of free radical generation following reperfusion of ischemic myocardium, Proc Natl Acad Sci USA, 84 (1987) 1404.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 1404
    • Zweier, J.L.1    Flaherty, J.T.2    Weisefeldt, M.L.3
  • 61
    • 0023507184 scopus 로고
    • Recombinant superoxide dismutase reduces oxygen free radical concentrations in reperfused myocardium
    • Zweier J L, Rayburn B K, Flaherty JT & Weisfeldt M L, Recombinant superoxide dismutase reduces oxygen free radical concentrations in reperfused myocardium, J Clin Invest, 80 (1987) 1728.
    • (1987) J Clin Invest , vol.80 , pp. 1728
    • Zweier, J.L.1    Rayburn, B.K.2    Flaherty, J.T.3    Weisfeldt, M.L.4
  • 62
    • 0023867107 scopus 로고
    • Measurement of superoxide-derived free radicals in the reperfused heart. Evidence for a free radical mechanism of reperfusion injury
    • Zweier J L, Measurement of superoxide-derived free radicals in the reperfused heart. Evidence for a free radical mechanism of reperfusion injury, J Biol Chem, 263 (1988) 1353.
    • (1988) J Biol Chem , vol.263 , pp. 1353
    • Zweier, J.L.1
  • 63
    • 0023626933 scopus 로고
    • Improvement of postischemic myocardial function and metabolism induced by administration of deferoxamine at the time of reflow: the role of iron in the pathogenesis of reperfusion injury
    • Ambrosio G, Zweier J L, Jacobus W E, Weisfeldt M L & Flaherty J T, Improvement of postischemic myocardial function and metabolism induced by administration of deferoxamine at the time of reflow: the role of iron in the pathogenesis of reperfusion injury, Circulation 76, (1987) 906.
    • (1987) Circulation , vol.76 , pp. 906
    • Ambrosio, G.1    Zweier, J.L.2    Jacobus, W.E.3    Weisfeldt, M.L.4    Flaherty, J.T.5
  • 64
    • 0022828004 scopus 로고
    • Effect of activated oxygen species on mitochondria isolated from myocardium after reperfusion injury
    • Dec
    • Blasig I E, Bor P, Tosaki A, Szekeres L & Löwe H, Effect of activated oxygen species on mitochondria isolated from myocardium after reperfusion injury, Gen Physiol Biophys, 5(6) (1986 Dec) 655.
    • (1986) Gen Physiol Biophys , vol.5 , Issue.6 , pp. 655
    • Blasig, I.E.1    Bor, P.2    Tosaki, A.3    Szekeres, L.4    Löwe, H.5
  • 65
    • 0023669283 scopus 로고
    • Identification of free radicals in myocardial ischemia/reperfusion by spin trapping with nitrone DMPO
    • Arroyo C M, Kramer J H, Dickens B F & Weglicki W B, Identification of free radicals in myocardial ischemia/reperfusion by spin trapping with nitrone DMPO, FEBS Lett, 221 (1987) 101.
    • (1987) FEBS Lett , vol.221 , pp. 101
    • Arroyo, C.M.1    Kramer, J.H.2    Dickens, B.F.3    Weglicki, W.B.4
  • 67
    • 0025246705 scopus 로고
    • Evaluation of the role of xanthine oxidase in myocardial reperfusion injury
    • Thompson-Gorman S L & Zweier J L, Evaluation of the role of xanthine oxidase in myocardial reperfusion injury, J Biol Chem, 265 (1990) 6656.
    • (1990) J Biol Chem , vol.265 , pp. 6656
    • Thompson-Gorman, S.L.1    Zweier, J.L.2
  • 68
    • 0027080170 scopus 로고
    • Direct measurement of myocardial free radical generation in an in vivo model: Effects of postischemic reperfusion and treatment with human recombinant superoxide dismutase
    • Grill H P, Flaherty J T, Zweier J L, Kuppusamy P & Weisfeldt M L, Direct measurement of myocardial free radical generation in an in vivo model: effects of postischemic reperfusion and treatment with human recombinant superoxide dismutase, J Am Coll Cardiol, 20 (1992) 1604.
    • (1992) J Am Coll Cardiol , vol.20 , pp. 1604
    • Grill, H.P.1    Flaherty, J.T.2    Zweier, J.L.3    Kuppusamy, P.4    Weisfeldt, M.L.5
  • 69
    • 0001786840 scopus 로고
    • Post ischemic myocardial "stunning"
    • edited by D M Yellon & R B Jennings (Raven Press, New York)
    • Bolli, R, Post ischemic myocardial "stunning", in Pathogenesis. pathophysiology and clinical relevance, edited by D M Yellon & R B Jennings (Raven Press, New York) 1992.
    • (1992) Pathogenesis. Pathophysiology and Clinical Relevance
    • Bolli, R.1
  • 70
    • 0025736557 scopus 로고
    • Reperfusion-induced injury: A possible role of oxidant stress and its manipulation
    • Hearse D J, Reperfusion-induced injury: A possible role of oxidant stress and its manipulation, Cardiovasc Drugs Ther, 5 (1991) 225.
    • (1991) Cardiovasc Drugs Ther , vol.5 , pp. 225
    • Hearse, D.J.1
  • 71
    • 4244087065 scopus 로고
    • Reactive oxygen species in living systems: Source, biochemistry and role in human disease
    • Halliwell B, Reactive oxygen species in living systems: Source, biochemistry and role in human disease, Am. J Med, 91 (3C) (1991) 13S.
    • (1991) Am. J Med , vol.91 , Issue.3 C
    • Halliwell, B.1
  • 72
    • 0018749490 scopus 로고
    • Role of superoxide dismutase in cancer: A review
    • Oberley L W & Buettner G R, Role of superoxide dismutase in cancer: a review, Cancer Research, 39 (1979) 1141.
    • (1979) Cancer Research , vol.39 , pp. 1141
    • Oberley, L.W.1    Buettner, G.R.2
  • 74
    • 0026021362 scopus 로고
    • Production of large amounts of hydrogen peroxide by human tumor cells
    • Szatrowski T P & Nathan C F, Production of large amounts of hydrogen peroxide by human tumor cells, Cancer Res, 51 (1991) 794.
    • (1991) Cancer Res , vol.51 , pp. 794
    • Szatrowski, T.P.1    Nathan, C.F.2
  • 77
    • 70349444411 scopus 로고
    • Bioantioxidants and synthetic inhibitors of radical processes
    • Burlokova E B, Bioantioxidants and synthetic inhibitors of radical processes, Russian Chemical Reviews, 44 (1975) 871.
    • (1975) Russian Chemical Reviews , vol.44 , pp. 871
    • Burlokova, E.B.1
  • 78
    • 0014414880 scopus 로고
    • Research on the lipid peroxidase inhibitors present in the cells of Yoshida ascites hepatoma
    • Ugazio G., Gabriel L & Burdino E, Research on the lipid peroxidase inhibitors present in the cells of Yoshida ascites hepatoma, Boll Soc Ital Biol Sper, 44 (1968) 30.
    • (1968) Boll Soc Ital Biol Sper , vol.44 , pp. 30
    • Ugazio, G.1    Gabriel, L.2    Burdino, E.3
  • 79
    • 0013853338 scopus 로고
    • 2+-induced lipid peroxidation and swelling in the mitochondria isolated from ascites tumor cells
    • 2+-induced lipid peroxidation and swelling in the mitochondria isolated from ascites tumor cells, Biochim Biohys Acta, 105 (1965) 368.
    • (1965) Biochim Biohys Acta , vol.105 , pp. 368
    • Utsumi, K.1    Yamamoto, G.2    Inaba, K.3
  • 80
    • 0016701593 scopus 로고
    • Superoxide radicals and hydrogen peroxide formation in mitochondria from normal and neoplastic tissues
    • Dionisi D, Galeotti T, Terranove T & Azzi A, Superoxide radicals and hydrogen peroxide formation in mitochondria from normal and neoplastic tissues, Biochim Biophys Acta, 403 (1975) 292.
    • (1975) Biochim Biophys Acta , vol.403 , pp. 292
    • Dionisi, D.1    Galeotti, T.2    Terranove, T.3    Azzi A4
  • 81
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1
    • Schreck R, Rieber P & Baeuerle P A, Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1, EMBO J, 10 (1991) 2247.
    • (1991) EMBO J , vol.10 , pp. 2247
    • Schreck, R.1    Rieber, P.2    Baeuerle, P.A.3
  • 82
    • 0023941812 scopus 로고
    • Oxidant stress induces the protooncogenes c-fos and c-myc in mouse epidermal cells
    • Crawford D, Zbinden I, Amstad P & Cerutti P, Oxidant stress induces the protooncogenes c-fos and c-myc in mouse epidermal cells, Oncogene, 3 (1988) 27.
    • (1988) Oncogene , vol.3 , pp. 27
    • Crawford, D.1    Zbinden, I.2    Amstad, P.3    Cerutti, P.4
  • 83
    • 0027431095 scopus 로고
    • Cloning from a mouse osteoblastic cell line of a set of transforming growth factor 1-regulated genes, one of which seems to encode a follistatin-related polypeptide
    • Shibanuma M, Mashimo J, Mita A, Kuroki T & Nose K, Cloning from a mouse osteoblastic cell line of a set of transforming growth factor 1-regulated genes, one of which seems to encode a follistatin-related polypeptide, Eur J Biochem, 217 (1993) 13.
    • (1993) Eur J Biochem , vol.217 , pp. 13
    • Shibanuma, M.1    Mashimo, J.2    Mita, A.3    Kuroki, T.4    Nose, K.5
  • 84
    • 0028270384 scopus 로고
    • Oxidative DNA base damage and antioxidant enzyme activities in human lung cancer
    • Jaruga P, Zastawny T H, Skokowski J, Dizdaroglu M & Olinski R, Oxidative DNA base damage and antioxidant enzyme activities in human lung cancer, FEBS Lett, 341 (1994) 59.
    • (1994) FEBS Lett , vol.341 , pp. 59
    • Jaruga, P.1    Zastawny, T.H.2    Skokowski, J.3    Dizdaroglu, M.4    Olinski, R.5
  • 85
    • 0016998961 scopus 로고
    • Biochemical Pathology in microtime
    • Slater T F, Biochemical Pathology in microtime, Panminerva Medica, 18 (1976) 381.
    • (1976) Panminerva Medica , vol.18 , pp. 381
    • Slater, T.F.1
  • 86
    • 0015319592 scopus 로고
    • The biologic clock: The mitochondria?
    • Harman D, The biologic clock: The mitochondria? J Amer Geriat Soc, 20 (1972) 145.
    • (1972) J Amer Geriat Soc , vol.20 , pp. 145
    • Harman, D.1
  • 87
    • 0003138331 scopus 로고
    • Theoretical and experimental support for an "oxygen radical-mitochondrial injury" hypothesis of cell aging
    • edited by J E Johnson, R Walford, D Harman & J Miquel (Alan R. Liss, New York)
    • Miquel J & Fleming J, Theoretical and experimental support for an "oxygen radical-mitochondrial injury" hypothesis of cell aging, in Free radicals, ageing and degenerative diseases, edited by J E Johnson, R Walford, D Harman & J Miquel (Alan R. Liss, New York) 1986, 51.
    • (1986) Free Radicals, Ageing and Degenerative Diseases , vol.51
    • Miquel, J.1    Fleming, J.2
  • 88
    • 0020066839 scopus 로고
    • Is cell aging caused by respirationdependent injury to the mitochondrial genome?
    • Fleming J E, Miquel J, Cottrell S F, Yengoyan L S & Economos A C, Is cell aging caused by respirationdependent injury to the mitochondrial genome? Gerontology, 28(1) (1982) 44.
    • (1982) Gerontology , vol.28 , Issue.1 , pp. 44
    • Fleming, J.E.1    Miquel, J.2    Cottrell, S.F.3    Yengoyan, L.S.4    Economos, A.C.5
  • 89
    • 0023265801 scopus 로고
    • Mechanism of toxicity of ionic copper and copper complexes to algae
    • Stauber J L & Florence T M, Mechanism of toxicity of ionic copper and copper complexes to algae, Mar Biol, 94 (1987) 511.
    • (1987) Mar Biol , vol.94 , pp. 511
    • Stauber, J.L.1    Florence, T.M.2
  • 91
    • 0020353123 scopus 로고
    • Age-related decline in the biosynthesis of mitiochondrial inner membrane proteins
    • Marcus D L, Ibrahim N G & L. Freedman L, Age-related decline in the biosynthesis of mitiochondrial inner membrane proteins, Exp Gerontol, 17 (1982) 333.
    • (1982) Exp Gerontol , vol.17 , pp. 333
    • Marcus, D.L.1    Ibrahim, N.G.2    Freedman, L.L.3
  • 92
    • 0344759851 scopus 로고
    • Spontaneous cancer and its possible relationship to oxygen metabolism
    • Totter J R, Spontaneous cancer and its possible relationship to oxygen metabolism, Proc Natl Acad Sci USA 77 (1980) 1763.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1763
    • Totter, J.R.1
  • 93
    • 0026166135 scopus 로고
    • Pivotal role of increased cell proliferation in human carcinogenesis
    • Cohen S M, Purtilo D T & Ellwein L B, Pivotal role of increased cell proliferation in human carcinogenesis, Mod Pathol, 4 (1991) 371.
    • (1991) Mod Pathol , vol.4 , pp. 371
    • Cohen, S.M.1    Purtilo, D.T.2    Ellwein, L.B.3
  • 94
    • 0027848672 scopus 로고
    • DNA lesions, inducible DNA repair, and cell division: Three key factors in mutagenesis and carcinogenesis
    • Dec. Review
    • Ames B N, Shigenaga M K & Gold L S, DNA lesions, inducible DNA repair, and cell division: three key factors in mutagenesis and carcinogenesis, Environ Health Perspect, Dec 101 Suppl 5 (1993) 35. Review
    • (1993) Environ Health Perspect , Issue.101 SUPPL. 5 , pp. 35
    • Ames, B.N.1    Shigenaga, M.K.2    Gold, L.S.3
  • 96
    • 0025976425 scopus 로고
    • Oxidant stress and carcinogenesis
    • Cerutti P A, Oxidant stress and carcinogenesis, Eur J Clin Invest, 21(1) (1991) 1.
    • (1991) Eur J Clin Invest , vol.21 , Issue.1 , pp. 1
    • Cerutti, P.A.1
  • 97
    • 0026753708 scopus 로고
    • Mechanism of c-fos induction by active oxygen
    • Amstad P A, Krupitza G & Cerutti P A, Mechanism of c-fos induction by active oxygen, Cancer Res, 52 (1992) 3952.
    • (1992) Cancer Res , vol.52 , pp. 3952
    • Amstad, P.A.1    Krupitza, G.2    Cerutti, P.A.3
  • 99
    • 0021964203 scopus 로고
    • Prooxidant states and tumor promotion
    • Cerutti P A, Prooxidant states and tumor promotion, Science, 227 (1985) 375.
    • (1985) Science , vol.227 , pp. 375
    • Cerutti, P.A.1
  • 100
    • 0024307578 scopus 로고
    • Oxygen toxicity and reactive oxygen metabolites in mammals
    • Jamieson D, Oxygen toxicity and reactive oxygen metabolites in mammals, Free Rad Biol Med, 7 (1989) 87.
    • (1989) Free Rad Biol Med , vol.7 , pp. 87
    • Jamieson, D.1
  • 101
    • 0025289049 scopus 로고
    • Free radicals, antioxidant enzymes, and carcinogenesis
    • Sun Y, Free radicals, antioxidant enzymes, and carcinogenesis, Free Rad Biol Med, 8, (1990) 583.
    • (1990) Free Rad Biol Med , vol.8 , pp. 583
    • Sun, Y.1
  • 102
    • 0021894614 scopus 로고
    • The role of oxygen radicals as a possible mechanism of tumor promotion
    • Troll W & Wiesner R., The role of oxygen radicals as a possible mechanism of tumor promotion, Annu Rev Pharmcol Toxicol, 25 (1985) 509.
    • (1985) Annu Rev Pharmcol Toxicol , vol.25 , pp. 509
    • Troll, W.1    Wiesner, R.2
  • 103
    • 0020080933 scopus 로고
    • Effects of oxygen scavengers and antioxidants on phagocyte-induced mutagenesis
    • Weitzman S A, & Stossel T P, Effects of oxygen scavengers and antioxidants on phagocyte-induced mutagenesis, J Immunol, 182 (1982) 2770.
    • (1982) J Immunol , vol.182 , pp. 2770
    • Weitzman, S.A.1    Stossel, T.P.2
  • 104
    • 0027503178 scopus 로고
    • The permissive role of oxygen-derived in the development of colonic cancer in the rat
    • Salim A S, The permissive role of oxygen-derived in the development of colonic cancer in the rat, Int J Cancer, (1993) 1031.
    • (1993) Int J Cancer , vol.1031
    • Salim, A.S.1
  • 105
    • 0026519981 scopus 로고
    • Oxygen-derived free-radical scavengers prolong survival in colonic cancer
    • Salim A S, Oxygen-derived free-radical scavengers prolong survival in colonic cancer, Chemotherapy, 38 (1992) 127.
    • (1992) Chemotherapy , vol.38 , pp. 127
    • Salim, A.S.1
  • 106
    • 0026605763 scopus 로고
    • Oxygen-derived free -radical scavengers prolong survival in gastric cancer
    • Salim A S, Oxygen-derived free -radical scavengers prolong survival in gastric cancer, Chemotherapy, 38 (1992) 135.
    • (1992) Chemotherapy , vol.38 , pp. 135
    • Salim, A.S.1
  • 107
    • 0026565257 scopus 로고
    • Removing oxygen-derived free radicals delays hepatic metastases and prolongs survival in colonic cancer
    • Salim A S, Removing oxygen-derived free radicals delays hepatic metastases and prolongs survival in colonic cancer, Oncology, 49 (1992) 58.
    • (1992) Oncology , vol.49 , pp. 58
    • Salim, A.S.1
  • 108
    • 0027104253 scopus 로고
    • Biochemistry of nitric oxide and its redox-activated forms
    • Stamle, J, Singel D J & Loscalz, J, Biochemistry of nitric oxide and its redox-activated forms, Science, 251 (1992) 1898.
    • (1992) Science , vol.251 , pp. 1898
    • Stamle, J.1    Singel, D.J.2    Loscalz, J.3
  • 109
    • 0026453418 scopus 로고
    • Peroxynitrite formation from macrophage-derived nitric oxide
    • Ischiropoulos H, Zhu L & Beckman J S, Peroxynitrite formation from macrophage-derived nitric oxide, Arch Biochem Biophys, 298 (1992) 446.
    • (1992) Arch Biochem Biophys , vol.298 , pp. 446
    • Ischiropoulos, H.1    Zhu, L.2    Beckman, J.S.3
  • 111
    • 0022615005 scopus 로고
    • Macrophagemediated induction of drug-resistant variants in a mouse mammary tumor cell line
    • Yamashina K, Miller B E & Heppner G H, Macrophagemediated induction of drug-resistant variants in a mouse mammary tumor cell line, Cancer Res, 46 (1986) 2396.
    • (1986) Cancer Res , vol.46 , pp. 2396
    • Yamashina, K.1    Miller, B.E.2    Heppner, G.H.3
  • 112
    • 0037462684 scopus 로고    scopus 로고
    • Globular adiponectin protected ob/ob mice from diabetes and apoE-deficient mice from atherosclerosis
    • Yamauchi T et al., Globular adiponectin protected ob/ob mice from diabetes and apoE-deficient mice from atherosclerosis, J Biol Chem, 278 (2003) 2461.
    • (2003) J Biol Chem , vol.278 , pp. 2461
    • Yamauchi, T.1
  • 113
    • 0023933449 scopus 로고
    • Hepatitis B virus. The major etiology of hepatocellular carcinoma
    • Beasley R P, Hepatitis B virus. The major etiology of hepatocellular carcinoma, Cancer, 61 (1988) 1942.
    • (1988) Cancer , vol.61 , pp. 1942
    • Beasley, R.P.1
  • 114
    • 0026518488 scopus 로고
    • Hepatitis C virus, a causative infectious agent of non-A, non-B hepatitis: Prevalence and structure--summary of a conference on hepatitis C virus as a cause of hepatocellular carcinoma
    • Tabor E & Kobayashi K, Hepatitis C virus, a causative infectious agent of non-A, non-B hepatitis: prevalence and structure--summary of a conference on hepatitis C virus as a cause of hepatocellular carcinoma, J Natl Cancer Inst, 84 (1992) 86.
    • (1992) J Natl Cancer Inst , vol.84 , pp. 86
    • Tabor, E.1    Kobayashi, K.2
  • 115
    • 0025934725 scopus 로고
    • Association between hepatitis C virus antibodies and hepatocellular carcinoma in Taiwan
    • Yu M-W, You S-L, Chang, A-S, Lu S-N, Liaw Y-F & Chen C-J, Association between hepatitis C virus antibodies and hepatocellular carcinoma in Taiwan, Cancer Res, 51 (1991) 5621.
    • (1991) Cancer Res , vol.51 , pp. 5621
    • Yu, M.-W.1    You, S.-L.2    Chang, A.-S.3    Lu, S.-N.4    Liaw, Y.-F.5    Chen, C.-J.6
  • 116
    • 0002048221 scopus 로고
    • Progress in assessment of. morbidity due to Schistosoma mansoni infection
    • Chen M & Mott K, Progress in assessment of. morbidity due to Schistosoma mansoni infection, Trop Diss Bull, 85 (1988) 2.
    • (1988) Trop Diss Bull , vol.85 , pp. 2
    • Chen, M.1    Mott, K.2
  • 117
    • 0002048221 scopus 로고
    • Progress in assessment of morbidity due to Schistosoma haematobium infection. A review of recent literature
    • Chen M & Mott K, Progress in assessment of morbidity due to Schistosoma haematobium infection. A review of recent literature, Trop Dis Bull, 86 (1989) 1.
    • (1989) Trop Dis Bull , vol.86 , pp. 1
    • Chen, M.1    Mott, K.2
  • 118
    • 0025982018 scopus 로고
    • Levels of nitrite, nitrate, N-nitroso compounds, ascorbic acid and total bile acids in gastric juice of patients with and without precancerous conditions of the stomach
    • Sobala G M, Pignatelli B, Schorah C J, Bartsch H, Sanderson M, Dixon M F, Shires S, King R F G & Axon A T R, Levels of nitrite, nitrate, N-nitroso compounds, ascorbic acid and total bile acids in gastric juice of patients with and without precancerous conditions of the stomach, Carcinogenesis, 12 (1991) 193.
    • (1991) Carcinogenesis , vol.12 , pp. 193
    • Sobala, G.M.1    Pignatelli, B.2    Schorah, C.J.3    Bartsch, H.4    Sanderson, M.5    Dixon, M.F.6    Shires, S.7    King, R.F.G.8    Axon, A.T.R.9
  • 122
    • 0026643058 scopus 로고
    • Helicobacter pylori and gastroduodenal disease
    • Cover T L & Blaser M J, Helicobacter pylori and gastroduodenal disease, Annu Rev Med, 43 (1992) 135.
    • (1992) Annu Rev Med , vol.43 , pp. 135
    • Cover, T.L.1    Blaser, M.J.2
  • 123
    • 0027176157 scopus 로고
    • The Eurogast Study Group An international association between Helicobacter pylori infection and gastric cancer
    • The Eurogast Study Group An international association between Helicobacter pylori infection and gastric cancer, Lancet, 341 (1993) 1359.
    • (1993) Lancet , vol.341 , pp. 1359
  • 124
    • 0026098786 scopus 로고
    • Role of asbestos and active oxygen species in activation and expression of ornithine decarboxylase in hamster tracheal epithelial cells
    • Marsh J P & Mossman B T, Role of asbestos and active oxygen species in activation and expression of ornithine decarboxylase in hamster tracheal epithelial cells, Cancer Res, 51 (1991) 167.
    • (1991) Cancer Res , vol.51 , pp. 167
    • Marsh, J.P.1    Mossman, B.T.2
  • 125
    • 0026558630 scopus 로고
    • Oxygen radicalmediated mutagenic effect of asbestos on human lymphocytes: Suppression by oxygen radical scavengers
    • Korkina L G, Durnev A D, Suslova T B, Cheremisina ZP, Daugel-Dauge N O & Afanas'ev I B, Oxygen radicalmediated mutagenic effect of asbestos on human lymphocytes: suppression by oxygen radical scavengers, Mutat Res, 265 (1992) 245.
    • (1992) Mutat Res , vol.265 , pp. 245
    • Korkina, L.G.1    Durnev, A.D.2    Suslova, T.B.3    Cheremisina, Z.P.4    Daugel-Dauge, N.O.5    Afanas'ev, I.B.6
  • 126
    • 0027312415 scopus 로고
    • Role of free radicals in cancer and artheroclerosis
    • Bankson D D, Kestin M & Rifia N, Role of free radicals in cancer and artheroclerosis, Clin Lab Med, 13 (1993) 463.
    • (1993) Clin Lab Med , vol.13 , pp. 463
    • Bankson, D.D.1    Kestin, M.2    Rifia, N.3
  • 127
    • 0027465289 scopus 로고
    • The role of oxygen radicals in human disease
    • Halliwell B, The role of oxygen radicals in human disease, Haemostasis, 23 (suppl) (1993) S118.
    • (1993) Haemostasis , vol.23 , Issue.SUPPL
    • Halliwell, B.1
  • 128
    • 0024662072 scopus 로고
    • The role of lipid peroxidation in the etiology and pathogenesis of artherosclerosis (review)
    • Lankin V Z, Vikhert A M, Tikhaze A K, et al., The role of lipid peroxidation in the etiology and pathogenesis of artherosclerosis (review), Vopr Med Khim, 35 (1989) 18-24
    • (1989) Vopr Med Khim , vol.35 , pp. 18-24
    • Lankin, V.Z.1    Vikhert, A.M.2    Tikhaze, A.K.3
  • 129
  • 130
    • 0025601848 scopus 로고
    • Smoking, antioxidants, essential fatty acids and coronary heart disease
    • Duthie G G & Wahle K J, Smoking, antioxidants, essential fatty acids and coronary heart disease, Biochem Soc Transact, 18 (1990) 1051.
    • (1990) Biochem Soc Transact , vol.18 , pp. 1051
    • Duthie, G.G.1    Wahle, K.J.2
  • 132
    • 0025652555 scopus 로고
    • The antioxidant hypothesis of cardiovascular disease: Epidemiology and mechanisms
    • Gey K F, The antioxidant hypothesis of cardiovascular disease: epidemiology and mechanisms, Biochem Soc Transact, 18 (1990) 1041.
    • (1990) Biochem Soc Transact , vol.18 , pp. 1041
    • Gey, K.F.1
  • 133
    • 0025610924 scopus 로고
    • Linoleic acid, antioxidants and coronary heart disease
    • Oliver M F, Linoleic acid, antioxidants and coronary heart disease, Biochem Soc Trans, 18 (1990) 1049.
    • (1990) Biochem Soc Trans , vol.18 , pp. 1049
    • Oliver, M.F.1
  • 134
    • 0026874975 scopus 로고
    • Antioxidants in the prevention of human atherosclerosis
    • Steinberg D, Antioxidants in the prevention of human atherosclerosis, Circulation, 85 (1992) 2337.
    • (1992) Circulation , vol.85 , pp. 2337
    • Steinberg, D.1
  • 136
    • 0029981370 scopus 로고    scopus 로고
    • Update on dietary antioxidants and cancer
    • Review
    • Gaziano J M & Hennekens C H, Update on dietary antioxidants and cancer, Pathol Biol (Paris), 44(1) (1996) 42. Review
    • (1996) Pathol Biol (Paris) , vol.44 , Issue.1 , pp. 42
    • Gaziano, J.M.1    Hennekens, C.H.2
  • 137
    • 0026576932 scopus 로고
    • Vitamin C intake and mortality among a sample of the United States population
    • Enstrom J E, Kanim L E & Klein M A, Vitamin C intake and mortality among a sample of the United States population, Epidemiology, 3 (1992) 194.
    • (1992) Epidemiology , vol.3 , pp. 194
    • Enstrom, J.E.1    Kanim, L.E.2    Klein, M.A.3
  • 138
    • 0026025851 scopus 로고
    • Inverse correlation between plasma vitamin E and mortality from ischemic heart disease in cross-cultural epidemiology
    • Gey K F, Puska P & Moser U K, Inverse correlation between plasma vitamin E and mortality from ischemic heart disease in cross-cultural epidemiology, Am J Clin Nutr, 53 (1991) 326S.
    • (1991) Am J Clin Nutr , vol.53
    • Gey, K.F.1    Puska, P.2    Moser, U.K.3
  • 139
    • 34548140158 scopus 로고    scopus 로고
    • Natural antioxidant compounds in risk factors for CVD
    • Kaliora A C & Dedoussis GV, Natural antioxidant compounds in risk factors for CVD, Pharmacol Res, 56 (2007) 99.
    • (2007) Pharmacol Res , vol.56 , pp. 99
    • Kaliora, A.C.1    Dedoussis, G.V.2
  • 144
    • 0027285792 scopus 로고
    • Antioxidant vitamins and coronary heart disease
    • Steinberg D, Antioxidant vitamins and coronary heart disease, N Eng J Med, 328 (1993) 1487.
    • (1993) N Eng J Med , vol.328 , pp. 1487
    • Steinberg, D.1
  • 145
    • 0024690724 scopus 로고
    • Lipid peroxidation and the major factors of its activation in patients with myocardial infarction
    • Golikovn A P, Polumiskov V J, Davydov B V et al., Lipid peroxidation and the major factors of its activation in patients with myocardial infarction, Cardiology, 29 (1989) 53.
    • (1989) Cardiology , vol.29 , pp. 53
    • Golikovn, A.P.1    Polumiskov, V.J.2    Davydov, B.V.3
  • 147
    • 0024400269 scopus 로고
    • Free radical mediated injuries alter coronary artery occlusion
    • Roth E, Torok B, Kellemen D et al., Free radical mediated injuries alter coronary artery occlusion, Basic Res Cardiol, 84(4) (1989) 388.
    • (1989) Basic Res Cardiol , vol.84 , Issue.4 , pp. 388
    • Roth, E.1    Torok, B.2    Kellemen, D.3
  • 148
    • 0023873792 scopus 로고
    • Lipid peroxidation and endothelial cell injury: Implications in atherosclerose
    • Hennig B & Chow C K, Lipid peroxidation and endothelial cell injury: Implications in atherosclerose, Free Radic Biol Med, 4 (1988) 99.
    • (1988) Free Radic Biol Med , vol.4 , pp. 99
    • Hennig, B.1    Chow, C.K.2
  • 149
    • 0026337912 scopus 로고
    • Mechanisms of endothelial cell injury
    • Ward P A,; Mechanisms of endothelial cell injury, J Lab Clin Med, 118 (1991) 421.
    • (1991) J Lab Clin Med , vol.118 , pp. 421
    • Ward, P.A.1
  • 150
    • 0027300736 scopus 로고
    • Lipid peroxidation: Its mechanism, measurement, and significance
    • Halliwell B & Chirico S, Lipid peroxidation: Its mechanism, measurement, and significance, Am J Clin Nutr, 1993(suppl) 715S.
    • (1993) Am J Clin Nutr , Issue.SUPPL.
    • Halliwell, B.1    Chirico, S.2
  • 152
    • 0019297268 scopus 로고
    • The scavenger cell pathway for lipoprotein degradation; Specificity of the binding site that mediates the uptake of neatively charged LDL by macrophage
    • Brown M S, Basu S K, Palck J R, Ho Y K & Goldstein J L, The scavenger cell pathway for lipoprotein degradation; Specificity of the binding site that mediates the uptake of neatively charged LDL by macrophage, J Supramol Struct, 13 (1980) 67.
    • (1980) J Supramol Struct , vol.13 , pp. 67
    • Brown, M.S.1    Basu, S.K.2    Palck, J.R.3    Ho, Y.K.4    Goldstein, J.L.5
  • 153
    • 0020972414 scopus 로고
    • Lipoprotein metabolism in the macrophage; Implications for cholesterol deposition in stherosclerosis
    • Brown M S & Goldstein J L, Lipoprotein metabolism in the macrophage; Implications for cholesterol deposition in stherosclerosis, Annu Rev Biochem, 52 (1983) 233.
    • (1983) Annu Rev Biochem , vol.52 , pp. 233
    • Brown, M.S.1    Goldstein, J.L.2
  • 154
    • 0026720145 scopus 로고
    • Kohlsch"tter A & Messmer K, Superoxide-dependent of leukocyte adhesion by oxidatively modified LDL
    • Lehr H, Becker M, Marklund S L, Hübner C, Arfors K E, Kohlsch"tter A & Messmer K, Superoxide-dependent of leukocyte adhesion by oxidatively modified LDL in vivo, Arterioscler Thromb, 12 (1992) 824.
    • (1992) Vivo Arterioscler Thromb , vol.12 , pp. 824
    • Lehr, H.1    Becker, M.2    Marklund, S.L.3    Hübner, C.4    Arfors, K.E.5
  • 157
    • 0025323149 scopus 로고
    • Free radical-mediated chain oxidation of low density lipoprotein and its synergistic inhibitation by vitamin E and vitamin C
    • Sato K, Niki E & Shimasaki H, Free radical-mediated chain oxidation of low density lipoprotein and its synergistic inhibitation by vitamin E and vitamin C, Arch biochem Biophys, 279 (1990) 402.
    • (1990) Arch biochem Biophys , vol.279 , pp. 402
    • Sato, K.1    Niki, E.2    Shimasaki, H.3
  • 158
    • 0022504408 scopus 로고
    • The effect of proteoglycans, collagen and lysyl oxidase on the metabolism of low density lipoprotein by macrophages
    • Ylä-Herttuala S, Jaakkola O, Solakivi T, Kuivaniemi H & Nikkari T, The effect of proteoglycans, collagen and lysyl oxidase on the metabolism of low density lipoprotein by macrophages, Atherosclerosis, 62 (1986) 73.
    • (1986) Atherosclerosis , vol.62 , pp. 73
    • Ylä-Herttuala, S.1    Jaakkola, O.2    Solakivi, T.3    Kuivaniemi, H.4    Nikkari, T.5
  • 159
    • 0027537768 scopus 로고
    • Glycation and oxidation: A role in the pathogenesis of atherosclerosis
    • Lyons T J, Glycation and oxidation: a role in the pathogenesis of atherosclerosis, Am J Cardiol, 71 (1993) 26B.
    • (1993) Am J Cardiol , vol.71
    • Lyons, T.J.1
  • 160
    • 0009627006 scopus 로고
    • Binding site on macrophages that mediates the uptake and degradation of acetylated low density lipoprotein producing massivecholesterol deposition
    • Goldstein J L, Ho Y K, Basu S K & Brown M S, Binding site on macrophages that mediates the uptake and degradation of acetylated low density lipoprotein producing massivecholesterol deposition, Proc Natl Acad Sci USA, 76 (1979) 333.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 333
    • Goldstein, J.L.1    Ho, Y.K.2    Basu, S.K.3    Brown, M.S.4
  • 161
    • 0011172276 scopus 로고
    • A role for endothelial cell lipoxygenase in the oxidative modification of low density lipoprotein
    • Parthasarathy S, Wieland E & Steinberg D, A role for endothelial cell lipoxygenase in the oxidative modification of low density lipoprotein, Proc Natl Acad Sci USA, 86 (1989) 1046.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 1046
    • Parthasarathy, S.1    Wieland, E.2    Steinberg, D.3
  • 162
    • 0025720430 scopus 로고
    • Ascorbic acid protects lipids in human plasma and the low-density lipoprotein against oxidative damage
    • Frei B, Ascorbic acid protects lipids in human plasma and the low-density lipoprotein against oxidative damage, Am J Clin Nutr, 54 (1991) 1113.
    • (1991) Am J Clin Nutr , vol.54 , pp. 1113
    • Frei, B.1
  • 165
    • 0026764766 scopus 로고
    • Ubiquinone protects cultured neurons against spontaneous and excitotoxin-induced degeneration
    • Favit A, Nicoletti F, Scapagnini U & Canonico P L, Ubiquinone protects cultured neurons against spontaneous and excitotoxin-induced degeneration, J Cereb Blood Flow Metab, 12. (1992) 638.
    • (1992) J Cereb Blood Flow Metab , vol.12 , pp. 638
    • Favit, A.1    Nicoletti, F.2    Scapagnini, U.3    Canonico, P.L.4
  • 166
    • 0026520111 scopus 로고
    • NGF restores decrease in catalase activity and increases superoxide dismutase and glutathione peroxidase activity in the brain of aged rats
    • Nisticò G, Ciriolo M R, Fiskin K, Iannone M, De Martino A & Rotilio G, NGF restores decrease in catalase activity and increases superoxide dismutase and glutathione peroxidase activity in the brain of aged rats, Free Rad Biol Med, 12 (1992) 177.
    • (1992) Free Rad Biol Med , vol.12 , pp. 177
    • Nisticò, G.1    Ciriolo, M.R.2    Fiskin, K.3    Iannone, M.4    De Martino, A.5    Rotilio, G.6
  • 167
    • 0026087383 scopus 로고
    • Oxygen free radicals and Parkinson's disease
    • Adams Jr. J D & Odunze I N, Oxygen free radicals and Parkinson's disease, Free Rad Biol. Med, 10 (1991) 161.
    • (1991) Free Rad Biol. Med , vol.10 , pp. 161
    • Adams Jr., J.D.1    Odunze, I.N.2
  • 169
    • 0026773281 scopus 로고
    • Oxygen radicals as key mediators in neurological disease: Fact or fiction?
    • Halliwell B, Oxygen radicals as key mediators in neurological disease: fact or fiction? Ann Neurol, 32 (1992) S10.
    • (1992) Ann Neurol , vol.32
    • Halliwell, B.1
  • 170
    • 0026647763 scopus 로고
    • Free radical damage to protein and DNA: Mechanisms involved and relevant observations on brain undergoing oxidative stress
    • Floyd R A & Carney J M, Free radical damage to protein and DNA: mechanisms involved and relevant observations on brain undergoing oxidative stress, Ann Neurol, 32 (1992) S22.
    • (1992) Ann Neurol , vol.32
    • Floyd, R.A.1    Carney, J.M.2
  • 171
    • 0026662216 scopus 로고
    • Biochemical and toxicological properties of the oxidation products of catecholamines
    • Bindoli A, Rigobello M P & Deeble D J, Biochemical and toxicological properties of the oxidation products of catecholamines, Free Radicals Biol Med, 13 (1992) 391.
    • (1992) Free Radicals Biol Med , vol.13 , pp. 391
    • Bindoli, A.1    Rigobello, M.P.2    Deeble, D.J.3
  • 172
    • 0020644952 scopus 로고
    • Superoxide radical: An endogenous toxicant
    • Fridovich I, Superoxide radical: an endogenous toxicant, Annu Rev Pharmacol Toxicol, 23 (1983) 239.
    • (1983) Annu Rev Pharmacol Toxicol , vol.23 , pp. 239
    • Fridovich, I.1
  • 173
    • 0021351203 scopus 로고
    • Oxygen toxicity, oxygen radicals, transition metals and disease
    • Halliwell B & Gutteridge J M C, (1984) Oxygen toxicity, oxygen radicals, transition metals and disease, Biochem J, 219 (1984) 11.
    • (1984) Biochem J , vol.219 , pp. 11
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 175
    • 0002124285 scopus 로고
    • Free radicals, oxygen toxicity and aging
    • edited by R S Sohal (Elsevier, Amsterdam)
    • Halliwell B, Free radicals, oxygen toxicity and aging, in Age pigments, edited by R S Sohal (Elsevier, Amsterdam) 1981.
    • (1981) Age pigments
    • Halliwell, B.1
  • 176
    • 0000821424 scopus 로고
    • Catalase, glutathione peroxidase, superoxide dismutase and cytochrome P-450 in the nervous system
    • edited by A Lajtha (New York, Plenum Publishing)
    • Cohen G, Catalase, glutathione peroxidase, superoxide dismutase and cytochrome P-450 in the nervous system, in Handbook of neurochemistry, edited by A Lajtha (New York, Plenum Publishing) 1983.
    • (1983) Handbook of Neurochemistry
    • Cohen, G.1
  • 177
    • 0018853019 scopus 로고
    • Hydrogen peroxide production by rat brain in vivo
    • Sinet P M, Heikkila R E & Cohen G, Hydrogen peroxide production by rat brain in vivo, J Neurochem, 34 (1980) 1421.
    • (1980) J Neurochem , vol.34 , pp. 1421
    • Sinet, P.M.1    Heikkila, R.E.2    Cohen, G.3
  • 179
    • 0021592857 scopus 로고
    • The possible relation of glutathione, melanin and 1-methyl-4-phenyl-1,2, 5,6- tetrahydropyridine (MPTP) to Parkinson's disease
    • Bannon M J, Goedert M & Williams B, The possible relation of glutathione, melanin and 1-methyl-4-phenyl-1,2,5,6- tetrahydropyridine (MPTP) to Parkinson's disease, Biochem Pharmacol, 33(17) (1984) 2697.
    • (1984) Biochem Pharmacol , vol.33 , Issue.17 , pp. 2697
    • Bannon, M.J.1    Goedert, M.2    Williams, B.3
  • 180
    • 0023106967 scopus 로고
    • A quantitative morphometric analysis of the neuronal and synaptic content of the frontal and temporal cortex in patients with AD
    • Davies C A, Mann D M A, Sumpter P Q & Yates P.O, A quantitative morphometric analysis of the neuronal and synaptic content of the frontal and temporal cortex in patients with AD, J Neurol Sci. 78 (1987) 151.
    • (1987) J Neurol Sci. , vol.78 , pp. 151
    • Davies, C.A.1    Mann, D.M.A.2    Sumpter, P.Q.3    Yates, P.O.4
  • 181
    • 0025269152 scopus 로고
    • Synapse loss in frontal cortex biopsies in AD correlation with cognitive severity
    • DeKosky S T & Scheff S W, Synapse loss in frontal cortex biopsies in AD correlation with cognitive severity, Ann Neurol, 27 (1990) 457.
    • (1990) Ann Neurol , vol.27 , pp. 457
    • DeKosky, S.T.1    Scheff, S.W.2
  • 183
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of AD
    • Hardy J & Allsop D, Amyloid deposition as the central event in the aetiology of AD, Trends Neurosci, 12 (1991) 383.
    • (1991) Trends Neurosci , vol.12 , pp. 383
    • Hardy, J.1    Allsop, D.2
  • 184
    • 0022480081 scopus 로고
    • Increased cerebral glucose-6-phosphate dehydrogenase activity in Alzheimer's disease may reflect oxidative stress
    • Martins R N, Harper C G, Stokes G B & Masters C L, Increased cerebral glucose-6-phosphate dehydrogenase activity in Alzheimer's disease may reflect oxidative stress, J Neurochem, 46 (1986) 1042.
    • (1986) J Neurochem , vol.46 , pp. 1042
    • Martins, R.N.1    Harper, C.G.2    Stokes, G.B.3    Masters, C.L.4
  • 186
    • 0026754574 scopus 로고
    • Reactive oxygen species and the central nervous system
    • Halliwell B, Reactive oxygen species and the central nervous system, J Neurochem, 59 (1992) 1609.
    • (1992) J Neurochem , vol.59 , pp. 1609
    • Halliwell, B.1
  • 187
    • 33646796790 scopus 로고
    • Free radical theory of aging: A hypothesis on pathogenesis of senile dementia of the Alzheimer's type
    • Harman D, Free radical theory of aging: a hypothesis on pathogenesis of senile dementia of the Alzheimer's type, Age, 16 (1993) 23.
    • (1993) Age , vol.16 , pp. 23
    • Harman, D.1
  • 188
    • 0027937548 scopus 로고
    • Oxidative stress: Free radical production in neuronal degeneration
    • Gotz M E, Kunig G, Riederer P, & Youdim M B H, Oxidative stress: free radical production in neuronal degeneration, Pharmacol Ther, 63 (1994) 37.
    • (1994) Pharmacol Ther , vol.63 , pp. 37
    • Gotz, M.E.1    Kunig, G.2    Riederer, P.3    Youdim, M.B.H.4
  • 189
    • 0028152717 scopus 로고
    • Oxidative damage to mitochondrial DNA is increased in Allzheimer's disease
    • Mecocci P, MacGarvey U & Beal M F, Oxidative damage to mitochondrial DNA is increased in Allzheimer's disease, Ann Neurol, 36 (1994) 747.
    • (1994) Ann Neurol , vol.36 , pp. 747
    • Mecocci, P.1    MacGarvey, U.2    Beal, M.F.3
  • 190
    • 0029266603 scopus 로고
    • Free radical mechanisms in dementia of Alzheimer type and the potential for anntioxidative treatment
    • Froelich L & Riederer P, Free radical mechanisms in dementia of Alzheimer type and the potential for anntioxidative treatment, Arzneimittelforschung Drug Res, 45 (1995) 443.
    • (1995) Arzneimittelforschung Drug Res , vol.45 , pp. 443
    • Froelich, L.1    Riederer, P.2
  • 192
    • 0028064502 scopus 로고
    • Involvement of free oxygen radixcals in ß-amyloidosis: An hypothesis
    • Friedlich A L & Butcher L L, Involvement of free oxygen radixcals in ß-amyloidosis: an hypothesis, Neurobiol Aging, 15 (1993) 443.
    • (1993) Neurobiol Aging , vol.15 , pp. 443
    • Friedlich, A.L.1    Butcher, L.L.2
  • 193
    • 0028128386 scopus 로고
    • Free radicals, proteolysis and the degeneration of neurons in Alzheimer disaese: How essential is the ß-amyloid link?
    • Nixon R A & Cataldo A M, Free radicals, proteolysis and the degeneration of neurons in Alzheimer disaese: how essential is the ß-amyloid link? Neurobiol Aging,15 (1994) 463.
    • (1994) Neurobiol Aging , vol.15 , pp. 463
    • Nixon, R.A.1    Cataldo, A.M.2
  • 194
    • 0002792366 scopus 로고
    • Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: Identification as the microtubule-associated protein tau
    • Goedert M, Wischik C, Crowther R, Walker J & Klug A, Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau, Proc Natl Acad Sci USA, 85 (1988) 4051.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4051
    • Goedert, M.1    Wischik, C.2    Crowther, R.3    Walker, J.4    Klug, A.5
  • 195
    • 0026539331 scopus 로고
    • Alzheimer's disease: A cell biological perspective
    • Kosik K, Alzheimer's disease: A cell biological perspective, Science, 256 (1993) 780.
    • (1993) Science , vol.256 , pp. 780
    • Kosik, K.1
  • 196
    • 0027731224 scopus 로고
    • Biochemical and anatomical redistribution of tau protein in Alzheimer's disease
    • Mukaetova-Ladinska E, Harrington C, Roth M & Wischik C, Biochemical and anatomical redistribution of tau protein in Alzheimer's disease, Am J Pathol, 143 (1993) 565.
    • (1993) Am J Pathol , vol.143 , pp. 565
    • Mukaetova-Ladinska, E.1    Harrington, C.2    Roth, M.3    Wischik, C.4
  • 200
    • 84855303577 scopus 로고
    • Oxygen free radicals and brain dysfunction
    • Jesberger J A & Richardson J S, Oxygen free radicals and brain dysfunction, Int J Neurosci, 57 (1991) 1.
    • (1991) Int J Neurosci , vol.57 , pp. 1
    • Jesberger, J.A.1    Richardson, J.S.2
  • 202
    • 0028963114 scopus 로고
    • Oxygen free radicals and human disease
    • Martinez-Cayuela M, Oxygen free radicals and human disease, Biochimie, 77 (1995) 147.
    • (1995) Biochimie , vol.77 , pp. 147
    • Martinez-Cayuela, M.1
  • 203
    • 0018873520 scopus 로고
    • Time-temperature relationships for heat-induced killing of mammalian cells
    • Henle K J & Dethlefsen L A, Time-temperature relationships for heat-induced killing of mammalian cells, Ann N Y Acad Sci, 335 (1980) 234.
    • (1980) Ann N Y Acad Sci , vol.335 , pp. 234
    • Henle, K.J.1    Dethlefsen, L.A.2
  • 204
    • 0021776417 scopus 로고
    • The heat shock response
    • Craig E A, The heat shock response, CRC Crit Rev Biochem, 18(3) (1985) 239.
    • (1985) CRC Crit Rev Biochem , vol.18 , Issue.3 , pp. 239
    • Craig, E.A.1
  • 206
    • 8544240980 scopus 로고
    • edited by J Overgaard (Taylor & Francis, London)
    • Burdon R H in Hyperthermie oncology, edited by J Overgaard (Taylor & Francis, London) 1984, 223
    • (1984) Hyperthermie Oncology , pp. 223
    • Burdon, R.H.1
  • 208
    • 0006198640 scopus 로고
    • Hydrogen peroxide-inducible proteins in Salmonella typhimurium overlap with heat shock and other stress proteins
    • Morgan R W, Chritsman M F, Jacobson F S, Story G & Ames B N, Hydrogen peroxide-inducible proteins in Salmonella typhimurium overlap with heat shock and other stress proteins, Proc Natl Acad Sci USA, 83 (1986) 8063.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8063
    • Morgan, R.W.1    Chritsman, M.F.2    Jacobson, F.S.3    Story, G.4    Ames, B.N.5
  • 209
    • 0021930684 scopus 로고
    • Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium
    • Christman M F, Morgan R W, Jacobson F S & Ames B N, Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium, Cell, 41 (1985) 753.
    • (1985) Cell , vol.41 , pp. 753
    • Christman, M.F.1    Morgan, R.W.2    Jacobson, F.S.3    Ames, B.N.4
  • 210
    • 0021846801 scopus 로고
    • Superoxide dismutase levels in Chinese hamster ovary cells and ovarian carcinoma cells after hyperthermia or exposure to cycloheximide
    • Loven D P, Leeper D B & Oberley LW, Superoxide dismutase levels in Chinese hamster ovary cells and ovarian carcinoma cells after hyperthermia or exposure to cycloheximide, Cancer Res, 45 (1985) 3029.
    • (1985) Cancer Res , vol.45 , pp. 3029
    • Loven, D.P.1    Leeper, D.B.2    Oberley, L.W.3
  • 211
    • 0018098206 scopus 로고
    • Effect of antabuse (disulfiram) on Rous sarcoma virus and on eukaryotic cells
    • Levinson W, Mikelens P, Oppermann H & Jackson J, Effect of antabuse (disulfiram) on Rous sarcoma virus and on eukaryotic cells, Biochem Biophys Acta, 519 (1978) 65.
    • (1978) Biochem Biophys Acta , vol.519 , pp. 65
    • Levinson, W.1    Mikelens, P.2    Oppermann, H.3    Jackson, J.4
  • 212
    • 0023279376 scopus 로고
    • Antioxidant enzymes and survival of normal and simian virus 40-transformed mouse embryo cells after hyperthermia
    • Omar R A, Yano S & Kikkawa Y, Antioxidant enzymes and survival of normal and simian virus 40-transformed mouse embryo cells after hyperthermia, Cancer Res, 47(13) (1987) 3473.
    • (1987) Cancer Res , vol.47 , Issue.13 , pp. 3473
    • Omar, R.A.1    Yano, S.2    Kikkawa, Y.3
  • 213
    • 0022994270 scopus 로고
    • Superoxide dismutase: Rationale for use in reperfusion injury and inflammation
    • McCord J M, Superoxide dismutase: rationale for use in reperfusion injury and inflammation, J Free Radic Biol Med, 2 (1986) 325.
    • (1986) J Free Radic Biol Med , vol.2 , pp. 325
    • McCord, J.M.1
  • 214
    • 0023845333 scopus 로고
    • Rugulation of the synthesis of superoxide dismutases in rat lungs during oxidant and hyperthermic stresses
    • Hass M A & Massaro D, Rugulation of the synthesis of superoxide dismutases in rat lungs during oxidant and hyperthermic stresses, J Biol Chem, 263 (1989) 776.
    • (1989) J Biol Chem , vol.263 , pp. 776
    • Hass, M.A.1    Massaro, D.2
  • 215
    • 0023746618 scopus 로고
    • Heat shock response is associated with enhanced postichemic ventricular recovery
    • Currie R W, Karmazyn M, Kloc M & Mailer K, Heat shock response is associated with enhanced postichemic ventricular recovery, Circ Res, 63 (1988) 543.
    • (1988) Circ Res , vol.63 , pp. 543
    • Currie, R.W.1    Karmazyn, M.2    Kloc, M.3    Mailer, K.4
  • 216
    • 0019073929 scopus 로고
    • The metabolic fate of mitochondrial hydrogen peroxide
    • Nohl H & Jordan W, The metabolic fate of mitochondrial hydrogen peroxide, Int J Biochem, 111 (1980) 203.
    • (1980) Int J Biochem , vol.111 , pp. 203
    • Nohl, H.1    Jordan, W.2
  • 218
    • 0025145831 scopus 로고
    • Acquisition and decay of heat shock enhanced post ischemic ventricular recovery
    • Karmazyn M, Mailer K & Vurrie R W, Acquisition and decay of heat shock enhanced post ischemic ventricular recovery, Am J Physiol, 259 (1990) H424.
    • (1990) Am J Physiol , vol.259
    • Karmazyn, M.1    Mailer, K.2    Vurrie, R.W.3
  • 221
    • 34250561475 scopus 로고
    • A new puffing pattern induced by temperature shock and DNP in Drosophila
    • Ritossa F, A new puffing pattern induced by temperature shock and DNP in Drosophila, Experimentia, 18 (1962) 571.
    • (1962) Experimentia , vol.18 , pp. 571
    • Ritossa, F.1
  • 222
    • 0027333423 scopus 로고
    • Role of the major heat shock proteins as molecular chaperones
    • Georgopoulos C & Welch W J, Role of the major heat shock proteins as molecular chaperones, Annu Rev Cell Biol, 9 (1993) 601.
    • (1993) Annu Rev Cell Biol , vol.9 , pp. 601
    • Georgopoulos, C.1    Welch, W.J.2
  • 223
    • 0025777354 scopus 로고
    • Heat shock, stress proteins, chaperones proteoxicity
    • Hightower L E, Heat shock, stress proteins, chaperones proteoxicity, Cell, 66 (1991) 191.
    • (1991) Cell , vol.66 , pp. 191
    • Hightower, L.E.1
  • 224
    • 84934438837 scopus 로고    scopus 로고
    • Protein misassembly: Macromolecular crowding and molecular chaperones
    • Ellis R J, Protein misassembly: macromolecular crowding and molecular chaperones, Adv Exp Med Biol, 594 (2007) 1.
    • (2007) Adv Exp Med Biol , vol.594 , pp. 1
    • Ellis, R.J.1
  • 225
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but underappreciated
    • Ellis R J, Macromolecular crowding: Obvious but underappreciated, Trends Biochem Sci, 26 (2001) 597.
    • (2001) Trends Biochem Sci , vol.26 , pp. 597
    • Ellis, R.J.1
  • 226
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • Lashuel H A, Hartley D, Petre B M, et al., Neurodegenerative disease: Amyloid pores from pathogenic mutations, Nature, 418 (2002) 291.
    • (2002) Nature , vol.418 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3
  • 227
    • 0034705224 scopus 로고    scopus 로고
    • Polyglutamine aggregates alter protein folding homeostasis in Caenorhabditis ellegans
    • Satyal S H, Schmidt E, Kitagawa K, et al., Polyglutamine aggregates alter protein folding homeostasis in Caenorhabditis ellegans, Proc.Natl Acad Sci USA, 97 (2000) 5750.
    • (2000) Proc.Natl Acad Sci USA , vol.97 , pp. 5750
    • Satyal, S.H.1    Schmidt, E.2    Kitagawa, K.3
  • 228
    • 0037147221 scopus 로고    scopus 로고
    • Proteinaceous infectious behavior in nonpathogenic proteins is controlled by molecular chapperones
    • Ben-Zvi A P & Goloubinoff P, Proteinaceous infectious behavior in nonpathogenic proteins is controlled by molecular chapperones, J Biol Chem, 277 (2002) 49422.
    • (2002) J Biol Chem , vol.277 , pp. 49422
    • Ben-Zvi, A.P.1    Goloubinoff, P.2
  • 229
    • 0035029482 scopus 로고    scopus 로고
    • Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol
    • Tomoyasu T, Mogk A, Laangen H, et al., Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol, Mol Microbiol, 40 (2001) 397.
    • (2001) Mol Microbiol , vol.40 , pp. 397
    • Tomoyasu, T.1    Mogk, A.2    Laangen, H.3
  • 230
    • 0025382832 scopus 로고
    • Nucleoplasmin: The archetypal molecular chaperone
    • Dingwall C & Lasky R A, Nucleoplasmin: The archetypal molecular chaperone, Semin Cell Biol, 1 (1990) 11.
    • (1990) Semin Cell Biol , vol.1 , pp. 11
    • Dingwall, C.1    Lasky, R.A.2
  • 231
    • 0030224998 scopus 로고    scopus 로고
    • Discovery of molecular chaperones
    • Ellis R J, Discovery of molecular chaperones, Cell Stress Chaperones, 1 (1996) 155.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 155
    • Ellis, R.J.1
  • 232
    • 0033617534 scopus 로고    scopus 로고
    • Chaperonin function: Folding by forced unfolding
    • Shtilerman M, Lorimer G H & Englander S W, Chaperonin function: Folding by forced unfolding, Science, 284 (1999) 822.
    • (1999) Science , vol.284 , pp. 822
    • Shtilerman, M.1    Lorimer, G.H.2    Englander, S.W.3
  • 233
    • 0035783169 scopus 로고    scopus 로고
    • Review: Mechanisms of disaggregation and refolding of stable protein aggregation by molecular chaperones
    • Ben-zvi A P & Goloubinoff P, Review: Mechanisms of disaggregation and refolding of stable protein aggregation by molecular chaperones, J Struct Biol, 135 (2001) 84.
    • (2001) J Struct Biol , vol.135 , pp. 84
    • Ben-zvi, A.P.1    Goloubinoff, P.2
  • 234
    • 25844466597 scopus 로고    scopus 로고
    • Heat shock response modulators as therapeutic tools for diseases of protein conformation
    • Westerheide S D & Morimoto R I, Heat shock response modulators as therapeutic tools for diseases of protein conformation, J Biol Chem, 280 (2005) 33097.
    • (2005) J Biol Chem , vol.280 , pp. 33097
    • Westerheide, S.D.1    Morimoto, R.I.2
  • 235
    • 0034671267 scopus 로고    scopus 로고
    • From minichaperone to GroEL 2: Importance of avidity of the multisiti ring structure
    • Chatellier J, Hill F & Fersht A.R, From minichaperone to GroEL 2: Importance of avidity of the multisiti ring structure, J Mol Biol, 304 (2000) 883.
    • (2000) J Mol Biol , vol.304 , pp. 883
    • Chatellier, J.1    Hill, F.2    Fersht, A.R.3
  • 236
    • 0033573135 scopus 로고    scopus 로고
    • Identification of thermolabile Eschericchia coli proteins, Prevention and reversion of aggregation by DnaK and ClpB
    • Mogk A, Tomoyasu T, Goloubinoff P, Rüdiger S, Röder D, Langen H & Bukau B, Identification of thermolabile Eschericchia coli proteins, Prevention and reversion of aggregation by DnaK and ClpB, EMBO J, 18 (1999) 6934.
    • (1999) EMBO J , vol.18 , pp. 6934
    • Mogk, A.1    Tomoyasu, T.2    Goloubinoff, P.3    Rüdiger, S.4    Röder, D.5    Langen, H.6    Bukau, B.7
  • 237
    • 0024820705 scopus 로고
    • Reconsstition of active dimeric ribulose bisphosphatechaperonin proteins and Mg-ATP
    • Goloubinoff P, Christeller J T, Gatennby A A, et al., Reconsstition of active dimeric ribulose bisphosphatechaperonin proteins and Mg-ATP, Nature, 342 (1989) 884.
    • (1989) Nature , vol.342 , pp. 884
    • Goloubinoff, P.1    Christeller, J.T.2    Gatennby, A.A.3
  • 238
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaaperone network
    • Goloubinoff P, Moggk A, Zvi A P, et al., Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaaperone network, Proc Natl Acad Sci USA, 96 (1999) 13732.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13732
    • Goloubinoff, P.1    Moggk, A.2    Zvi, A.P.3
  • 239
    • 0030347863 scopus 로고    scopus 로고
    • Revisiting the anfinsen cage
    • Ellis R J, Revisiting the Anfinsen cage, Folding and Design, 1 (1996) R9.
    • (1996) Folding and Design , vol.1
    • Ellis, R.J.1
  • 240
    • 34147102801 scopus 로고    scopus 로고
    • Molecular chaperonesn and proteases: Cellular fold-controlling factors of proteins in neurodegenerative diseases and aging
    • (In Press)
    • Hinault M P & Goloubinoff P, Molecular chaperonesn and proteases: Cellular fold-controlling factors of proteins in neurodegenerative diseases and aging, J Mol Neurosci, (2006) (In Press).
    • (2006) J Mol Neurosci
    • Hinault, M.P.1    Goloubinoff, P.2
  • 241
    • 0034630346 scopus 로고    scopus 로고
    • Age-related alterations in the activation of heat shock transcription factor 1 in rat hepatocytes
    • Heydari A R, You S, Takahashi R, et al., Age-related alterations in the activation of heat shock transcription factor 1 in rat hepatocytes, Exp Cell Res, 256 (2000) 83.
    • (2000) Exp Cell Res , vol.256 , pp. 83
    • Heydari, A.R.1    You, S.2    Takahashi, R.3
  • 242
    • 0142186172 scopus 로고    scopus 로고
    • Aging and molecular chaperones
    • Soti C & Csermely P, Aging and molecular chaperones, Exp Gerontol, 38 (2003) 1037.
    • (2003) Exp Gerontol , vol.38 , pp. 1037
    • Soti, C.1    Csermely, P.2
  • 243
    • 0034253474 scopus 로고    scopus 로고
    • Negative regulation of the Apaf-1 apoptosome by HSP70
    • Saleh A, Srinivasula S M, Balkir L, et al., Negative regulation of the Apaf-1 apoptosome by HSP70, Natl Cell Biol, 2 (2000) 476.
    • (2000) Natl Cell Biol , vol.2 , pp. 476
    • Saleh, A.1    Srinivasula, S.M.2    Balkir, L.3
  • 244
    • 28744444484 scopus 로고    scopus 로고
    • Induction of HSP70 expression and recruitment of HSC70 and HSP70 in the nucleus reduce aggregation of a polyalanine expansion mutant of PABPN1 in HeLa cells
    • Waang Q, Mosser D D & Bag J, Induction of HSP70 expression and recruitment of HSC70 and HSP70 in the nucleus reduce aggregation of a polyalanine expansion mutant of PABPN1 in HeLa cells, Hum Mol Genet,14 (2005) 3673.
    • (2005) Hum Mol Genet , vol.14 , pp. 3673
    • Waang, Q.1    Mosser, D.D.2    Bag, J.3
  • 245
    • 19944426695 scopus 로고    scopus 로고
    • Celastrols as inducers of the heat shock response and cytoprotection
    • Westerheide S D, Bosman J D, Mbadugha B N, et al., Celastrols as inducers of the heat shock response and cytoprotection, J Biol Chem, 279 (2004) 566053.
    • (2004) J Biol Chem , vol.279 , pp. 566053
    • Westerheide, S.D.1    Bosman, J.D.2    Mbadugha, B.N.3
  • 246
    • 20344378481 scopus 로고    scopus 로고
    • Resveratrol: Preventtingg properties agaainst vascular alterations and ageing
    • Delmas D, Jannin B & Latruffe N, Resveratrol: Preventtingg properties agaainst vascular alterations and ageing, Mol Nutr Food Res, 49 (2005) 377.
    • (2005) Mol Nutr Food Res , vol.49 , pp. 377
    • Delmas, D.1    Jannin, B.2    Latruffe, N.3
  • 247
    • 0035834026 scopus 로고    scopus 로고
    • Single oral dose of genanylgeranylacetone induces heat-shock prrotein 72 and renders protection against ischemia/reperfusion injury in rat heart
    • Ooie T, Takkaahhashi N & Saikawa T, Single oral dose of genanylgeranylacetone induces heat-shock prrotein 72 and renders protection against ischemia/reperfusion injury in rat heart, Circulation, 1104 (2001) 1837.
    • (2001) Circulation , vol.1104 , pp. 1837
    • Ooie, T.1    Takkaahhashi, N.2    Saikawa, T.3
  • 248
    • 0036893153 scopus 로고    scopus 로고
    • Sciennce review: Redox and oxygen-sensitive transcription factors in the regulation of oxidant-mediated lung injury: Role for nuclear factor-kappaB
    • Haddad J J, Sciennce review: Redox and oxygen-sensitive transcription factors in the regulation of oxidant-mediated lung injury: Role for nuclear factor-kappaB, Crit Care, 6 (2002) 481.
    • (2002) Crit Care , vol.6 , pp. 481
    • Haddad, J.J.1
  • 250
    • 0031594166 scopus 로고    scopus 로고
    • A mathematical model of the HSP70 regulation in the cell
    • Lopez-Neblina F, Toledo A.H & Toledo-Pereyra L H, Molecular biology of apoptosis in ischemia and reperfusion, J Invest Surg, 18 (2005) 335. 246 Peper A, Grimbergen C A, Spaan J A E, Souren J E M & Van Wijk R, A mathematical model of the HSP70 regulation in the cell, Int J Hyperthermia 14 (1998) 97.
    • (1998) Int J Hyperthermia , vol.14 , pp. 97
    • Peper A1    Grimbergen, C.A.2    Spaan, J.A.E.3    Souren, J.E.M.4    Van Wijk, R.5
  • 251
    • 33846924300 scopus 로고    scopus 로고
    • How many transcription factors does it take to turn on the heme oxygenase-1 gene?
    • Alam J & Cook J L, How many transcription factors does it take to turn on the heme oxygenase-1 gene? Am J Respir Cell Mol Biol, 36 (2007) 166.
    • (2007) Am J Respir Cell Mol Biol , vol.36 , pp. 166
    • Alam, J.1    Cook, J.L.2
  • 252
    • 0028054189 scopus 로고
    • Stressor-specific induction of heat shock proteins in rat hepatoma cells
    • Wiegant F A C, Souren J E M, Van Rijn J & Van Wijk R, Stressor-specific induction of heat shock proteins in rat hepatoma cells, Toxicology 94 (1994) 143.
    • (1994) Toxicology , vol.94 , pp. 143
    • Wiegant, F.A.C.1    Souren, J.E.M.2    Van Rijn, J.3    Van Wijk, R.4
  • 253
    • 0030886054 scopus 로고    scopus 로고
    • Reduced stress defense in heme oxygenase 1-deficient cells
    • Poss K D & Tonegawa S, Reduced stress defense in heme oxygenase 1-deficient cells, Proc Natl Acad Sci USA, 94 (1997) 10925.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10925
    • Poss, K.D.1    Tonegawa, S.2
  • 254
    • 4544272023 scopus 로고    scopus 로고
    • The heme oxygenase system: Past, present and future
    • Maines M D, The heme oxygenase system: past, present and future, Antioxid Redox Signal, 6 (2004) 797.
    • (2004) Antioxid Redox Signal , vol.6 , pp. 797
    • Maines, M.D.1
  • 255
    • 33645945014 scopus 로고    scopus 로고
    • Heme oxygenase-1/carbon monoxide: From basic science to therapeutic application
    • Ryter S, Alam J & Choi A M, Heme oxygenase-1 / carbon monoxide: from basic science to therapeutic application, Physiol Rev, 85 (2006) 583.
    • (2006) Physiol Rev , vol.85 , pp. 583
    • Ryter, S.1    Alam, J.2    Choi, A.M.3
  • 256
    • 33845613215 scopus 로고    scopus 로고
    • The heme catabolic pathway and its protective effects on oxidative stress-mediated diseases
    • Vitek L & Schwertner H A, The heme catabolic pathway and its protective effects on oxidative stress-mediated diseases, Adv Clin Chem, 43 (2007) 1.
    • (2007) Adv Clin Chem , vol.43 , pp. 1
    • Vitek, L.1    Schwertner, H.A.2
  • 259
    • 8544257019 scopus 로고    scopus 로고
    • Heme oxygenase expression in human central nervous disorders
    • Schipper H M, Heme oxygenase expression in human central nervous disorders, Free Radical Biol Med, 37 (2004) 1995.
    • (2004) Free Radical Biol Med , vol.37 , pp. 1995
    • Schipper, H.M.1
  • 260
    • 0032819013 scopus 로고    scopus 로고
    • Stimulation of survival capacity in heat shocked cells by subsequent exposure to minute amounts of chemical stressors; role of similarity in HSP-inducing effects
    • Wiegant F A C, Souren J E M & Van Wijk R, Stimulation of survival capacity in heat shocked cells by subsequent exposure to minute amounts of chemical stressors; role of similarity in HSP-inducing effects, Hum Exp Toxicol, 18 (1999) 460.
    • (1999) Hum Exp Toxicol , vol.18 , pp. 460
    • Wiegant, F.A.C.1    Souren, J.E.M.2    Van Wijk, R.3
  • 261
    • 0031761706 scopus 로고    scopus 로고
    • Protein precipitation: A common etiology in neurodegenerative disorders?
    • Kakizuka A, Protein precipitation: A common etiology in neurodegenerative disorders? Trends Genet, 14 (1998) 396.
    • (1998) Trends Genet , vol.14 , pp. 396
    • Kakizuka, A.1
  • 263
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani M & Dobson C M, Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution, J Mol Med, 81 (2003) 678.
    • (2003) J Mol Med , vol.81 , pp. 678
    • Stefani, M.1    Dobson, C.M.2
  • 265
    • 0035237310 scopus 로고    scopus 로고
    • Protein folding and its links with human disease
    • Dobson C.M, Protein folding and its links with human disease, Biochem Soc Symp, 68 (2001) 1.
    • (2001) Biochem Soc Symp , vol.68 , pp. 1
    • Dobson, C.M.1
  • 268
    • 0036186384 scopus 로고    scopus 로고
    • Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum
    • Fassio A & Sitia R, Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum, Histochem Cell Biol, 117 (2002) 151.
    • (2002) Histochem Cell Biol , vol.117 , pp. 151
    • Fassio, A.1    Sitia, R.2
  • 269
    • 4444236143 scopus 로고    scopus 로고
    • Peroxynitrite and vascular endothelial dysfunction in diabetes mellitus
    • Zou M H, Cohen R & Ullrich V, Peroxynitrite and vascular endothelial dysfunction in diabetes mellitus. Endothelium 2004; 11:89-9.
    • (2004) Endothelium , vol.11 , pp. 89-90
    • Zou, M.H.1    Cohen, R.2    Ullrich, V.3
  • 270
    • 0034676477 scopus 로고    scopus 로고
    • Nitric oxide and neuronal and pancreatic beta cell death
    • Adeghate E, Parvez SH. Nitric oxide and neuronal and pancreatic beta cell death, Toxicology, 153 (2000) 143.
    • (2000) Toxicology , vol.153 , pp. 143
    • Adeghate, E.1    Parvez, S.H.2
  • 271
    • 0034676477 scopus 로고    scopus 로고
    • Nitric oxide and neuronal pancreatic beta cell death
    • Adeghate E & Parvez S H, Nitric oxide and neuronal pancreatic beta cell death, Toxicology, 153 (2000) 143.
    • (2000) Toxicology , vol.153 , pp. 143
    • Adeghate, E.1    Parvez, S.H.2
  • 272
    • 0035668056 scopus 로고    scopus 로고
    • Diabetes-associated nitration of tyrosine and inactivation of succinyl-CoA:3- oxoacid CoA-transferase
    • Turko I V, Marcondes S & Murad F, Diabetes-associated nitration of tyrosine and inactivation of succinyl-CoA:3- oxoacid CoA-transferase, Am J Physiol Heart Circ Physiol, 281 (2001) H2289.
    • (2001) Am J Physiol Heart Circ Physiol , vol.281
    • Turko, I.V.1    Marcondes, S.2    Murad, F.3
  • 273
    • 0036632466 scopus 로고    scopus 로고
    • Islet redox stress: The manifold toxicities of insulin resistance, metabolic syndrome and amylin derived islet amyloid in type 2 diabetes mellitus
    • Hayden M R & Tyagi S C, Islet redox stress: the manifold toxicities of insulin resistance, metabolic syndrome and amylin derived islet amyloid in type 2 diabetes mellitus, JOP J Pancreas, 3 (2002) 86.
    • (2002) JOP J Pancreas , vol.3 , pp. 86
    • Hayden, M.R.1    Tyagi, S.C.2
  • 274
    • 3442884258 scopus 로고    scopus 로고
    • Molecular and cellular basis of the aetiology and management of diabetic cardiomyopathy: A short review
    • Adeghate E, Molecular and cellular basis of the aetiology and management of diabetic cardiomyopathy: a short review, Mol Cell Biochem, 261 (2004) 187.
    • (2004) Mol Cell Biochem , vol.261 , pp. 187
    • Adeghate, E.1
  • 275
    • 1342346538 scopus 로고    scopus 로고
    • Nitrosative injury and antioxidant therapy in the management of diabetic neuropathy
    • Cowell R M & Russell J W, Nitrosative injury and antioxidant therapy in the management of diabetic neuropathy, J Investig Med, 52 (2004) 33.
    • (2004) J Investig Med , vol.52 , pp. 33
    • Cowell, R.M.1    Russell, J.W.2
  • 276
    • 0042822112 scopus 로고    scopus 로고
    • Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: Evidence for role ofislet amyloid formation rather than direct action of amyloid
    • Butler A E, Janson J, Soeller W C & Butler P C, Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role ofislet amyloid formation rather than direct action of amyloid, Diabetes, 52 (2003) 2304.
    • (2003) Diabetes , vol.52 , pp. 2304
    • Butler, A.E.1    Janson, J.2    Soeller, W.C.3    Butler, P.C.4
  • 277
    • 0033048453 scopus 로고    scopus 로고
    • The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic a myloid particles
    • Janson J, Ashley R H, Harrison D, McIntyre S & Butler P C, The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic a myloid particles, Diabetes, 48 (1999) 491.
    • (1999) Diabetes , vol.48 , pp. 491
    • Janson, J.1    Ashley, R.H.2    Harrison, D.3    McIntyre, S.4    Butler, P.C.5
  • 278
    • 0038015599 scopus 로고    scopus 로고
    • Replication increases beta-cell vulnerability to human islet amyloid polypeptide-induced apoptosis
    • Ritzel R A & Butler P C, Replication increases beta-cell vulnerability to human islet amyloid polypeptide-induced apoptosis, Diabetes, 52 (2003) 1701.
    • (2003) Diabetes , vol.52 , pp. 1701
    • Ritzel, R.A.1    Butler, P.C.2
  • 279
    • 0032969276 scopus 로고    scopus 로고
    • Islet amyloid: A long-recognized but underappreciated pathological feature of type 2 diabetes
    • Kahn S E, Andrikopoulos S & Verchere C B, Islet amyloid: a long-recognized but underappreciated pathological feature of type 2 diabetes, Diabetes, 48 (1999) 241.
    • (1999) Diabetes , vol.48 , pp. 241
    • Kahn, S.E.1    Andrikopoulos, S.2    Verchere, C.B.3
  • 280
    • 2542581025 scopus 로고    scopus 로고
    • Diabetes due to a progressive defect in beta-cell mass in rats transgenic for human islet amyloid polypeptide (HIP Rat): A new model for type 2
    • Butler A E, Jang J, Gurlo T, Carty M D, Soeller W C & Butler P Cl, Diabetes due to a progressive defect in beta-cell mass in rats transgenic for human islet amyloid polypeptide (HIP Rat): a new model for type 2, Diabetes, 53 (2004) 1509.
    • (2004) Diabetes , vol.53 , pp. 1509
    • Butler, A.E.1    Jang, J.2    Gurlo, T.3    Carty, M.D.4    Soeller, W.C.5    Butler, P.C.6
  • 281
    • 0035411025 scopus 로고    scopus 로고
    • 'A' is for amylin and amyloid in type 2 diabetes mellitus
    • Hayden M R & Tyagi S C, 'A' is for amylin and amyloid in type 2 diabetes mellitus, JOP J Pancreas, 2 (2001) 124-139
    • (2001) JOP J Pancreas , vol.2 , pp. 124-139
    • Hayden, M.R.1    Tyagi, S.C.2
  • 283
    • 0030581498 scopus 로고    scopus 로고
    • Mitochondrial oxidative phosphorylation changes in the life span. Molecular aspects and physiopathological implications
    • Papa S, Mitochondrial oxidative phosphorylation changes in the life span. Molecular aspects and physiopathological implications, Biochim Biophys Acta,1276 (1996) 87.
    • (1996) Biochim Biophys Acta , vol.1276 , pp. 87
    • Papa, S.1
  • 284
    • 2542505678 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial DNA mutations in human aging
    • 279 Wei Y H, Oxidative stress and mitochondrial DNA mutations in human aging, Proc Soc Exp Biol Med, 217 (1998) 53.
    • (1998) Proc Soc Exp Biol Med , vol.217 , pp. 53
    • Wei, Y.H.1
  • 285
    • 0026023219 scopus 로고
    • Hydrogen peroxide release by mitochondria increases during aging
    • Sohal R S & Sohal B H, Hydrogen peroxide release by mitochondria increases during aging, Mech Aging Dev, 57 (1991) 187.
    • (1991) Mech Aging Dev , vol.57 , pp. 187
    • Sohal, R.S.1    Sohal, B.H.2
  • 287
    • 0029147191 scopus 로고
    • Mitochondrial superoxide and hydrogen peroxide generation, protein oxidative damage and longevity in different species of flies
    • Sohal R S, Sohal B H. & Orr W C, Mitochondrial superoxide and hydrogen peroxide generation, protein oxidative damage and longevity in different species of flies, Free Radical Biol. Med, 19 (1995) 499.
    • (1995) Free Radical Biol. Med , vol.19 , pp. 499
    • Sohal, R.S.1    Sohal, B.H.2    Orr, W.C.3
  • 288
    • 0032429396 scopus 로고    scopus 로고
    • Aging- and smoking-associated alteration in the relative content in human lung
    • Lee H C, Lu C Y, Fahn H J & Wei Y H, Aging- and smoking-associated alteration in the relative content in human lung, FEBS Lett, 441 (1998) 292.
    • (1998) FEBS Lett , vol.441 , pp. 292
    • Lee, H.C.1    Lu, C.Y.2    Fahn, H.J.3    Wei, Y.H.4
  • 290
    • 0033557111 scopus 로고    scopus 로고
    • Concurrent increase of oxidative DNA damage and lipid peroxidation together with mitochondrial DNA mutation in human lung tissues during aging-smoking enhances oxidative stress on the aged tissues
    • Lee H C, Lim M L R, Lu C Y, Liu V W S, Fahn H J, Zhang C, Nagley P & Wei Y H, Concurrent increase of oxidative DNA damage and lipid peroxidation together with mitochondrial DNA mutation in human lung tissues during aging-smoking enhances oxidative stress on the aged tissues, Arch Biochem Biophys, 362 (1999) 309.
    • (1999) Arch Biochem Biophys , vol.362 , pp. 309
    • Lee, H.C.1    Lim, M.L.R.2    Lu, C.Y.3    Liu, V.W.S.4    Fahn, H.J.5    Zhang, C.6    Nagley, P.7    Wei, Y.H.8
  • 291
    • 0029762274 scopus 로고    scopus 로고
    • Simultaneous increase of mitochondrial DNA deletions and lipid peroxidation in human aging
    • Wei Y H, Kao S H & Lee H C, Simultaneous increase of mitochondrial DNA deletions and lipid peroxidation in human aging, Ann N Y Acad Sci, 786 (1996) 24.
    • (1996) Ann N Y Acad Sci , vol.786 , pp. 24
    • Wei, Y.H.1    Kao, S.H.2    Lee, H.C.3
  • 292
    • 0002026429 scopus 로고
    • Oxidative damage elicited by imbalance of free radical scavenging enzymes is associated with large-scale mtDNA deletions in aging human skin
    • Lu C Y, Lee H C, Fahn H J & Wei Y H, Oxidative damage elicited by imbalance of free radical scavenging enzymes is associated with large-scale mtDNA deletions in aging human skin, Mutat Res, 423 (1991) 11.
    • (1991) Mutat Res , vol.423 , pp. 11
    • Lu, C.Y.1    Lee, H.C.2    Fahn, H.J.3    Wei, Y.H.4
  • 294
    • 0034214103 scopus 로고    scopus 로고
    • Increase of mitochondria and nitochondrial DNA in response to oxidative stress in human cells
    • Lee H C, Yin P H, Lu C Y, Chi C W & Wei Y H, Increase of mitochondria and nitochondrial DNA in response to oxidative stress in human cells, Biochem J, 348 (2000) 425.
    • (2000) Biochem J , vol.348 , pp. 425
    • Lee, H.C.1    Yin, P.H.2    Lu, C.Y.3    Chi, C.W.4    Wei, Y.H.5
  • 295
    • 0037059040 scopus 로고    scopus 로고
    • Chaperoning brain degeneration
    • Bonini N M, Chaperoning brain degeneration, Proc Natl Acad Sci USA, 99 (2002) 16407.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16407
    • Bonini, N.M.1
  • 296
    • 0036850456 scopus 로고    scopus 로고
    • Genetic modulation of polyglutamine toxicity by protein conjugation pathways in Drosophila
    • Chan H Y, Warrick J M, Andriola I, et al., Genetic modulation of polyglutamine toxicity by protein conjugation pathways in Drosophila, Hum Mol Genet, 11 (2002) 2895.
    • (2002) Hum Mol Genet , vol.11 , pp. 2895
    • Chan, H.Y.1    Warrick, J.M.2    Andriola, I.3
  • 297
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and alterred subcellular proteasome localization imply protein misfolding in SCA1
    • Cummings C J, Mancini M A, Antalffy B, et al., Chaperone suppression of aggregation and alterred subcellular proteasome localization imply protein misfolding in SCA1, Nat Genet, (1998) 148.
    • (1998) Nat Genet , vol.148
    • Cummings, C.J.1    Mancini, M.A.2    Antalffy, B.3
  • 298
    • 0028143527 scopus 로고
    • CAC expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1
    • Kawaguchi T, Okamoto T, Taniwaki M, et al., CAC expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1, Nat Genet, 8 (1994) 221.
    • (1994) Nat Genet , vol.8 , pp. 221
    • Kawaguchi, T.1    Okamoto, T.2    Taniwaki, M.3
  • 299
    • 0028216760 scopus 로고
    • Unstable expansion of CAC repeat in hereditary dentatorubral- pallidoluysian atrophy (DRPLA)
    • Koide R, Ikeuchi T, Onodera O, et al., Unstable expansion of CAC repeat in hereditary dentatorubral-pallidoluysian atrophy (DRPLA), Nat Genet, 6 (1994) 9.
    • (1994) Nat Genet , vol.6 , pp. 9
    • Koide R1    Ikeuchi, T.2    Onodera O3
  • 300
    • 0025800526 scopus 로고
    • Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy
    • La Spada A R, Wilson E M, Lubahn D R, et al., Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy, Nature, 352 (1991) 77.
    • (1991) Nature , vol.352 , pp. 77
    • La Spada, A.R.1    Wilson, E.M.2    Lubahn, D.R.3
  • 301
    • 0027164698 scopus 로고
    • Expansion of an unstable trinucleotide CAG repeat in spinocerebellar ataxia type 1
    • Orr H T, Chung M Y, Banfi, et al., Expansion of an unstable trinucleotide CAG repeat in spinocerebellar ataxia type 1, Nat Genet, 4 (1993) 221.
    • (1993) Nat Genet , vol.4 , pp. 221
    • Orr, H.T.1    Chung, M.Y.2    Banfi3
  • 302
    • 0026733343 scopus 로고
    • Linkage and mutational analysis of familial Alzheimer disease kindreds for the APP gene region
    • Kamino K, Orr H T, Payami H, et al., Linkage and mutational analysis of familial Alzheimer disease kindreds for the APP gene region, Am J Hum Genet, 51 (1992) 998.
    • (1992) Am J Hum Genet , vol.51 , pp. 998
    • Kamino, K.1    Orr, H.T.2    Payami, H.3
  • 303
    • 0030703699 scopus 로고    scopus 로고
    • Cu/Zn superoxide dismutase gene mutations in amyotrophic lateral sclerosis: Correlation between genetype and clinical features
    • Laing N G & Siddique T, Cu/Zn superoxide dismutase gene mutations in amyotrophic lateral sclerosis: Correlation between genetype and clinical features, J Neurosurg Psychiatry, 63 (1997) 815.
    • (1997) J Neurosurg Psychiatry , vol.63 , pp. 815
    • Laing, N.G.1    Siddique, T.2
  • 304
    • 0342368772 scopus 로고    scopus 로고
    • Association between early-onset of Parkinson's disease and mutations in the parkin gene, French Parkinson's Disease Genetics Study Group
    • Lucking CB, Durr A, Bonifati V, et al., Association between early-onset of Parkinson's disease and mutations in the parkin gene, French Parkinson's Disease Genetics Study Group, N Engl J Med, 342 (2000) 1560.
    • (2000) N Engl J Med , vol.342 , pp. 1560
    • Lucking, C.B.1    Durr, A.2    Bonifati, V.3
  • 305
    • 17044447638 scopus 로고    scopus 로고
    • Familial Parkinson's disease, Alpha-synuclein and parkin
    • Mizuno Y, Hattori N, Kitada T, et al., Familial Parkinson's disease, Alpha-synuclein and parkin, Adv Neurol, 86 (2001) 13.
    • (2001) Adv Neurol , vol.86 , pp. 13
    • Mizuno, Y.1    Hattori, N.2    Kitada, T.3
  • 306
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the alpha-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos M H, Lavedan C, Leroy E, et al., Mutation in the alpha-synuclein gene identified in families with Parkinson's disease, Science, 2276 (1997) 2045.
    • (1997) Science , vol.2276 , pp. 2045
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3
  • 307
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen D R, Siddique T, Patterson D, et al., Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis, Nature, 362 (1993) 59.
    • (1993) Nature , vol.362 , pp. 59
    • Rosen, D.R.1    Siddique, T.2    Patterson, D.3
  • 308
    • 0037373633 scopus 로고    scopus 로고
    • Dying for a cause: Invertebrate genetics takes on human neurodegeneration
    • Driscoll M & Gerstbrein B, Dying for a cause: Invertebrate genetics takes on human neurodegeneration, Nat Rev Genet, 4 (2003) 181.
    • (2003) Nat Rev Genet , vol.4 , pp. 181
    • Driscoll, M.1    Gerstbrein, B.2
  • 309
    • 0035975702 scopus 로고    scopus 로고
    • Transgenic invertebrate models of age-associated neurodegenerative diseases
    • Link C D, Transgenic invertebrate models of age-associated neurodegenerative diseases, Mech Ageing Dev, 122 (2001) 1639.
    • (2001) Mech Ageing Dev , vol.122 , pp. 1639
    • Link, C.D.1
  • 310
    • 0642336407 scopus 로고    scopus 로고
    • Invertebrate models of neurologic disease: Inssights into pathogenesis and therapy
    • Thompson L M & Marsh J L, Invertebrate models of neurologic disease: Inssights into pathogenesis and therapy, Curr Neurol Neurosci Rep, 3 (2003) 442.
    • (2003) Curr Neurol Neurosci Rep , vol.3 , pp. 442
    • Thompson, L.M.1    Marsh, J.L.2
  • 312
    • 26844459053 scopus 로고    scopus 로고
    • Animal models of Kennedy disease
    • Merry D E, Animal models of Kennedy disease, NeuroRx, 2 (2005) 471.
    • (2005) NeuroRx , vol.2 , pp. 471
    • Merry, D.E.1
  • 313
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross C A & Poirier M A, Protein aggregation and neurodegenerative disease, Nat Med, 10 (2004) S10.
    • (2004) Nat Med , vol.10
    • Ross C.A1    Poirier, M.A.2
  • 314
    • 70349476002 scopus 로고    scopus 로고
    • The stress of misfolded proteins: C. elegans models for neurodegenerative disease and aging,disease and aging
    • edited by P Csermely & L Vígh (Springer, New York)
    • Brignull, H.R., Morley J.F., Morimoto R.I. The stress of misfolded proteins: C. elegans models for neurodegenerative disease and aging, disease and aging, in Molecular aspects of the stress response: Chaperones, Membranes and Networks, edited by P Csermely & L Vígh (Springer, New York) 2006, 167.
    • (2006) Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks , vol.167
    • Brignull, H.R.1    Morley, J.F.2    Morimoto, R.I.3
  • 315
    • 0036021375 scopus 로고    scopus 로고
    • Genetic analysis of tissue aging in Caenorhabditis elegans; A role for heat-shock factor and bacterial proliferation
    • Garigan D, Hsu A L, Fraser A G, et al., Genetic analysis of tissue aging in Caenorhabditis elegans; A role for heat-shock factor and bacterial proliferation, Genetics, 161 (2002) 1101.
    • (2002) Genetics , vol.161 , pp. 1101
    • Garigan, D.1    Hsu, A.L.2    Fraser, A.G.3
  • 316
    • 0038701745 scopus 로고    scopus 로고
    • Regulation of aging and age-related disease by DAF-16 and heat-shock factor
    • Hsu A L, Murphy C T & Kenyon C, Regulation of aging and age-related disease by DAF-16 and heat-shock factor, Science, 300 (2003) 1142.
    • (2003) Science , vol.300 , pp. 1142
    • Hsu, A.L.1    Murphy, C.T.2    Kenyon, C.3
  • 317
    • 0742323000 scopus 로고    scopus 로고
    • Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones
    • Morley J F & Morimoto R I, Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones, Mol Biol Cell, 15 (2004) 657.
    • (2004) Mol Biol Cell , vol.15 , pp. 657
    • Morley, J.F.1    Morimoto, R.I.2
  • 318
    • 0025369970 scopus 로고
    • The measurement and mechanisms of lipid peroxidation in biological systems
    • Gutteridge J M C & Halliwell B, The measurement and mechanisms of lipid peroxidation in biological systems, Trends Biochem Sci, 15 (1990) 129.
    • (1990) Trends Biochem Sci , vol.15 , pp. 129
    • Gutteridge, J.M.C.1    Halliwell, B.2
  • 320
    • 0023676276 scopus 로고
    • Luminescence research and its relation to ultra weak cell radiation
    • Slawinski J, Luminescence research and its relation to ultra weak cell radiation, Experientia, 44 (1988) 559.
    • (1988) Experientia , vol.44 , pp. 559
    • Slawinski, J.1
  • 322
    • 0004202404 scopus 로고
    • (Princeton University Press, Princeton)
    • Harvey E N, Living light (Princeton University Press, Princeton) 1940.
    • (1940) Living Light
    • Harvey, E.N.1
  • 323
    • 0007899354 scopus 로고
    • (American Philosophical Society, Philadelphia, Pennsylvania)
    • Harvey E N, A History of luminescence (American Philosophical Society, Philadelphia, Pennsylvania) 1957
    • (1957) A History of Luminescence
    • Harvey, E.N.1
  • 324
    • 73049160439 scopus 로고
    • Investigation of the ultraviolet hemi luminescence of biological systems
    • Troitskii N A, Konev S V & Katibnikov M A, Investigation of the ultraviolet hemi luminescence of biological systems, Biofizika, 6(2) (1961) 80.
    • (1961) Biofizika , vol.6 , Issue.2 , pp. 80
    • Troitskii, N.A.1    Konev, S.V.2    Katibnikov, M.A.3
  • 325
    • 42049111073 scopus 로고
    • On the problem of the role of the nature of ultraweak luminescence in biological systems
    • Vladimirov IuA, Litvin F F & T'an M C, On the problem of the role of the nature of ultraweak luminescence in biological systems, Biofizika, 7 (1962) 675.
    • (1962) Biofizika , vol.7 , pp. 675
    • Vladimirov, I.A.1    Litvin, F.F.2    T'an, M.C.3
  • 326
    • 0000372063 scopus 로고
    • Spectral emission and quantum yield of firefly bioluminescence
    • Seliger H H & McElroy W D, Spectral emission and quantum yield of firefly bioluminescence, Arch Biochem Biophys, 88 (1960) 136.
    • (1960) Arch Biochem Biophys , vol.88 , pp. 136
    • Seliger, H.H.1    McElroy, W.D.2
  • 327
    • 70349477375 scopus 로고
    • Model studies on chemical carcinogenesis and on the photodynamic effect of 3,4 - Benzopyrene and UV light in aqueous protein solutions with different SH group reactivity
    • Stauff J & Reske G, Model studies on chemical carcinogenesis and on the photodynamic effect of 3,4 - Benzopyrene and UV light in aqueous protein solutions with different SH group reactivity, Z Naturforsch B, 19 (1964) 716.
    • (1964) Z Naturforsch B , vol.19 , pp. 716
    • Stauff, J.1    Reske, G.2
  • 328
    • 0016159104 scopus 로고
    • Weak luminescence from the yeast Saccharomyces cerevisiae and the existence of mitogenetic radiation
    • Quickenden T I & Quee Hee S S, Weak luminescence from the yeast Saccharomyces cerevisiae and the existence of mitogenetic radiation, Biochem Biophys Res Commun, 60 (1974) 764.
    • (1974) Biochem Biophys Res Commun , vol.60 , pp. 764
    • Quickenden, T.I.1    Quee Hee, S.S.2
  • 329
    • 0015524885 scopus 로고
    • Evidence for the generation of an electronic excitation state(s) in human polymorphonuclear leukocytes and its participation in bactericidal activity
    • Allen R C, Stjernholm R L & Steele R H, Evidence for the generation of an electronic excitation state(s) in human polymorphonuclear leukocytes and its participation in bactericidal activity, Biochem Biophys Res Commun, 47 (1972) 79.
    • (1972) Biochem Biophys Res Commun , vol.47 , pp. 79
    • Allen, R.C.1    Stjernholm, R.L.2    Steele, R.H.3
  • 330
    • 0018375737 scopus 로고
    • Low level chemiluminescence of intact polymorphonuclear leukocytes
    • Kakinuma K, Cadenas E, Boveris A & Chance B, Low level chemiluminescence of intact polymorphonuclear leukocytes, FEBS Lett, 102 (1979) 38.
    • (1979) FEBS Lett , vol.102 , pp. 38
    • Kakinuma, K.1    Cadenas, E.2    Boveris, A.3    Chance B4
  • 331
    • 0019888827 scopus 로고
    • Low level chemiluminescence of alveolar macrophages: Spectral evidence for singlet oxygen generation
    • Cadenas E, Daniele R P & Chance B, Low level chemiluminescence of alveolar macrophages: spectral evidence for singlet oxygen generation, FEBS Lett, 123 (1981) 225.
    • (1981) FEBS Lett , vol.123 , pp. 225
    • Cadenas, E.1    Daniele, R.P.2    Chance, B.3
  • 332
    • 0019629512 scopus 로고
    • Low-level chemiluminescence of isolated hepatocytes
    • Cadenas E, WefersH & Sies H, Low-level chemiluminescence of isolated hepatocytes, Eur J Biochem 119, (1981) 531.
    • (1981) Eur J Biochem , vol.119 , pp. 531
    • Cadenas, E.1    Wefers, H.2    Sies, H.3
  • 333
    • 0345246336 scopus 로고
    • Accuracy and sensitivity of the human eye
    • Pirenne M H & Denton E J, Accuracy and sensitivity of the human eye, Nature, 170 (1952) 1039.
    • (1952) Nature , vol.170 , pp. 1039
    • Pirenne, M.H.1    Denton, E.J.2
  • 335
    • 0017283283 scopus 로고
    • A possible mechanism of the generation of singlet molecular oxygen in nadph-dependent microsomal lipid peroxidation
    • Sugioka K & Nakano M, A possible mechanism of the generation of singlet molecular oxygen in nadph-dependent microsomal lipid peroxidation, Biochim Biophys Acta, 423 (1976) 203.
    • (1976) Biochim Biophys Acta , vol.423 , pp. 203
    • Sugioka, K.1    Nakano, M.2
  • 336
    • 0017772285 scopus 로고
    • A new type of biological chemiluminescence: The microsomal chemiluminescence of benzo[a]pyrene arises from the diol epoxide product of the 7,8-dihydrodiol
    • Hamman J P, Gorby D R & Selige.H H, A new type of biological chemiluminescence: the microsomal chemiluminescence of benzo[a]pyrene arises from the diol epoxide product of the 7,8-dihydrodiol, Biochem Biophys Res Commun, 75, (1977) 793.
    • (1977) Biochem Biophys Res Commun , vol.75 , pp. 793
    • Hamman, J.P.1    Gorby, D.R.2    Selige, H.H.3
  • 338
    • 0019325018 scopus 로고
    • Low-level chemiluminescence of bovine heart submitochondrial particles
    • Cadenas E, Boveris A & Chance B, Low-level chemiluminescence of bovine heart submitochondrial particles, Biochem J, 186 (1980) 659.
    • (1980) Biochem J , vol.186 , pp. 659
    • Cadenas, E.1    Boveris, A.2    Chance, B.3
  • 339
    • 0016829812 scopus 로고
    • Singlet oxygen production associated with enzyme-catalyzed lipid peroxidation in liver microsomes
    • King M M, Lai E K & McCay P B, Singlet oxygen production associated with enzyme-catalyzed lipid peroxidation in liver microsomes, J Biochem, 250 (1975) 6496.
    • (1975) J Biochem , vol.250 , pp. 6496
    • King, M.M.1    Lai, E.K.2    McCay, P.B.3
  • 340
    • 0014791346 scopus 로고
    • Lipid oxidation in biological membranes. I. Lipid oxidation in submitochondrial particles and microsomes induced by chaotropic agents
    • Hatefi Y & Hanstein W G, Lipid oxidation in biological membranes. I. Lipid oxidation in submitochondrial particles and microsomes induced by chaotropic agents, Arch Biochem Biophys, 138 (1970) 73.
    • (1970) Arch Biochem Biophys , vol.138 , pp. 73
    • Hatefi, Y.1    Hanstein, W.G.2
  • 341
    • 0014792280 scopus 로고
    • Lipid oxidation in biological membranes. II. Kinetics and mechanism of lipid oxidation in submitochondrial particles
    • 335A.Hanstein W G & Hatefi Y, Lipid oxidation in biological membranes. II. Kinetics and mechanism of lipid oxidation in submitochondrial particles, Arch Biochem Biophys, 138(1) (1970) 87.
    • (1970) Arch Biochem Biophys , vol.138 , Issue.1 , pp. 87
    • Hanstein, W.G.1    Hatefi, Y.2
  • 342
    • 3843141783 scopus 로고
    • Studies of the mechanism of vitamin E action. III. In vitro copolymerization of oxidized fats with protein
    • Tappel A L, Studies of the mechanism of vitamin E action. III. In vitro copolymerization of oxidized fats with protein, Arch Biochem Biophys, 54 (1955) 266.
    • (1955) Arch Biochem Biophys , vol.54 , pp. 266
    • Tappel, A.L.1
  • 343
    • 0015914868 scopus 로고
    • A peroxide-dependent reduction of cytochrome c by NADH
    • Misra H & Fridovich I, A peroxide-dependent reduction of cytochrome c by NADH, Biochem Biophys Acta, 292 (1973) 815.
    • (1973) Biochem Biophys Acta , vol.292 , pp. 815
    • Misra, H.1    Fridovich, I.2
  • 344
    • 0017833890 scopus 로고
    • Superoxide-dependent production of hydroxyl radical catalyzed by iron-EDTA complex
    • McCord J M & Day jr. E D, Superoxide-dependent production of hydroxyl radical catalyzed by iron-EDTA complex, FEBS Lett, 86 (1978) 139.
    • (1978) FEBS Lett , vol.86 , pp. 139
    • McCord, J.M.1    Day Jr., E.D.2
  • 345
    • 0018145231 scopus 로고
    • Superoxide-dependent formation of hydroxyl radicals in the presence of iron chelates: Is it a mechanism for hydroxyl radical production in biochemical systems?
    • Halliwell B, Superoxide-dependent formation of hydroxyl radicals in the presence of iron chelates: is it a mechanism for hydroxyl radical production in biochemical systems? FEBS Lett, 92 (1978) 321.
    • (1978) FEBS Lett , vol.92 , pp. 321
    • Halliwell, B.1
  • 346
    • 0003674687 scopus 로고
    • edited by A M Michelson, J M McCord & I. Fridovich (Academic Press, New York)
    • Cohen G. in Superoxide and superoxide dismutases, edited by A M Michelson, J M McCord & I. Fridovich (Academic Press, New York) 1977, 317.
    • (1977) Superoxide and Superoxide Dismutases , vol.317
    • Cohen, G.1
  • 347
    • 3643087067 scopus 로고
    • Chemistry of superoxide ion. II. Reaction with hydroperoxides
    • Peters J W & Foote C S, Chemistry of superoxide ion. II. Reaction with hydroperoxides, J Am Chem Soc, 98 (1976) 873.
    • (1976) J Am Chem Soc , vol.98 , pp. 873
    • Peters, J.W.1    Foote, C.S.2
  • 348
    • 0019881761 scopus 로고
    • Oxygenor organic hydroperoxide-induced chemiluminescence of brain and liver homogenase
    • Cadenas E, Vasavsky A I, Boveris A & Chance B, Oxygenor organic hydroperoxide-induced chemiluminescence of brain and liver homogenase, Biochem J, 198 (1981) 645.
    • (1981) Biochem J , vol.198 , pp. 645
    • Cadenas, E.1    Vasavsky, A.I.2    Boveris, A.3    Chance B4
  • 350
    • 0015952772 scopus 로고
    • Ethane evolution: A new index of lipid peroxidation
    • Riely C A, Cohen G & Lieberman M, Ethane evolution: a new index of lipid peroxidation, Science, 183 (1974) 208.
    • (1974) Science , vol.183 , pp. 208
    • Riely, C.A.1    Cohen, G.2    Lieberman, M.3
  • 351
    • 0017342246 scopus 로고
    • Effect of dietary vitamin E on expiration of pentane and ethane by the rat
    • Dillard C J, Dumelin E E & Tappel A L, Effect of dietary vitamin E on expiration of pentane and ethane by the rat, Lipids, 12 (1977) 109.
    • (1977) Lipids , vol.12 , pp. 109
    • Dillard, C.J.1    Dumelin, E.E.2    Tappel, A.L.3
  • 352
    • 0026492143 scopus 로고
    • Oxygen radical generation during ischemia-reperfusion in the isolated perfused rat liver monitored by enhanced chemiluminescence
    • Okuda M, Lee H C, Kumar C & Chance, Oxygen radical generation during ischemia-reperfusion in the isolated perfused rat liver monitored by enhanced chemiluminescence, Circulatory Shock, 38 (1992) 228.
    • (1992) Circulatory Shock , vol.38 , pp. 228
    • Okuda, M.1    Lee, H.C.2    Kumar, C.3    Chance4
  • 353
    • 0016590545 scopus 로고
    • Effects of seven anthracycline antibiotics on electrocardiogram and mitochondrial function of rat hearts
    • Bachmann E, Weber E & Zbinden G, Effects of seven anthracycline antibiotics on electrocardiogram and mitochondrial function of rat hearts, Agents Actions, 5 (1975) 383.
    • (1975) Agents Actions , vol.5 , pp. 383
    • Bachmann, E.1    Weber, E.2    Zbinden, G.3
  • 354
    • 0027323949 scopus 로고
    • Activated polymorphonuclear leukocytes increase low-level chemiluminescence of isolated perfused rat lungs
    • Barnard M L, Gurdian S & Turrens J F, Activated polymorphonuclear leukocytes increase low-level chemiluminescence of isolated perfused rat lungs, J Appl Physiol, 75 (1993) 933.
    • (1993) J Appl Physiol , vol.75 , pp. 933
    • Barnard, M.L.1    Gurdian, S.2    Turrens, J.F.3
  • 356
    • 0023028913 scopus 로고
    • Redox cycling of anthracyclines by cardiac mitochondria. II. Formation of superoxide anion, hydrogen peroxide and hydroxyl radical
    • Doroshow J H & Davies K J A, Redox cycling of anthracyclines by cardiac mitochondria. II. Formation of superoxide anion, hydrogen peroxide and hydroxyl radical, J Biol Chem, 261 (1986) 3068.
    • (1986) J Biol Chem , vol.261 , pp. 3068
    • Doroshow, J.H.1    Davies, K.J.A.2
  • 357
    • 0021034824 scopus 로고
    • Generation of hydroxyl radicals during the enzymatic reductions of the Fe'.-ADP-EDTA systems, Less unvolvement of hydroxyl radical and a great importance of proposed perferryl ion complexes in lipid peroxidation
    • Sugioka K, Nakano H, Nakano M, Tero-Kubota S &Ikegami Y., Generation of hydroxyl radicals during the enzymatic reductions of the Fe'.-ADP-EDTA systems, Less unvolvement of hydroxyl radical and a great importance of proposed perferryl ion complexes in lipid peroxidation, Biochim Biophys Acta, 753 (1983) 411.
    • (1983) Biochim Biophys Acta , vol.753 , pp. 411
    • Sugioka, K.1    Nakano, H.2    Nakano, M.3    Tero-Kubota, S.4    Ikegami, Y.5
  • 358
    • 0019921584 scopus 로고
    • The role of lipid peroxidation in pathogenesis of ischemic damage and the antioxidant protection of the heart
    • Meerson F Z, Kagan V E, Kozlov Yu P, Belinka L M & Arkhipenko Yu V, The role of lipid peroxidation in pathogenesis of ischemic damage and the antioxidant protection of the heart, Basic Res Cardiol, 77 (1982) 465.
    • (1982) Basic Res Cardiol , vol.77 , pp. 465
    • Meerson, F.Z.1    Kagan, V.E.2    Kozlov Yu, P.3    Belinka, L.M.4    Arkhipenko Yu, V.5
  • 359
    • 0023176114 scopus 로고
    • The role of lipid peroxidation in the pathogenesis of arrhythmias and prevention of cardiac fibrillation with antioxidant
    • Meerson F Z, Belkina L M, Sazontova T G, Saltykova V A & Arkhipenko Yu V, The role of lipid peroxidation in the pathogenesis of arrhythmias and prevention of cardiac fibrillation with antioxidant, Basic Res.Cardiol, 82 (1987) 123.
    • (1987) Basic Res.Cardiol , vol.82 , pp. 123
    • Meerson, F.Z.1    Belkina, L.M.2    Sazontova, T.G.3    Saltykova, V.A.4    Arkhipenko Yu, V.5
  • 360
    • 0018899101 scopus 로고
    • Role of oxygen in the cellular damage induced by reoxygenation of hypoxic heart
    • Guarnieri C, Flamigni F & Caldarera C M, Role of oxygen in the cellular damage induced by reoxygenation of hypoxic heart, J Mol Cell Cardiol, 12 (1980) 797.
    • (1980) J Mol Cell Cardiol , vol.12 , pp. 797
    • Guarnieri, C.1    Flamigni, F.2    Caldarera, C.M.3
  • 362
    • 0023069361 scopus 로고
    • Spin-trapping evidence that graded myocardial ischemia alters post-ischemic superoxide production
    • Kramer J H, Arroyo C M, Dickens B F & Weglicki W B, Spin-trapping evidence that graded myocardial ischemia alters post-ischemic superoxide production, Free Radic Biol Med, 3 (1987) 153.
    • (1987) Free Radic Biol Med , vol.3 , pp. 153
    • Kramer, J.H.1    Arroyo, C.M.2    Dickens, B.F.3    Weglicki, W.B.4
  • 363
    • 0023272808 scopus 로고
    • Direct detection of free radicals in the reperfused rat heart using electron spin resonance spectroscopy
    • Garlick P B, Davies M J, Hearse D J & Slater T S, Direct detection of free radicals in the reperfused rat heart using electron spin resonance spectroscopy, Circul Res, 61 (1987) 757.
    • (1987) Circul Res , vol.61 , pp. 757
    • Garlick, P.B.1    Davies, M.J.2    Hearse, D.J.3    Slater, T.S.4
  • 365
    • 0024308199 scopus 로고
    • Increased ultra weak chemiluminescence from rat heart at postischemie reoxygenation: Protective role of vitamin E
    • Barsacchi R, Coassin M, Maiorino M, Pelosi G, Simonelli C & Ursini F, Increased ultra weak chemiluminescence from rat heart at postischemie reoxygenation: protective role of vitamin E, Free Rad Biol & Medic, 5 (1989) 573.
    • (1989) Free Rad Biol & Medic , vol.5 , pp. 573
    • Barsacchi, R.1    Coassin, M.2    Maiorino, M.3    Pelosi, G.4    Simonelli, C.5    Ursini, F.6
  • 366
    • 0023758565 scopus 로고
    • Ischemia-reperfusion injury: A radical view
    • Parks D A & Granger D N, Ischemia-reperfusion injury: A radical view, Hepatology, 8 (1988) 680.
    • (1988) Hepatology , vol.8 , pp. 680
    • Parks, D.A.1    Granger, D.N.2
  • 367
    • 0029064010 scopus 로고
    • Chemiluminescent measurement of increased free radical formation after ischemia/reperfusion
    • Nunes F A, Kumar C, Chance B & Brass C A, Chemiluminescent measurement of increased free radical formation after ischemia/reperfusion, Digestive Diseases and Sciences, 40(5) ( 1995) 1045.
    • (1995) Digestive Diseases and Sciences , vol.40 , Issue.5 , pp. 1045
    • Nunes, F.A.1    Kumar, C.2    Chance, B.3    Brass, C.A.4
  • 370
    • 0001067564 scopus 로고
    • Low-level chemiluminescence of biological systems
    • edited by W A Pryor (New York, Academic Press)
    • Cadenas E, Boveris A, & Chance B, Low-level chemiluminescence of biological systems, in Free radical in biology,edited by W A Pryor (New York, Academic Press) 1984, 211.
    • (1984) Free Radical in Biology , vol.211
    • Cadenas, E.1    Boveris, A.2    Chance, B.3
  • 371
    • 0019320760 scopus 로고
    • Partial spectral analysis of the hydroperoxide-induced chemiluminescence of the perfused lung
    • Cadenas E, Arad I D, Boveris A, Fisher A B & Chance B, Partial spectral analysis of the hydroperoxide-induced chemiluminescence of the perfused lung, FEBS Lett, 111 (1980) 413.
    • (1980) FEBS Lett , vol.111 , pp. 413
    • Cadenas, E.1    Arad, I.D.2    Boveris, A.3    Fisher, A.B.4    Chance, B.5
  • 373
    • 0027323949 scopus 로고
    • Activated polymorphonuclear leukocytes increase low-level chemiluminescence of isolated perfused rat lungs
    • Barnard M L, Gurdian S & Turrens J F, Activated polymorphonuclear leukocytes increase low-level chemiluminescence of isolated perfused rat lungs, J Appl Physiol, 75 (1993) 933.
    • (1993) J Appl Physiol , vol.75 , pp. 933
    • Barnard, M.L.1    Gurdian, S.2    Turrens, J.F.3
  • 374
    • 0027176938 scopus 로고
    • Characteristics of neutrophil influx in rat lungs following fecal peritonitis
    • Peralta J G, Barnard M L & Turrens J K, Characteristics of neutrophil influx in rat lungs following fecal peritonitis, Inflammation, 17 (1993) 263.
    • (1993) Inflammation , vol.17 , pp. 263
    • Peralta, J.G.1    Barnard, M.L.2    Turrens, J.K.3
  • 375
    • 0023727303 scopus 로고
    • Photobiochemistry without light
    • Cilento G, Photobiochemistry without light, Experientia, 44 (1988) 572.
    • (1988) Experientia , vol.44 , pp. 572
    • Cilento, G.1
  • 376
    • 21444441373 scopus 로고    scopus 로고
    • Looking and listening to light: The evolution of whole body photonic imaging
    • Ntziachristos V, Ripoll J, Wang L V, Weissleder R, Looking and listening to light: the evolution of whole body photonic imaging. Nature Biotechnol, 23 (2005) 313.
    • (2005) Nature Biotechnol , vol.23 , pp. 313
    • Ntziachristos, V.1    Ripoll, J.2    Wang, L.V.3    Weissleder, R.4
  • 377
    • 0032776744 scopus 로고    scopus 로고
    • Twodimensional photon counting imaging and spatiotemporal characterization of ultraweak photon emission from a rat's brain in vivo
    • Kobayashi M, Takeda M, Ito, K-I, Kato H & Inaba H, Twodimensional photon counting imaging and spatiotemporal characterization of ultraweak photon emission from a rat's brain in vivo, J Neurosci Methods, 93 (1999) 163.
    • (1999) J Neurosci Methods , vol.93 , pp. 163
    • Kobayashi, M.1    Takeda, M.2    Ito, K.-I.3    Kato, H.4    Inaba, H.5
  • 378
    • 34548817364 scopus 로고    scopus 로고
    • Two-dimensional imaging and spatiotemporal analysis of biophoton
    • edited by X Shen & R Van Wijk (Springer, New York)
    • st century, edited by X Shen & R Van Wijk (Springer, New York) 2005, 155.
    • (2005) st Century , vol.155
    • Kobayashi, M.1
  • 379
    • 0022297699 scopus 로고
    • Increased liver chemiluminescence in tumor-bearing mice
    • Boveris A, Llesuy S F & Fraga C G, Increased liver chemiluminescence in tumor-bearing mice, J Free Rad Biol Med, 1(2) (1985) 131.
    • (1985) J Free Rad Biol Med , vol.1 , Issue.2 , pp. 131
    • Boveris, A.1    Llesuy, S.F.2    Fraga, C.G.3
  • 380
    • 0015066128 scopus 로고
    • Free-radical mechanism of ultraweak chemiluminescence accompanying the peroxidation of unsaturated fatty acids
    • Neifakh E A, Free-radical mechanism of ultraweak chemiluminescence accompanying the peroxidation of unsaturated fatty acids, Biofizika, 16 (1971) 560.
    • (1971) Biofizika , vol.16 , pp. 560
    • Neifakh, E.A.1
  • 382
    • 0025040955 scopus 로고
    • A combined therapy of hyperthermia and tumor necrosis factor for nude mice bearing KK-47 bladder cancer
    • Amano T, Kunimi K, Nakashima K, Uchibayashi T & Hisazumi H, A combined therapy of hyperthermia and tumor necrosis factor for nude mice bearing KK-47 bladder cancer, J Urol, (1990) 144.
    • (1990) J Urol , vol.144
    • Amano, T.1    Kunimi, K.2    Nakashima, K.3    Uchibayashi, T.4    Hisazumi, H.5
  • 383
    • 0028846497 scopus 로고
    • Ultraweak biophoton emission imaging of transplanted bladder cancer
    • Amano T, Kobayashi M, Devaraj B, Inaba H, Ultraweak biophoton emission imaging of transplanted bladder cancer, Urol Res, 23 (1995) 315
    • (1995) Urol Res , vol.23 , pp. 315
    • Amano, T.1    Kobayashi, M.2    Devaraj, B.3    Inaba, H.4
  • 384
    • 28444488524 scopus 로고    scopus 로고
    • Measurements of spontaneous photon emission and delayed luminescence from human cancer tissues
    • Kim J, Choi C, Lim J, You H, Sim S, Yom Y, Kim E & Soh K, Measurements of spontaneous photon emission and delayed luminescence from human cancer tissues, J Altern Complement Med, 11 (2005) 879.
    • (2005) J Altern Complement Med , vol.11 , pp. 879
    • Kim, J.1    Choi, C.2    Lim, J.3    You, H.4    Sim, S.5    Yom, Y.6    Kim, E.7    Soh, K.8
  • 385
    • 0015699670 scopus 로고
    • Measuring methods for ultra-low light intensity and their application to extra-weak spontaneous bioluminescence from living tissues
    • Shimizu Y, Inaba H, Kumaki K, Mizuno K, Hata S & Tomita S, Measuring methods for ultra-low light intensity and their application to extra-weak spontaneous bioluminescence from living tissues, IEEE Trans Instrum Meas, IM-22 (1973) 153.
    • (1973) IEEE Trans Instrum Meas , vol.153 IM-22
    • Shimizu, Y.1    Inaba, H.2    Kumaki, K.3    Mizuno, K.4    Hata, S.5    Tomita, S.6
  • 389
    • 0001658637 scopus 로고    scopus 로고
    • Whole-body counting of biophotons and its relation to biological rhythms
    • edited by J J Chang, J Fisch & F A Popp (Kluwer Academic, Dordrecht)
    • Cohen S & Popp F A, Whole-body counting of biophotons and its relation to biological rhythms, in Biophotons, edited by J J Chang, J Fisch & F A Popp (Kluwer Academic, Dordrecht) 1998, 183.
    • (1998) Biophotons , vol.183
    • Cohen, S.1    Popp, F.A.2
  • 390
    • 12944336467 scopus 로고    scopus 로고
    • Ultraweak photon emission of human skin in vivo: Influence of topically applied antioxidants on human skin
    • Sauermann G, Mei W P, Hoppe U & Stäb F, Ultraweak photon emission of human skin in vivo: Influence of topically applied antioxidants on human skin, Methods Enzymol, 300 (1999) 419.
    • (1999) Methods Enzymol , vol.300 , pp. 419
    • Sauermann, G.1    Mei, W.P.2    Hoppe, U.3    Stäb, F.4
  • 392
    • 20944431527 scopus 로고    scopus 로고
    • Multi-site registration and spectral analysis of spontaneous emission from human body
    • Van Wijk E P A. & Van Wijk R, Multi-site registration and spectral analysis of spontaneous emission from human body, Res in Complimentary Classical Natural Med, 12 (2005) 96.
    • (2005) Res in Complimentary Classical Natural Med , vol.12 , pp. 96
    • Van Wijk, E.P.A.1    Van Wijk, R.2
  • 393
    • 33745050792 scopus 로고    scopus 로고
    • Ultra weak photon emission of human body
    • edited by X Shen & R. Van Wijk (Kluwer, New York)
    • st Century, edited by X Shen & R. Van Wijk (Kluwer, New York) 2006.
    • (2006) st Century
    • Van Wijk, E.P.A.1    Van Wijk, R.2
  • 396
    • 13444307033 scopus 로고    scopus 로고
    • Modern technology on physical analysis of biophoton emission and its potential extracting the physiological information
    • edited by F Musumeci, L S Brizhik & M W Ho (World Scientific Publishers, New Jersey, London)
    • Kobayashi M, Modern technology on physical analysis of biophoton emission and its potential extracting the physiological information, in Energy and information transfer in biological systems, edited by F Musumeci, L S Brizhik & M W Ho (World Scientific Publishers, New Jersey, London) 2003, 157.
    • (2003) Energy and Information Transfer in Biological Systems , vol.157
    • Kobayashi, M.1
  • 399
    • 84872911106 scopus 로고    scopus 로고
    • Measurement of spontaneous ultra-weak photon emission from human body: Spontaneous ultra-weak photon emission varies diurnally
    • Cifra M, Van Wijk E P A, Koch H, Bosman S & Van Wijk R, Measurement of spontaneous ultra-weak photon emission from human body: spontaneous ultra-weak photon emission varies diurnally, Measurement (2007).
    • (2007) Measurement
    • Cifra, M.1    Van Wijk, E.P.A.2    Koch, H.3    Bosman, S.4    Van Wijk, R.5
  • 402
    • 22144482316 scopus 로고    scopus 로고
    • Ultra-weak photon emission from human hand: Influence of temperature and oxygen concentration on emission
    • Nakamura K & Hiramatsu M, Ultra-weak photon emission from human hand: influence of temperature and oxygen concentration on emission, J Photochem Photobiol B, 80 (2005) 156.
    • (2005) J Photochem Photobiol B , vol.80 , pp. 156
    • Nakamura, K.1    Hiramatsu, M.2
  • 404
    • 70349457536 scopus 로고    scopus 로고
    • Biophoton emission and blood flow in human hand
    • Yang J M, Lee C, Yi S H, Yang J S & Soh K S, Biophoton emission and blood flow in human hand, ISLIS, 22 (2004) 344.
    • (2004) ISLIS , vol.22 , pp. 344
    • Yang, J.M.1    Lee, C.2    Yi, S.H.3    Yang, J.S.4    Soh, K.S.5
  • 405
  • 406
    • 0038670753 scopus 로고    scopus 로고
    • Quantum coherence of biophotons and living systems
    • Bajpai R J, Quantum coherence of biophotons and living systems, Indian J.Exp Biol, 41 (2003) 514.
    • (2003) Indian J.Exp Biol , vol.41 , pp. 514
    • Bajpai, R.J.1
  • 407
    • 1142273322 scopus 로고    scopus 로고
    • Biophotons emission in a squeezed state from a sample of Parmelia tinctorum
    • Bajpai R J, Biophotons emission in a squeezed state from a sample of Parmelia tinctorum, Phys Lett A, 322 (2004) 131.
    • (2004) Phys Lett A , vol.322 , pp. 131
    • Bajpai, R.J.1
  • 408
    • 15244361934 scopus 로고    scopus 로고
    • Squeezed state description of the spectral decomposition of a biophoton signal
    • Bajpai R P, Squeezed state description of the spectral decomposition of a biophoton signal, Phys Lett A, 337 (2005) 265.
    • (2005) Phys Lett A , vol.337 , pp. 265
    • Bajpai, R.P.1
  • 409
    • 33745022410 scopus 로고    scopus 로고
    • Photon count distribution of photons emitted from three sites of a human body
    • Van Wijk R, Van Wijk E & Bajpai RP, Photon count distribution of photons emitted from three sites of a human body, J Photochem Photobiol B, 84 (2006) 46.
    • (2006) J Photochem Photobiol B , vol.84 , pp. 46
    • Van Wijk, R.1    Van Wijk, E.2    Bajpai, R.P.3
  • 411
    • 20944452101 scopus 로고
    • Spontaneous photon emission from human body
    • Usa M & Inaba H, Spontaneous photon emission from human body, Med. Imaging Technol, 13 (1995) 47.
    • (1995) Med. Imaging Technol , vol.13 , pp. 47
    • Usa, M.1    Inaba, H.2
  • 413
    • 0031217770 scopus 로고    scopus 로고
    • Biophoton emission of the human body
    • Cohen S & Popp F A, Biophoton emission of the human body, J Photochem Photobiol B, 40 (1997) 187.
    • (1997) J Photochem Photobiol B , vol.40 , pp. 187
    • Cohen, S.1    Popp, F.A.2
  • 414
    • 0038670763 scopus 로고    scopus 로고
    • Biophoton emission of the human body
    • Cohen S & Popp F A, Biophoton emission of the human body, Indian J Exp Biol, 41 (2003) 440.
    • (2003) Indian J Exp Biol , vol.41 , pp. 440
    • Cohen, S.1    Popp, F.A.2
  • 417
    • 0027318196 scopus 로고
    • Lipid peroxides as the initiating factor of atherosclerosis
    • Naito C, Kawamura M & Yamamoto Y, Lipid peroxides as the initiating factor of atherosclerosis, Ann N Y Acad Sci, 676 (1993) 27.
    • (1993) Ann N Y Acad Sci , vol.676 , pp. 27
    • Naito, C.1    Kawamura, M.2    Yamamoto, Y.3
  • 418
    • 0028323529 scopus 로고
    • Psychological stress and lipoperoxidation in miscarriage
    • Scarpellini F, Sbracia M & Scarpellini L, Psychological stress and lipoperoxidation in miscarriage, Ann N Y Sci, 709 (1994) 210.
    • (1994) Ann N Y Sci , vol.709 , pp. 210
    • Scarpellini, F.1    Sbracia, M.2    Scarpellini, L.3
  • 419
    • 0027818833 scopus 로고
    • Oxidative damage of nuclear DNA in liver of rats exposed to psychological stress
    • Adachi S, Kawamura K & Takemoto K, Oxidative damage of nuclear DNA in liver of rats exposed to psychological stress, Cancer Res, 53 (1993) 4153.
    • (1993) Cancer Res , vol.53 , pp. 4153
    • Adachi, S.1    Kawamura, K.2    Takemoto, K.3
  • 422
    • 23044495142 scopus 로고    scopus 로고
    • Effect of comprehensive yoga-based life style modification program on lipid peroxidation
    • Yadav R K, Ray R B, Vempati R & Bijlani R L, Effect of comprehensive yoga-based life style modification program on lipid peroxidation, Indian J Physiol Pharmacol, 49 (2005) 358.
    • (2005) Indian J Physiol Pharmacol , vol.49 , pp. 358
    • Yadav, R.K.1    Ray, R.B.2    Vempati, R.3    Bijlani, R.L.4
  • 423
    • 33644745251 scopus 로고    scopus 로고
    • Spatial characterization of human ultra-weak photon emission in TM practitioners and control subjects
    • Van Wijk E P A, Koch H, Bosman S, Van Wijk R, Spatial characterization of human ultra-weak photon emission in TM practitioners and control subjects, J Altern Complement Med, 12 (2006) 31.
    • (2006) J Altern Complement Med , vol.12 , pp. 31
    • Van Wijk, E.P.A.1    Koch, H.2    Bosman, S.3    Van Wijk, R.4
  • 424
  • 425
    • 50649092899 scopus 로고    scopus 로고
    • Quantum squeezed state analysis of spontaneous ultra-weak photon emission of practitioners of meditation and control subjects
    • Van Wijk R, Van Wijk E P A & Bajpai R P, Quantum squeezed state analysis of spontaneous ultra-weak photon emission of practitioners of meditation and control subjects, Indian J Exp Biol, 46 (2008) 345.
    • (2008) Indian J Exp Biol , vol.46 , pp. 345
    • Van Wijk, R.1    Van Wijk, E.P.A.2    Bajpai, R.P.3
  • 428
    • 0019796887 scopus 로고
    • Lipid peroxide levels of serum lipoprotein fractions of diabetic patients
    • Nishigaki I, Hagihara M, Tsunekawa H, Maseki M & Yagi K, Lipid peroxide levels of serum lipoprotein fractions of diabetic patients, Biochem Med, 25 (1981) 373.
    • (1981) Biochem Med , vol.25 , pp. 373
    • Nishigaki, I.1    Hagihara, M.2    Tsunekawa, H.3    Maseki, M.4    Yagi, K.5
  • 431
    • 0027428582 scopus 로고
    • The role of anti-oxidative treatment in diabetes mellitus
    • Packer L, The role of anti-oxidative treatment in diabetes mellitus, Diabetologia, 36 (1993) 1212.
    • (1993) Diabetologia , vol.36 , pp. 1212
    • Packer, L.1
  • 432
    • 0026563633 scopus 로고
    • Effects of ageing and exercise on soleus and extensor digitorum longus muscles of female rats
    • Brown M, Ross T P & Holloszy J O, Effects of ageing and exercise on soleus and extensor digitorum longus muscles of female rats, Mech Ageing Dev, 63 (1992) 69.
    • (1992) Mech Ageing Dev , vol.63 , pp. 69
    • Brown, M.1    Ross, T.P.2    Holloszy, J.O.3
  • 433
    • 33646672079 scopus 로고    scopus 로고
    • Effect of exercise training on iNOS and pro-apoptotic signaling in aging skeletal muscle
    • Song W, Kwak H B & Lawler J M, Effect of exercise training on iNOS and pro-apoptotic signaling in aging skeletal muscle, FASEB J, 18 (2004) A753.
    • (2004) FASEB J , vol.18
    • Song, W.1    Kwak, H.B.2    Lawler, J.M.3
  • 434
    • 33646697753 scopus 로고    scopus 로고
    • Exercise training attenuates age-induced changes in apoptotic signaling in rat skeletal muscle
    • Song W, Kwak H B & Lawler J M, Exercise training attenuates age-induced changes in apoptotic signaling in rat skeletal muscle, Antioxidants Redox Signaling, 8 (2006) 517.
    • (2006) Antioxidants Redox Signaling , vol.8 , pp. 517
    • Song, W.1    Kwak, H.B.2    Lawler, J.M.3
  • 435
    • 0030771274 scopus 로고    scopus 로고
    • Changes in skeletal muscle biochemistry and histology relative to fibertype in rats with heart failure
    • Delp M D, Duan C, Mattson J P & Musch T I, Changes in skeletal muscle biochemistry and histology relative to fibertype in rats with heart failure, J Appl Physiol, 83 (1997) 1291.
    • (1997) J Appl Physiol , vol.83 , pp. 1291
    • Delp, M.D.1    Duan, C.2    Mattson, J.P.3    Musch, T.I.4
  • 437
    • 14844336534 scopus 로고    scopus 로고
    • Muscle-specific expression of OGF-1 blocks angiotensin II-induced skeletal muscle waisting
    • Song Y H, Li Y, Du J, Mitch W E, Rosenthal N & Delafontaine P, Muscle-specific expression of OGF-1 blocks angiotensin II-induced skeletal muscle waisting, J Clin Invest, 115 (2005) 451.
    • (2005) J Clin Invest , vol.115 , pp. 451
    • Song, Y.H.1    Li, Y.2    Du, J.3    Mitch, W.E.4    Rosenthal, N.5    Delafontaine, P.6
  • 438
    • 0033984788 scopus 로고    scopus 로고
    • Effects of exercise and cardiac rehabilitation on cardiovascular outcomes
    • Ades P A & Coello C E, Effects of exercise and cardiac rehabilitation on cardiovascular outcomes. Med Clin North Am, 84 (2000) 251.
    • (2000) Med Clin North Am , vol.84 , pp. 251
    • Ades, P.A.1    Coello, C.E.2
  • 439
    • 0033061884 scopus 로고    scopus 로고
    • Cardiac rehabilitation and preventive cardiology in the elderly
    • Lavie C J & Milani R V, Cardiac rehabilitation and preventive cardiology in the elderly, Cardiol Clin, 17 (1999) 233.
    • (1999) Cardiol Clin , vol.17 , pp. 233
    • Lavie, C.J.1    Milani, R.V.2
  • 440
    • 0345561653 scopus 로고    scopus 로고
    • Significance of skeltal muscle properties on fitness, long-term physical training and serum lipids
    • Tikkanen H O, Hamalainen E & Harkonen M, Significance of skeltal muscle properties on fitness, long-term physical training and serum lipids, Atherosclerosis, 142 (1999) 367.
    • (1999) Atherosclerosis , vol.142 , pp. 367
    • Tikkanen, H.O.1    Hamalainen, E.2    Harkonen, M.3
  • 441
    • 0026709444 scopus 로고
    • Exercise training-induced alterations in skeletal muscle oxidative and antioxidant enzyme activity in senescent rats
    • Hammeren J, Powers S, Lawler J, Criswell D, Martin D, Lowenthal D & Pollock M, Exercise training-induced alterations in skeletal muscle oxidative and antioxidant enzyme activity in senescent rats, Int J Sports Med, 13 (1992) 412.
    • (1992) Int J Sports Med , vol.13 , pp. 412
    • Hammeren, J.1    Powers, S.2    Lawler, J.3    Criswell, D.4    Martin, D.5    Lowenthal, D.6    Pollock, M.7


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