메뉴 건너뛰기




Volumn , Issue , 2005, Pages 455-506

Drugs, nutrients, and hormones in mitochondrial function

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84862667168     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (2)

References (234)
  • 1
    • 0027418625 scopus 로고
    • Mitochondria as a source of reactive oxygen species during reductive stress in rat hepatocytes
    • TL Dawson, GJ Gores, AL Nieminen, B Herman, JJ Lemasters. Mitochondria as a source of reactive oxygen species during reductive stress in rat hepatocytes. Am J Physiol 264: C961-967; 1993.
    • (1993) Am J Physiol , vol.264 , pp. C961-C967
    • Dawson, T.L.1    Gores, G.J.2    Nieminen, A.L.3    Herman, B.4    Lemasters, J.J.5
  • 2
    • 0031299037 scopus 로고    scopus 로고
    • Mitochondria generate superoxide anion radicals and hydrogen peroxide
    • RS Sohal. Mitochondria generate superoxide anion radicals and hydrogen peroxide. FASEB J 11:1269-1270; 1997.
    • (1997) FASEB J , vol.11 , pp. 1269-1270
    • Sohal, R.S.1
  • 3
    • 0025953504 scopus 로고
    • Initiation of lipid peroxidation in submitochondrial particles: Effects of respiratory inhibitors
    • M Glinn, L Ernster, CP Lee. Initiation of lipid peroxidation in submitochondrial particles: Effects of respiratory inhibitors. Arch Biochem Biophys 290:57-65; 1991.
    • (1991) Arch Biochem Biophys , vol.290 , pp. 57-65
    • Glinn, M.1    Ernster, L.2    Lee, C.P.3
  • 4
    • 0027164227 scopus 로고
    • Studies on Hg(II) induced H2O2 formation and oxidative stress in vivo and in vitro in rat kidney mitochondria
    • B-O Lund, DM Miller, JS Woods. Studies on Hg(II) induced H2O2 formation and oxidative stress in vivo and in vitro in rat kidney mitochondria. Biochem Pharmacol 45:2017-2024; 1993.
    • (1993) Biochem Pharmacol , vol.45 , pp. 2017-2024
    • Lund, B.-O.1    Miller, D.M.2    Woods, J.S.3
  • 6
    • 0029909113 scopus 로고    scopus 로고
    • Inhibition of mitochondrial complex I may account for IDDM induced by intoxication with rodenticide Vacor
    • MD Espositi, A Ngo, MA Myers. Inhibition of mitochondrial complex I may account for IDDM induced by intoxication with rodenticide Vacor. Diabetes 45:1531-1534; 1996.
    • (1996) Diabetes , vol.45 , pp. 1531-1534
    • Espositi, M.D.1    Ngo, A.2    Myers, M.A.3
  • 7
    • 0034064334 scopus 로고    scopus 로고
    • Beta-cell mitochondria in the regulation of insulin secretion: A new culprit in type 2 diabetes
    • CB Wolheim. Beta-cell mitochondria in the regulation of insulin secretion: A new culprit in type 2 diabetes. Diabetologia43:265-277; 2000.
    • (2000) Diabetologia , vol.43 , pp. 265-277
    • Wolheim, C.B.1
  • 10
    • 0014209501 scopus 로고
    • Induction of renal tumors by streptozotocin in rat
    • RN Arison, FL Feudale. Induction of renal tumors by streptozotocin in rat. Nature 214:1254-1255; 1967.
    • (1967) Nature , vol.214 , pp. 1254-1255
    • Arison, R.N.1    Feudale, F.L.2
  • 11
    • 0014034750 scopus 로고
    • Light and electron microscopy of lesions in rats rendered diabetic with streptozotocin
    • RN Arison, EL Ciaccio, MS Glitzer, JA Cassaro, MP Pruss. Light and electron microscopy of lesions in rats rendered diabetic with streptozotocin. Diabetes 16:51-56; 1967.
    • (1967) Diabetes , vol.16 , pp. 51-56
    • Arison, R.N.1    Ciaccio, E.L.2    Glitzer, M.S.3    Cassaro, J.A.4    Pruss, M.P.5
  • 12
    • 0014572551 scopus 로고
    • Streptozotocin diabetes in the mouse and guinea pig
    • G Brosky, J Logothetopolous. Streptozotocin diabetes in the mouse and guinea pig. Diabetes 18:606-611; 1969.
    • (1969) Diabetes , vol.18 , pp. 606-611
    • Brosky, G.1    Logothetopolous, J.2
  • 13
    • 0021263869 scopus 로고
    • Tubular lesions in streptozotoci-diabetic rats
    • R Rasch. Tubular lesions in streptozotoci-diabetic rats. Diabe-tologia 27:32-37, 1984.
    • (1984) Diabe-Tologia , vol.27 , pp. 32-37
    • Rasch, R.1
  • 14
    • 0017179001 scopus 로고
    • Streptozotocin-induced pancreatic insu-litis: New model of diabetes mellitus
    • AA Like, AA Rossini. Streptozotocin-induced pancreatic insu-litis: New model of diabetes mellitus. Science 193:415-417; 1976.
    • (1976) Science , vol.193 , pp. 415-417
    • Like, A.A.1    Rossini, A.A.2
  • 15
    • 0019135171 scopus 로고
    • Insulin-dependent diabetes mellitus induced by subdiabetogenic doses of streptozotocin: Obligatory role of cell-mediated autoimmune processes
    • S-G Paik, N Fleischer, S-I Shin. Insulin-dependent diabetes mellitus induced by subdiabetogenic doses of streptozotocin: Obligatory role of cell-mediated autoimmune processes. Proc Nat Acad Sci 77:6129-6133; 1980.
    • (1980) Proc Nat Acad Sci , vol.77 , pp. 6129-6133
    • Paik, S.-G.1    Fleischer, N.2    Shin, S.-I.3
  • 16
    • 0019409101 scopus 로고
    • Diabetes induced with multiple subdiabetogenic doses of streptozotocin. Lack of protection by exogenous superoxide dis-mutase
    • G Gold, M Manning, A Heldt, R Nowlain, JR Pettit, GA Grod-sky. Diabetes induced with multiple subdiabetogenic doses of streptozotocin. Lack of protection by exogenous superoxide dis-mutase. Diabetes 30:634-638; 1981.
    • (1981) Diabetes , vol.30 , pp. 634-638
    • Gold, G.1    Manning, M.2    Heldt, A.3    Nowlain, R.4    Pettit, J.R.5    Grod-Sky, G.A.6
  • 17
    • 0025900541 scopus 로고
    • Decreased mitochondrial gene expression in isolated islets of rats injected neonatally with streptozotocin
    • N. Welsh, S Paabo, M Welsh. Decreased mitochondrial gene expression in isolated islets of rats injected neonatally with streptozotocin. Diabetologia 34:626-631; 1991.
    • (1991) Diabetologia , vol.34 , pp. 626-631
    • Welsh, N.1    Paabo, S.2    Welsh, M.3
  • 19
    • 0016678715 scopus 로고
    • Time course of changes in blood glucose and ketone bodies, plasma lipids and liver fatty acid composition in streptozotocin-diabetic male rats
    • DL Topping, ME Targ. Time course of changes in blood glucose and ketone bodies, plasma lipids and liver fatty acid composition in streptozotocin-diabetic male rats. Hormone Res6:129-137; 1975.
    • (1975) Hormone Res , vol.6 , pp. 129-137
    • Topping, D.L.1    Targ, M.E.2
  • 20
    • 0019119454 scopus 로고
    • Altered fatty acid desaturation and microsomal fatty acid composition in the streptozotocin-treated diabetic rat
    • FH Fass, WL Carter. Altered fatty acid desaturation and microsomal fatty acid composition in the streptozotocin-treated diabetic rat. Lipids 15:953-961; 1980.
    • (1980) Lipids , vol.15 , pp. 953-961
    • Fass, F.H.1    Carter, W.L.2
  • 21
    • 0022345550 scopus 로고
    • Corrrection of abnormal lipid fluidity and composition of rat ileal microvillus membranes in chronic streptozotocin-induced diabetes by insulin therapy
    • TA Brasitus, PK Dudeja. Corrrection of abnormal lipid fluidity and composition of rat ileal microvillus membranes in chronic streptozotocin-induced diabetes by insulin therapy. J Biol Chem 260:12405-12409; 1985.
    • (1985) J Biol Chem , vol.260 , pp. 12405-12409
    • Brasitus, T.A.1    Dudeja, P.K.2
  • 22
    • 0027293774 scopus 로고
    • Diabetes increases excretion of urinary malonaldehyde conjugates in rats
    • DD Gallaher, AS Csallany, DW Shoeman, JM Olson. Diabetes increases excretion of urinary malonaldehyde conjugates in rats. Lipids 28:663-666; 1993.
    • (1993) Lipids , vol.28 , pp. 663-666
    • Gallaher, D.D.1    Csallany, A.S.2    Shoeman, D.W.3    Olson, J.M.4
  • 23
    • 0022550524 scopus 로고
    • Inhibition by streptozotocin of the activity of succinyl-CoA synthetase in vitro and
    • L Boquist, I Ericsson. Inhibition by streptozotocin of the activity of succinyl-CoA synthetase in vitro and in vivo. FEBS196:341-343; 1986.
    • (1986) Vivo. FEBS , vol.196 , pp. 341-343
    • Boquist, L.1    Ericsson, I.2
  • 25
    • 0023748601 scopus 로고
    • Alloxan: History and mechanism of action
    • S Lenzen, U Panten. Alloxan: History and mechanism of action. Diabetologia 31:337-342; 1988.
    • (1988) Diabetologia , vol.31 , pp. 337-342
    • Lenzen, S.1    Panten, U.2
  • 26
    • 0017681502 scopus 로고
    • Free radical production by alloxan
    • RE Heikkila. Free radical production by alloxan. Eur J Pharmacol 44:191-196; 1977.
    • (1977) Eur J Pharmacol , vol.44 , pp. 191-196
    • Heikkila, R.E.1
  • 27
    • 0020382491 scopus 로고
    • Alloxan toxicity to the pancreatic B-cell. A new hypothesis
    • WJ Malaisse. Alloxan toxicity to the pancreatic B-cell. A new hypothesis. Biochem Pharmacol 31:3527-3534; 1982.
    • (1982) Biochem Pharmacol , vol.31 , pp. 3527-3534
    • Malaisse, W.J.1
  • 29
    • 0033017850 scopus 로고    scopus 로고
    • Zidovudine (AZT) causes an oxidation of mitochondrial DNA in mouse liver
    • JG Asuncion, ML Olmo, J Sastre, FV Pallardo, J Vina. Zidovudine (AZT) causes an oxidation of mitochondrial DNA in mouse liver. Hepatology 29:985-987; 1999.
    • (1999) Hepatology , vol.29 , pp. 985-987
    • Asuncion, J.G.1    Olmo, M.L.2    Sastre, J.3    Pallardo, F.V.4    Vina, J.5
  • 31
    • 0019501881 scopus 로고
    • Adriamycin: A chemotherapeutic drug for malignancy treatment
    • RC Young, RF Ozols, CE Meyers. Adriamycin: A chemotherapeutic drug for malignancy treatment. N Eng J Med305:139-153; 1981.
    • (1981) N Eng J Med , vol.305 , pp. 139-153
    • Young, R.C.1    Ozols, R.F.2    Meyers, C.E.3
  • 32
    • 0023185692 scopus 로고
    • Effects of adriamycin on respiratory chain acitivités in mitochondria from rat liver, rat heart and bovine heart. Evidence for a preferential inhibition of complex III and IV
    • K Nicolay, B De Kruijff. Effects of adriamycin on respiratory chain acitivités in mitochondria from rat liver, rat heart and bovine heart. Evidence for a preferential inhibition of complex III and IV. Biochemica Biophysica Acta 892:320-330; 1987.
    • (1987) Biochemica Biophysica Acta , vol.892 , pp. 320-330
    • Nicolay, K.1    De Kruijff, B.2
  • 35
    • 0025856496 scopus 로고
    • The effect of copper deficiency on adriamycin toxicity
    • J Fischer, MA Johnson, RL Tackett. The effect of copper deficiency on adriamycin toxicity. Toxicol Lett 57:147-158; 1991.
    • (1991) Toxicol Lett , vol.57 , pp. 147-158
    • Fischer, J.1    Johnson, M.A.2    Tackett, R.L.3
  • 36
    • 0017649905 scopus 로고
    • Inhibition of the cardiac mitochondrial calcium pump by adriamycin in vitro
    • L Moore, EJ Landon, DA Cooney. Inhibition of the cardiac mitochondrial calcium pump by adriamycin in vitro. Biochem Med 18:131-138; 1977.
    • (1977) Biochem Med , vol.18 , pp. 131-138
    • Moore, L.1    Landon, E.J.2    Cooney, D.A.3
  • 37
    • 0023899815 scopus 로고
    • Mitochondrial sulfhydryl group modification by adriamycin aglycones
    • PM Sokolove. Mitochondrial sulfhydryl group modification by adriamycin aglycones. FEB 234:199-202; 1988.
    • (1988) FEB , vol.234 , pp. 199-202
    • Sokolove, P.M.1
  • 39
    • 0014802524 scopus 로고
    • Inhibition of thyroid hormone induction of mitochondrial a-glycerophosphate dehydrogenase in riboflavin deficiency
    • G Wolf, RS Rivlin. Inhibition of thyroid hormone induction of mitochondrial a-glycerophosphate dehydrogenase in riboflavin deficiency. Endocrinol 86:1347-1353; 1970.
    • (1970) Endocrinol , vol.86 , pp. 1347-1353
    • Wolf, G.1    Rivlin, R.S.2
  • 40
    • 0014851437 scopus 로고
    • Uncoupling action of sulfonylureas on brown fat cells
    • SS Chan, JN Fain. Uncoupling action of sulfonylureas on brown fat cells. Mol Pharmacol 6:513-523; 1970.
    • (1970) Mol Pharmacol , vol.6 , pp. 513-523
    • Chan, S.S.1    Fain, J.N.2
  • 42
    • 0031800882 scopus 로고    scopus 로고
    • Development of infrared imaging to measure thermogenesis in cell culture: Thermogenic effects of uncoupling protein-2, troglitazone and b-adrenergic agents
    • MA Paulik, RG Buckholz, ME Lancaster, WS Dallas, EA Hull-Ryde, JE Weiel, JM Lenhard. Development of infrared imaging to measure thermogenesis in cell culture: Thermogenic effects of uncoupling protein-2, troglitazone and b-adrenergic agents. Pharmaceutical Res 15:944-949; 1998.
    • (1998) Pharmaceutical Res , vol.15 , pp. 944-949
    • Paulik, M.A.1    Buckholz, R.G.2    Lancaster, M.E.3    Dallas, W.S.4    Hull-Ryde, E.A.5    Weiel, J.E.6    Lenhard, J.M.7
  • 44
    • 0015511661 scopus 로고
    • Oxidative phosphorylation and respiration by rat liver mitochondria from aspirin treated rats
    • MA Mehlman, RB Tobin, EM Sporn. Oxidative phosphorylation and respiration by rat liver mitochondria from aspirin treated rats. Biochem Pharmacol 21:3279-3285; 1972.
    • (1972) Biochem Pharmacol , vol.21 , pp. 3279-3285
    • Mehlman, M.A.1    Tobin, R.B.2    Sporn, E.M.3
  • 45
    • 85057663362 scopus 로고
    • The aspirin effect on respiration is due to its conversion to salicylic acid
    • L Thomkins, KH Lee. The aspirin effect on respiration is due to its conversion to salicylic acid. J Pharm Sci 58:102-106; 1969.
    • (1969) J Pharm Sci , vol.58 , pp. 102-106
    • Thomkins, L.1    Lee, K.H.2
  • 46
    • 0028190518 scopus 로고
    • Mitochondrial energy metabolism in chronic alcoholism
    • JB Hoek. Mitochondrial energy metabolism in chronic alcoholism. Curr Topics Bioenergetics 17:197-241; 1994.
    • (1994) Curr Topics Bioenergetics , vol.17 , pp. 197-241
    • Hoek, J.B.1
  • 48
    • 0021280363 scopus 로고
    • Biochemical and morphological alterations of baboon hepatic mitochondria after chronic ethanol consumption
    • M Arai, MA Leo, M Nakano, ER Gordon, CS Lieber. Biochemical and morphological alterations of baboon hepatic mitochondria after chronic ethanol consumption. Hepatology 4:165-174; 1984.
    • (1984) Hepatology , vol.4 , pp. 165-174
    • Arai, M.1    Leo, M.A.2    Nakano, M.3    Gordon, E.R.4    Lieber, C.S.5
  • 50
    • 0014483486 scopus 로고
    • Inhibition of hepatic gluconeogenesis by ethanol
    • HA Krebs, RA Freedland, R Hems, M Stubbs. Inhibition of hepatic gluconeogenesis by ethanol. Biochem J 112:117-124; 1969.
    • (1969) Biochem J , vol.112 , pp. 117-124
    • Krebs, H.A.1    Freedland, R.A.2    Hems, R.3    Stubbs, M.4
  • 52
    • 0026448725 scopus 로고
    • The discovery and development of HMG-CoA reductase inhibitors
    • A Endo. The discovery and development of HMG-CoA reductase inhibitors. J Lipid Res 33:1569-1562; 1992.
    • (1992) J Lipid Res , vol.33 , pp. 1562-1569
    • Endo, A.1
  • 54
    • 0029837064 scopus 로고    scopus 로고
    • Lipid lowering drugs and mitochondrial function: Effects of HMG-CoA reductase inhibitors on serum ubiquinone and blood lactate/pyruvate ratio
    • G De Pinieux, P Chariot, M Ammi-Said, F Louarn, JL Lejone, A Astier, B Jacotot, R Gherardi. Lipid lowering drugs and mitochondrial function: Effects of HMG-CoA reductase inhibitors on serum ubiquinone and blood lactate/pyruvate ratio. Br J Clin Pharmacol 42:333-337; 1996.
    • (1996) Br J Clin Pharmacol , vol.42 , pp. 333-337
    • De Pinieux, G.1    Chariot, P.2    Ammi-Said, M.3    Louarn, F.4    Lejone, J.L.5    Astier, A.6    Jacotot, B.7    Gherardi, R.8
  • 55
    • 0019870216 scopus 로고
    • Dose dependent stimulation of hepatic oxygen consumption and alanine conversion to CO2 and glucose by 3,5,3'-triiodo-L-thyronine (T3) in isolated perfused liver of hypothyroid rats
    • MJ Muller, HJ Seitz. Dose dependent stimulation of hepatic oxygen consumption and alanine conversion to CO2 and glucose by 3,5,3'-triiodo-L-thyronine (T3) in isolated perfused liver of hypothyroid rats. Life Sci 28:2243-2249; 1981.
    • (1981) Life Sci , vol.28 , pp. 2243-2249
    • Muller, M.J.1    Seitz, H.J.2
  • 56
    • 0020664853 scopus 로고
    • Effects of thyroid hormone on the gluconeogenic capacity of lipemic BHE rats
    • CD Berdanier. Effects of thyroid hormone on the gluconeogenic capacity of lipemic BHE rats. Proc Sco Exp Biol Med172:187-193; 1983.
    • (1983) Proc Sco Exp Biol Med , vol.172 , pp. 187-193
    • Berdanier, C.D.1
  • 58
    • 0019459877 scopus 로고
    • Effects of thyroid hormone on mitochondrial activity in lipemic BHE rats
    • CD Berdanier, D Shubeck. Effects of thyroid hormone on mitochondrial activity in lipemic BHE rats. Proc Soc Exp Biol Med166:348-354; 1981.
    • (1981) Proc Soc Exp Biol Med , vol.166 , pp. 348-354
    • Berdanier, C.D.1    Shubeck, D.2
  • 59
    • 0011246486 scopus 로고
    • The uncoupling of oxidative phosphorylation in rat liver mitochondria
    • HG Klemperer. The uncoupling of oxidative phosphorylation in rat liver mitochondria. Biochem J 60:122-128; 1955.
    • (1955) Biochem J , vol.60 , pp. 122-128
    • Klemperer, H.G.1
  • 60
    • 0025186853 scopus 로고
    • Thyroid-hormone control of state-3 respiration in isolated rat liver mitochondria
    • RP Hafner, GC Brown, MD Brand. Thyroid-hormone control of state-3 respiration in isolated rat liver mitochondria. Bio-chem J 265:731-734; 1990.
    • (1990) Bio-Chem J , vol.265 , pp. 731-734
    • Hafner, R.P.1    Brown, G.C.2    Brand, M.D.3
  • 61
    • 0029994180 scopus 로고    scopus 로고
    • Effect of thyroid state on characteristics determining the susceptibility to oxidative stress of mitochondrial fractions from rat liver
    • P Venditti, S Di Meo, T De Leo. Effect of thyroid state on characteristics determining the susceptibility to oxidative stress of mitochondrial fractions from rat liver. Cell Physiol Biochem 6:283-295; 1996.
    • (1996) Cell Physiol Biochem , vol.6 , pp. 283-295
    • Venditti, P.1    Di Meo, S.2    De Leo, T.3
  • 62
    • 0021848981 scopus 로고
    • Rapid thyroid-hormone effect on mitochondrial and cytosolic ATP/ADP ratios in the intact liver cell
    • HJ Seitz, MJ Muller, S Soboll. Rapid thyroid-hormone effect on mitochondrial and cytosolic ATP/ADP ratios in the intact liver cell. Biochem J 227:149-153; 1985.
    • (1985) Biochem J , vol.227 , pp. 149-153
    • Seitz, H.J.1    Muller, M.J.2    Soboll, S.3
  • 63
    • 0018032988 scopus 로고
    • Evaluation of oxidative phosphorylation in hearts from euthyroid, hypothyroid and hyperthyroid rats
    • K Nishiki, M Erecinska, DF Wilson, S Copper. Evaluation of oxidative phosphorylation in hearts from euthyroid, hypothyroid and hyperthyroid rats. Am J Physiol 235:C212-C219; 1978.
    • (1978) Am J Physiol , vol.235 , pp. C212-C219
    • Nishiki, K.1    Erecinska, M.2    Wilson, D.F.3    Copper, S.4
  • 64
    • 0025931997 scopus 로고
    • On the thyroid hormone-induced increase in respiratory capacity of isolated rat hepatocytes
    • RB Gregory, MN Berry. On the thyroid hormone-induced increase in respiratory capacity of isolated rat hepatocytes. Biochem Biophys Acta 1098:61-67; 1991.
    • (1991) Biochem Biophys Acta , vol.1098 , pp. 61-67
    • Gregory, R.B.1    Berry, M.N.2
  • 65
    • 0026755197 scopus 로고
    • Mechanism of loss of thermodynamic control in mitochondria due to hyperthyroidism and temperature
    • S Luvisetto, I Schmehl, E Intravaia, E Conti, GF Azzone. Mechanism of loss of thermodynamic control in mitochondria due to hyperthyroidism and temperature. J Biol Chem267:15348-15355; 1992.
    • (1992) J Biol Chem , vol.267 , pp. 15348-15355
    • Luvisetto, S.1    Schmehl, I.2    Intravaia, E.3    Conti, E.4    Azzone, G.F.5
  • 67
    • 0023616601 scopus 로고
    • The influence of nanomolar calcium ions and physiological levels of thyroid hormone on oxidative phosphorylation in rat liver mitochondria. A possible signal amplification mechanism
    • WE Thomas, A Crespo-Armas, J Mowbray. The influence of nanomolar calcium ions and physiological levels of thyroid hormone on oxidative phosphorylation in rat liver mitochondria. A possible signal amplification mechanism. Biochem J247:315-320; 1987.
    • (1987) Biochem J , vol.247 , pp. 315-320
    • Thomas, W.E.1    Crespo-Armas, A.2    Mowbray, J.3
  • 68
    • 0025827016 scopus 로고
    • Activation of respiration and loss of thermodynamic control in hyperthyroidism. Is it due to increased slipping of mitochondrial pumps?
    • S Luvisetto, I Schmehl, E Conti, E Intravaia, GF Azzone. Activation of respiration and loss of thermodynamic control in hyperthyroidism. Is it due to increased slipping of mitochondrial pumps? FEBS 291:17-20; 1991.
    • (1991) FEBS , vol.291 , pp. 17-20
    • Luvisetto, S.1    Schmehl, I.2    Conti, E.3    Intravaia, E.4    Azzone, G.F.5
  • 69
    • 0028915135 scopus 로고
    • Use of top-down elasticity analysis to identify sites of thyroid hormone-induced thermogenesis
    • ME Harper, MD Brand. Use of top-down elasticity analysis to identify sites of thyroid hormone-induced thermogenesis. Proc Soc Exp Biol Med 208:228-237; 1995.
    • (1995) Proc Soc Exp Biol Med , vol.208 , pp. 228-237
    • Harper, M.E.1    Brand, M.D.2
  • 70
    • 0018501038 scopus 로고
    • Early effects of thyroidectomy and triiodothyronine administration on rat liver mitochondria
    • J Bouhnik, J-P Clot, M Baudry, R Michel. Early effects of thyroidectomy and triiodothyronine administration on rat liver mitochondria. Mol Cell Endocrinol 15:1-12; 1979.
    • (1979) Mol Cell Endocrinol , vol.15 , pp. 1-12
    • Bouhnik, J.1    Clot, J.-P.2    Baudry, M.3    Michel, R.4
  • 71
    • 0018403085 scopus 로고
    • Thyroid hormone action at the cell level
    • K Sterling. Thyroid hormone action at the cell level. N Eng J Med 300:117-123; 173-177; 1979.
    • (1979) N Eng J Med , vol.300 , Issue.117-123 , pp. 173-177
    • Sterling, K.1
  • 72
    • 84998344212 scopus 로고
    • Deterioration of mitochondrial function in heart muscles of rats with hypothyroidism
    • S Sugiyama, T Kato, T Ozawa, K Yagi. Deterioration of mitochondrial function in heart muscles of rats with hypothyroidism. J Clin Biochem Nutr 11:199-204; 1991.
    • (1991) J Clin Biochem Nutr , vol.11 , pp. 199-204
    • Sugiyama, S.1    Kato, T.2    Ozawa, T.3    Yagi, K.4
  • 73
    • 0021260659 scopus 로고
    • Alterations of oxidative phosphorylation reactions in mitochondria isolated from hypothyroid rat liver
    • I Ezawa, M Yamamoto, S Kimura, E Ogata. Alterations of oxidative phosphorylation reactions in mitochondria isolated from hypothyroid rat liver. Eur J Biochem 141:9-13; 1984.
    • (1984) Eur J Biochem , vol.141 , pp. 9-13
    • Ezawa, I.1    Yamamoto, M.2    Kimura, S.3    Ogata, E.4
  • 74
    • 0026020972 scopus 로고
    • The effect of thyroid state and cold exposure on rat liver oxidative phosphorylation
    • S Iossa, A Barletta, G Liverini. The effect of thyroid state and cold exposure on rat liver oxidative phosphorylation. Mol Cell Endocrinol 75:15-18; 1991.
    • (1991) Mol Cell Endocrinol , vol.75 , pp. 15-18
    • Iossa, S.1    Barletta, A.2    Liverini, G.3
  • 75
    • 0019439493 scopus 로고
    • Thyroid control over biomembranes: Vi lipids in liver mitochondria and microsomes of hypothyroid rats
    • FL Hoch, C Subramanian, GA Dhopeshwarkar, JF Mead. Thyroid control over biomembranes: Vi lipids in liver mitochondria and microsomes of hypothyroid rats. Lipids 16:328-335; 1981.
    • (1981) Lipids , vol.16 , pp. 328-335
    • Hoch, F.L.1    Subramanian, C.2    Dhopeshwarkar, G.A.3    Mead, J.F.4
  • 76
    • 0026009326 scopus 로고
    • Hypothyroidism and thyroxin substitution affect the n-3 fatty acid composition of rat liver mitochondria
    • D Raederstorff, CA Meier, U Moser, P Walter. Hypothyroidism and thyroxin substitution affect the n-3 fatty acid composition of rat liver mitochondria. Lipids 26:781-787; 1991.
    • (1991) Lipids , vol.26 , pp. 781-787
    • Raederstorff, D.1    Meier, C.A.2    Moser, U.3    Walter, P.4
  • 77
    • 0026068262 scopus 로고
    • The influence of hypothyroidism on the transport of phosphate and on the lipid composition in rat liver mitochondria
    • G Paradies, FM Ruggiero, P Dinoi. The influence of hypothyroidism on the transport of phosphate and on the lipid composition in rat liver mitochondria. Biochem Biophys Acta1070:180-189; 1991.
    • (1991) Biochem Biophys Acta , vol.1070 , pp. 180-189
    • Paradies, G.1    Ruggiero, F.M.2    Dinoi, P.3
  • 78
    • 0019129219 scopus 로고
    • Thyroid control over biomembranes. Liver microsomal cytochrome b5 in hypothyroidism
    • FL Hoch, JW Depierre, L Ernster. Thyroid control over biomembranes. Liver microsomal cytochrome b5 in hypothyroidism. Eur J Biochem 109:301-306; 1980.
    • (1980) Eur J Biochem , vol.109 , pp. 301-306
    • Hoch, F.L.1    Depierre, J.W.2    Ernster, L.3
  • 79
    • 0023261274 scopus 로고
    • The influence of dietary fatty acids and hypothyroidism on mitochondrial fatty acid composition
    • KW Withers, AJ Hubert. The influence of dietary fatty acids and hypothyroidism on mitochondrial fatty acid composition. Nutr Res 7:1139-1159; 1987.
    • (1987) Nutr Res , vol.7 , pp. 1139-1159
    • Withers, K.W.1    Hubert, A.J.2
  • 80
    • 0019951753 scopus 로고
    • The metabolism of fatty acids in hepatocytes isolated from triiodothyronine-treated rats
    • JA Stakkestad, J Bremer. The metabolism of fatty acids in hepatocytes isolated from triiodothyronine-treated rats. Bio-chem Biophys Acta 711:90-100; 1982.
    • (1982) Bio-Chem Biophys Acta , vol.711 , pp. 90-100
    • Stakkestad, J.A.1    Bremer, J.2
  • 81
    • 0021346839 scopus 로고
    • Lipid composition of liver mitochondria and microsomes in hyperthyroid rats
    • FM Ruggiero, C Landriscina, GV Gnoni, E Quagiariello. Lipid composition of liver mitochondria and microsomes in hyperthyroid rats. Lipids 19:171-178; 1984.
    • (1984) Lipids , vol.19 , pp. 171-178
    • Ruggiero, F.M.1    Landriscina, C.2    Gnoni, G.V.3    Quagiariello, E.4
  • 82
    • 0028868130 scopus 로고
    • Thyroid hormone treatment alters phospholipid composition and membrane fluidity of rat brain mitochondria
    • CS Bangur, JL Howland, SS Kattare. Thyroid hormone treatment alters phospholipid composition and membrane fluidity of rat brain mitochondria. Biochem J 305:9-32; 1995.
    • (1995) Biochem J , vol.305 , pp. 9-32
    • Bangur, C.S.1    Howland, J.L.2    Kattare, S.S.3
  • 83
    • 0024575096 scopus 로고
    • Influence of thyroid status on the membranes of rat liver mitochondria. Unique localization of L-glycerol-3-phosphate dehydrogenase
    • Z Beleznai, E Amler, H Rauchova, Z Drahota, V Janecsik. Influence of thyroid status on the membranes of rat liver mitochondria. Unique localization of L-glycerol-3-phosphate dehydrogenase. FEB 243:247-250; 1989.
    • (1989) FEB , vol.243 , pp. 247-250
    • Beleznai, Z.1    Amler, E.2    Rauchova, H.3    Drahota, Z.4    Janecsik, V.5
  • 84
    • 0025260953 scopus 로고
    • Enhanced activity of the tricarbox-ylate carrier and modification of lipids in hepatic mitochondria from hyperthyroid rats
    • G Paradies, FM Ruggiero. Enhanced activity of the tricarbox-ylate carrier and modification of lipids in hepatic mitochondria from hyperthyroid rats. Arch Biochem Biophys 278:425-430; 1990.
    • (1990) Arch Biochem Biophys , vol.278 , pp. 425-430
    • Paradies, G.1    Ruggiero, F.M.2
  • 85
    • 0021174622 scopus 로고
    • Response of hepatic mitochondrial a-glycerophosphate dehydrogenase and malic enzyme to constant infusions of L-triiodothyronine in rats bearing the Walker 256 carcinoma. Evidence for the divergent postreceptor regulation of the thyroid hormone response
    • JM Tibaldi, N Sahnoun, MI Surks. Response of hepatic mitochondrial a-glycerophosphate dehydrogenase and malic enzyme to constant infusions of L-triiodothyronine in rats bearing the Walker 256 carcinoma. Evidence for the divergent postreceptor regulation of the thyroid hormone response. J Clin Invest 74:705-714; 1984.
    • (1984) J Clin Invest , vol.74 , pp. 705-714
    • Tibaldi, J.M.1    Sahnoun, N.2    Surks, M.I.3
  • 86
    • 0000341119 scopus 로고
    • Enhanced oxidation of a-glycerophosphate by mitochondria of thyroid-fed rats
    • Y-P Lee, AE Takemori, H Lardy. Enhanced oxidation of a-glycerophosphate by mitochondria of thyroid-fed rats. J Biol Chem 234:3051-3055; 1959.
    • (1959) J Biol Chem , vol.234 , pp. 3051-3055
    • Lee, Y.-P.1    Takemori, A.E.2    Lardy, H.3
  • 87
    • 0017325774 scopus 로고
    • Stimulation of hepatic mitochondrial a-glycerophosphate dehydrogenase and malic enzyme by L-triiodothyronine. Characteristics of the response with specific nuclear thyroid hormone binding sites fully saturated
    • JH Oppenheimer, E Silva, HL Schwartz, MI Surks. Stimulation of hepatic mitochondrial a-glycerophosphate dehydrogenase and malic enzyme by L-triiodothyronine. Characteristics of the response with specific nuclear thyroid hormone binding sites fully saturated. J Clin Invest 59:517-527; 1977.
    • (1977) J Clin Invest , vol.59 , pp. 517-527
    • Oppenheimer, J.H.1    Silva, E.2    Schwartz, H.L.3    Surks, M.I.4
  • 88
    • 0017277605 scopus 로고
    • Sensitivity of mitochondrial a-glycerophosphate dehydrogenase to thyroid hormone in skeletal muscle of the rat
    • C van Hardeveld, R Rusche, AAH Kassenaar. Sensitivity of mitochondrial a-glycerophosphate dehydrogenase to thyroid hormone in skeletal muscle of the rat. Horm Metab Res8:153-154; 1976.
    • (1976) Horm Metab Res , vol.8 , pp. 153-154
    • Van Hardeveld, C.1    Rusche, R.2    Kassenaar, A.A.H.3
  • 89
    • 0014984674 scopus 로고
    • Thyroid control over mitochondrial a-glycerophosphate dehydrogenase in rat liver as a function of age
    • B Bulos, B Saktor, IW Grossman, N Altman. Thyroid control over mitochondrial a-glycerophosphate dehydrogenase in rat liver as a function of age. J Gerontol 26:13-19; 1971.
    • (1971) J Gerontol , vol.26 , pp. 13-19
    • Bulos, B.1    Saktor, B.2    Grossman, I.W.3    Altman, N.4
  • 90
    • 0028080098 scopus 로고
    • Cloning of a cDNA for the FAD-linked glycerol-3-phosphate dehydrogenase from rat liver and its regulation by thyroid hormones
    • S Muller, HJ Seitz. Cloning of a cDNA for the FAD-linked glycerol-3-phosphate dehydrogenase from rat liver and its regulation by thyroid hormones. Proc Nat Acad Sci USA91:10581-10585; 1994.
    • (1994) Proc Nat Acad Sci USA , vol.91 , pp. 10581-10585
    • Muller, S.1    Seitz, H.J.2
  • 91
    • 0023722875 scopus 로고
    • Thyroid hormone effect on gene expression of the adenine nucleotide translocase in different rat tissues
    • W Hoppner, UB Rasmussen, G Abuerreish, H Wohlrab, HJ Seitz. Thyroid hormone effect on gene expression of the adenine nucleotide translocase in different rat tissues. Mol Endocrinol2:1127-1131; 1988.
    • (1988) Mol Endocrinol , vol.2 , pp. 1127-1131
    • Hoppner, W.1    Rasmussen, U.B.2    Abuerreish, G.3    Wohlrab, H.4    Seitz, H.J.5
  • 92
    • 0026693011 scopus 로고
    • The mechanism of the increase in mitochondrial proton permeability induced by thyroid hormones
    • MD Brand, D Steverding, B Kadenbach, PM Stevenson, RP Hafner. The mechanism of the increase in mitochondrial proton permeability induced by thyroid hormones. Eur J Biochem206:775-781; 1992.
    • (1992) Eur J Biochem , vol.206 , pp. 775-781
    • Brand, M.D.1    Steverding, D.2    Kadenbach, B.3    Stevenson, P.M.4    Hafner, R.P.5
  • 93
    • 0019301217 scopus 로고
    • Ion transport in liver mitochondria from normal and thyroxine-treated rats
    • SB Shears, JR Bronk. Ion transport in liver mitochondria from normal and thyroxine-treated rats. J Bioenergetics Biomembranes 12:379-393; 1980.
    • (1980) J Bioenergetics Biomembranes , vol.12 , pp. 379-393
    • Shears, S.B.1    Bronk, J.R.2
  • 94
    • 0031829828 scopus 로고    scopus 로고
    • 3,5,3'-triiodothyro-nine induces mitochondrial permeability transition mediated by reactive oxygen species and membrane protein thiol oxidation
    • RF Castilho, AJ Kowaltowski, AE Vercesi. 3,5,3'-triiodothyro-nine induces mitochondrial permeability transition mediated by reactive oxygen species and membrane protein thiol oxidation. Arch Biochem Biophys 354:151-157; 1998.
    • (1998) Arch Biochem Biophys , vol.354 , pp. 151-157
    • Castilho, R.F.1    Kowaltowski, A.J.2    Vercesi, A.E.3
  • 95
    • 0025072728 scopus 로고
    • Stimulation of phosphate transport in rat-liver mitochondria by thyroid hormones
    • G Paradies, FM Ruggiero. Stimulation of phosphate transport in rat-liver mitochondria by thyroid hormones. Biochim Bio-phys Acta 1019:133-136; 1990.
    • (1990) Biochim Bio-Phys Acta , vol.1019 , pp. 133-136
    • Paradies, G.1    Ruggiero, F.M.2
  • 97
    • 0019503383 scopus 로고
    • Influence of diet composition on serum triiodothyronine (T3) concentration, hepatic mitochondrial metabolism and shuttle system activity in rats
    • RS Tyzbir, AS Kunin, NM Sims, E Danforth. Influence of diet composition on serum triiodothyronine (T3) concentration, hepatic mitochondrial metabolism and shuttle system activity in rats. J Nutr 111:252-259; 1981.
    • (1981) J Nutr , vol.111 , pp. 252-259
    • Tyzbir, R.S.1    Kunin, A.S.2    Sims, N.M.3    Danforth, E.4
  • 98
    • 0022493282 scopus 로고
    • Diet effects on mitochondrial phospholipid fatty acids and mitochondrial function in BHE rats
    • OE Deaver, RC Wander, RH McCusker, CD Berdanier. Diet effects on mitochondrial phospholipid fatty acids and mitochondrial function in BHE rats. J Nutr 116:1148-1155; 1986.
    • (1986) J Nutr , vol.116 , pp. 1148-1155
    • Deaver, O.E.1    Wander, R.C.2    McCusker, R.H.3    Berdanier, C.D.4
  • 99
    • 0021929791 scopus 로고
    • Effects of dietary carbohydrate on mitochondrial composition and function in two strains of rats
    • RC Wander, CD Berdanier. Effects of dietary carbohydrate on mitochondrial composition and function in two strains of rats. J Nutr 115:190-199; 1985.
    • (1985) J Nutr , vol.115 , pp. 190-199
    • Wander, R.C.1    Berdanier, C.D.2
  • 100
    • 0024412445 scopus 로고
    • The impact of nutrition on thyroid hormone physiology and action
    • E Danforth, AG Burger. The impact of nutrition on thyroid hormone physiology and action. Annu Rev Nutr 9:210-227; 1989.
    • (1989) Annu Rev Nutr , vol.9 , pp. 210-227
    • Danforth, E.1    Burger, A.G.2
  • 101
    • 0022352562 scopus 로고
    • Hepatic proliferation of mitochopndria in response to a high protein diet
    • R Didier, C Remesy, C Demigne, P Fafournoux. Hepatic proliferation of mitochopndria in response to a high protein diet. Nutr Res 5:1093-1102; 1985.
    • (1985) Nutr Res , vol.5 , pp. 1093-1102
    • Didier, R.1    Remesy, C.2    Demigne, C.3    Fafournoux, P.4
  • 102
    • 0021762762 scopus 로고
    • Nutritional effects on mitochondrial bioenergetics. Alterations in oxidative phosphorylation by rat liver mitochondria
    • J Ferreira, L Gil. Nutritional effects on mitochondrial bioenergetics. Alterations in oxidative phosphorylation by rat liver mitochondria. Biochem J 218:61-67; 1984.
    • (1984) Biochem J , vol.218 , pp. 61-67
    • Ferreira, J.1    Gil, L.2
  • 103
    • 0029176035 scopus 로고
    • Functional aspects of oxidative phosphorylation and electron transport in cardiac mitochondria of copper deficient rats
    • JM Matz, JT Saari, AM Bode. Functional aspects of oxidative phosphorylation and electron transport in cardiac mitochondria of copper deficient rats. J Nutr Biochem 6:644-652; 1995.
    • (1995) J Nutr Biochem , vol.6 , pp. 644-652
    • Matz, J.M.1    Saari, J.T.2    Bode, A.M.3
  • 104
    • 0029111661 scopus 로고
    • Marginal copper-restricted diets produce altered cardiac ultrastructure in the rat
    • REC Wildman, R Hopkins, ML Failla, DM Medeiros. Marginal copper-restricted diets produce altered cardiac ultrastructure in the rat. Proc Soc Exp Biol Med 210:43-49; 1995.
    • (1995) Proc Soc Exp Biol Med , vol.210 , pp. 43-49
    • Wildman, R.1    Hopkins, R.2    Failla, M.L.3    Medeiros, D.M.4
  • 105
    • 0028816445 scopus 로고
    • Altered nucleotide content and changes in mitochondrial energy states associated with copper deficiency in rat platelets
    • WT Johnson, SN Dufault, SM Neuman. Altered nucleotide content and changes in mitochondrial energy states associated with copper deficiency in rat platelets. J Nutr Biochem6:551-556; 1995.
    • (1995) J Nutr Biochem , vol.6 , pp. 551-556
    • Johnson, W.T.1    Dufault, S.N.2    Neuman, S.M.3
  • 106
    • 0027221487 scopus 로고
    • Oxygen dependence of redox state of copper in cytochrome oxidase
    • Y Hoshi, O Hazeki, M Tamura. Oxygen dependence of redox state of copper in cytochrome oxidase in vitro. J Appl Physiol74:1622-1627; 1993.
    • (1993) Vitro. J Appl Physiol , vol.74 , pp. 1622-1627
    • Hoshi, Y.1    Hazeki, O.2    Tamura, M.3
  • 107
    • 0024443065 scopus 로고
    • Influence of menhaden oil on mitochondrial respiration in BHE rats
    • M-JC Kim, CD Berdanier. Influence of menhaden oil on mitochondrial respiration in BHE rats. Proc Soc Exp Biol Med192:172-1176; 1989.
    • (1989) Proc Soc Exp Biol Med , vol.192 , pp. 172-1176
    • Kim, M.-J.1    Berdanier, C.D.2
  • 108
    • 0031952581 scopus 로고    scopus 로고
    • Nutrient-gene interactions determine mitochondrial function: Effect of dietary fat
    • M-JC Kim, CD Berdanier. Nutrient-gene interactions determine mitochondrial function: Effect of dietary fat. FASEB J12:243-248; 1998.
    • (1998) FASEB J , vol.12 , pp. 243-248
    • Kim, M.-J.1    Berdanier, C.D.2
  • 109
    • 0029129862 scopus 로고
    • Menhaden oil feeding increases potential for renal free radical production in BHE/cdb rats
    • K Wickwire, K Kras, C Gunnett, D Hartle, CD Berdanier. Menhaden oil feeding increases potential for renal free radical production in BHE/cdb rats. Proc Soc Exp Biol Med209:397-402; 1995.
    • (1995) Proc Soc Exp Biol Med , vol.209 , pp. 397-402
    • Wickwire, K.1    Kras, K.2    Gunnett, C.3    Hartle, D.4    Berdanier, C.D.5
  • 110
    • 0026778034 scopus 로고
    • Lifespan is shortened in BHE/cdb rats fed a diet containing 9% menhaden oil and 1% corn oil
    • CD Berdanier, B Johnson, DK Hartle, WA Crowell. Lifespan is shortened in BHE/cdb rats fed a diet containing 9% menhaden oil and 1% corn oil. J Nutr 122:1109-1131; 1992.
    • (1992) J Nutr , vol.122 , pp. 1109-1131
    • Berdanier, C.D.1    Johnson, B.2    Hartle, D.K.3    Crowell, W.A.4
  • 111
    • 0026040225 scopus 로고
    • Selective inhibition of NADH-CoQ oxidoreductase (Complex I) of rat brain mitochondria by arachidonic acid
    • H Morii, Y Takeuchi, Y Watanabe. Selective inhibition of NADH-CoQ oxidoreductase (complex I) of rat brain mitochondria by arachidonic acid. Biochem Biophys Res Commun178:1120-1126; 1991.
    • (1991) Biochem Biophys Res Commun , vol.178 , pp. 1120-1126
    • Morii, H.1    Takeuchi, Y.2    Watanabe, Y.3
  • 112
    • 0022547043 scopus 로고
    • Free fatty acids decouple oxidative phosphorylation by dissipating intramembranal protons without inhibiting ATP synthesis driven by the proton electrochemical gradient
    • H Rottenberg, S Steiner-Mordoch. Free fatty acids decouple oxidative phosphorylation by dissipating intramembranal protons without inhibiting ATP synthesis driven by the proton electrochemical gradient. FEBS 202:314-318; 1986.
    • (1986) FEBS , vol.202 , pp. 314-318
    • Rottenberg, H.1    Steiner-Mordoch, S.2
  • 113
    • 0022517409 scopus 로고
    • Fatty acid uncoupling of oxidative phosphorylation in rat liver mitochondria
    • H Rottenberg, K Hashimoto. Fatty acid uncoupling of oxidative phosphorylation in rat liver mitochondria. Biochemistry25:1747-1755; 1986.
    • (1986) Biochemistry , vol.25 , pp. 1747-1755
    • Rottenberg, H.1    Hashimoto, K.2
  • 114
    • 0024413816 scopus 로고
    • Nutrient supply and mitochondrial function
    • TY Aw, DP Jones. Nutrient supply and mitochondrial function. Annu Rev Nutr 9:229-251; 1989.
    • (1989) Annu Rev Nutr , vol.9 , pp. 229-251
    • Aw, T.Y.1    Jones, D.P.2
  • 115
    • 0019404223 scopus 로고
    • Biochemical adaptation of mitochondria, muscle and whole animal respiration to endurance training
    • KJA Davies, L Packer, GA Brooks. Biochemical adaptation of mitochondria, muscle and whole animal respiration to endurance training. Arch Biochem Biophys 209:539-554; 1981.
    • (1981) Arch Biochem Biophys , vol.209 , pp. 539-554
    • Davies, K.1    Packer, L.2    Brooks, G.A.3
  • 116
    • 0020299664 scopus 로고
    • Exercise induced alterations of hepatic mitochondrial function
    • CA Tate, PE Wolkowicz, J McMillin-Wood. Exercise induced alterations of hepatic mitochondrial function. Biochem J208:695-701; 1982.
    • (1982) Biochem J , vol.208 , pp. 695-701
    • Tate, C.A.1    Wolkowicz, P.E.2    McMillin-Wood, J.3
  • 118
    • 0030874890 scopus 로고    scopus 로고
    • ADP-regulation of mitochondrial free radical production is different with complex I or complex II-linked substrates: Implications for the exercise paradox and brain hypermetabolism
    • A Herrero, G Barja. ADP-regulation of mitochondrial free radical production is different with complex I or complex II-linked substrates: Implications for the exercise paradox and brain hypermetabolism. J Bioenergetics Biomembranes 29:241-249; 1997.
    • (1997) J Bioenergetics Biomembranes , vol.29 , pp. 241-249
    • Herrero, A.1    Barja, G.2
  • 119
    • 0029793882 scopus 로고    scopus 로고
    • Extreme exercise and oxidative DNA modification
    • HE Poulson, S Loft, K Vistisen. Extreme exercise and oxidative DNA modification. J Sports Sci 14:343-346; 1996.
    • (1996) J Sports Sci , vol.14 , pp. 343-346
    • Poulson, H.E.1    Loft, S.2    Vistisen, K.3
  • 120
    • 0018173419 scopus 로고
    • Glucagon-induced stimulation of 2-oxoglutarate metabolism in mitochondria from rat liver
    • EA Siess, OH Wieland. Glucagon-induced stimulation of 2-oxoglutarate metabolism in mitochondria from rat liver. FEBS Lett 93:301-306; 1978.
    • (1978) FEBS Lett , vol.93 , pp. 301-306
    • Siess, E.A.1    Wieland, O.H.2
  • 121
    • 0020964243 scopus 로고
    • Stimulation of mitochondrial functions by glucagon treatment. Evidence that effects are not artifacts of mitochondrial isolation
    • CB Jensen, FD Sistare, HC Hamman, RC Haynes. Stimulation of mitochondrial functions by glucagon treatment. Evidence that effects are not artifacts of mitochondrial isolation. Bio-chem J 210:819-827; 1983.
    • (1983) Bio-Chem J , vol.210 , pp. 819-827
    • Jensen, C.B.1    Sistare, F.D.2    Hamman, H.C.3    Haynes, R.C.4
  • 122
    • 0025633299 scopus 로고
    • Stimulation of the electron transport chain in mitochondria isolated from rats treated with mannoheptulose or glucagon
    • MD Brand, L D’Alessandri, HMGPV Reis, RP Hafner. Stimulation of the electron transport chain in mitochondria isolated from rats treated with mannoheptulose or glucagon. Arch Bio-chem Biophys 283:278-284; 1990.
    • (1990) Arch Bio-Chem Biophys , vol.283 , pp. 278-284
    • Brand, M.D.1    D’Alessandri, L.2    Reis, H.M.3    Hafner, R.P.4
  • 123
    • 85057655905 scopus 로고    scopus 로고
    • DHEA and mitochondrial respiration
    • (M Kalimi and W Regelson, Eds.) Walter de Gruyter & Co, Berlin
    • CD Berdanier, WF Flatt. DHEA and mitochondrial respiration. In: Dehydroepiandrosterone (M Kalimi and W Regelson, Eds.) Walter de Gruyter & Co, Berlin. 377-391; 2000.
    • (2000) Dehydroepiandrosterone , pp. 377-391
    • Berdanier, C.D.1    Flatt, W.F.2
  • 124
    • 0021067382 scopus 로고
    • Stimulation of hepatic oxidative phosphorylation following dexamethasone treatment of rats
    • EH Allen, AB Chisholm, MA Titheradge. Stimulation of hepatic oxidative phosphorylation following dexamethasone treatment of rats. Biochem Biophys Acta 725:71-76; 1983.
    • (1983) Biochem Biophys Acta , vol.725 , pp. 71-76
    • Allen, E.H.1    Chisholm, A.B.2    Titheradge, M.A.3
  • 125
    • 0344287290 scopus 로고
    • Uncoupling of oxidative phosphorylation in rat liver mitochondria by general anesthetics
    • H Rottenberg. Uncoupling of oxidative phosphorylation in rat liver mitochondria by general anesthetics. Proc Nat Acad Sci USA 80:3313-3317; 1983.
    • (1983) Proc Nat Acad Sci USA , vol.80 , pp. 3313-3317
    • Rottenberg, H.1
  • 126
    • 0021928031 scopus 로고
    • Cooperativity in inhibition of coupled and uncoupled respiration in rat liver and brain mitochondria by imipramine
    • RR Rajan, SS Katyare. Cooperativity in inhibition of coupled and uncoupled respiration in rat liver and brain mitochondria by imipramine. Indian J Biochem Biophys 22:71-77; 1985.
    • (1985) Indian J Biochem Biophys , vol.22 , pp. 71-77
    • Rajan, R.R.1    Katyare, S.S.2
  • 127
    • 0024588205 scopus 로고
    • Oxidative and nonoxidative mechanisms in the inactivation of cardiac mitochondrial electron transport chain components by doxirubicin
    • O Marcillat, Y Zhang, KJA Davies. Oxidative and nonoxidative mechanisms in the inactivation of cardiac mitochondrial electron transport chain components by doxirubicin. Biochem J259:181-189; 1989.
    • (1989) Biochem J , vol.259 , pp. 181-189
    • Marcillat, O.1    Zhang, Y.2    Davies, K.J.A.3
  • 129
    • 0025990161 scopus 로고
    • Mitochondrial bioenergetics as affected by DDT
    • AJM Moreno, VMC Madeira. Mitochondrial bioenergetics as affected by DDT. Biochem Biophys Acta 1060:166-174; 1991.
    • (1991) Biochem Biophys Acta , vol.1060 , pp. 166-174
    • Moreno, A.1    Madeira, V.M.C.2
  • 130
    • 0034625498 scopus 로고    scopus 로고
    • Rapid and transient inhibition of mitochondrial function following methamphet-amine or 3,4-methylenedioxymethamphetamine administration
    • KB Burrows, G Gudelsky, BK Yamamoto. Rapid and transient inhibition of mitochondrial function following methamphet-amine or 3,4-methylenedioxymethamphetamine administration. Eur J Pharmacol 9:11-18; 2000.
    • (2000) Eur J Pharmacol , vol.9 , pp. 11-18
    • Burrows, K.B.1    Gudelsky, G.2    Yamamoto, B.K.3
  • 131
    • 0028223609 scopus 로고
    • Low levels of mitochondrial transcription factor A in mitochondrial depletion
    • N-G Larsson, A Oldfors, E Holme, DA Clayton. Low levels of mitochondrial transcription factor A in mitochondrial depletion. Biochem Biophys Res Comm 200:1374-1381; 1994.
    • (1994) Biochem Biophys Res Comm , vol.200 , pp. 1374-1381
    • Larsson, N.-G.1    Oldfors, A.2    Holme, E.3    Clayton, D.A.4
  • 132
    • 0345493790 scopus 로고    scopus 로고
    • Autonomous regulation in mammalian mitochondrial DNA transcription
    • JA Enriquez, P Fernandez-Silva, J Montoya. Autonomous regulation in mammalian mitochondrial DNA transcription. Biol Chem 380:737-747; 1999.
    • (1999) Biol Chem , vol.380 , pp. 737-747
    • Enriquez, J.A.1    Fernandez-Silva, P.2    Montoya, J.3
  • 133
    • 0025230267 scopus 로고
    • Novel regulatory enhancer in the nuclear gene of human mitochondrial ATP synthase ß-subunit
    • H Tomura, H Endo, Y Kagawa, S Ohta. Novel regulatory enhancer in the nuclear gene of human mitochondrial ATP synthase ß-subunit. J Biol Chem 265:6525-6529; 1990.
    • (1990) J Biol Chem , vol.265 , pp. 6525-6529
    • Tomura, H.1    Endo, H.2    Kagawa, Y.3    Ohta, S.4
  • 134
    • 0028011017 scopus 로고
    • Activation of the human mitochondrial transcription factor A gene by nuclear respiratory factors. A potential regulatory link between nuclear and mitochondrial gene expression in organelle biogenesis
    • JV Verbasius, RC Scarpulla. Activation of the human mitochondrial transcription factor A gene by nuclear respiratory factors. A potential regulatory link between nuclear and mitochondrial gene expression in organelle biogenesis. Proc Natl Acad Sci USA 91:1309-1312; 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1309-1312
    • Verbasius, J.V.1    Scarpulla, R.C.2
  • 135
    • 0025313512 scopus 로고
    • NRF-1: A trans-activator of nuclear-encoded respiratory genes in animal cells
    • MJ Evans, RC Scarpulla. NRF-1: A trans-activator of nuclear-encoded respiratory genes in animal cells. Genes Dev4:1023-1034; 1990.
    • (1990) Genes Dev , vol.4 , pp. 1023-1034
    • Evans, M.J.1    Scarpulla, R.C.2
  • 136
    • 0026656327 scopus 로고
    • Nuclear respiratory factor 1 activation sites in genes encoding the (Subunit of ATP synthase, eukaryotic initiation factor 2a and tyrosine aminotransferase: Specific interaction of purified NRF-1 with multiple target genes
    • CA Chau, MJ Evans, RC Scarpulla. Nuclear respiratory factor 1 activation sites in genes encoding the subunit of ATP synthase, eukaryotic initiation factor 2a and tyrosine aminotransferase: Specific interaction of purified NRF-1 with multiple target genes. J Biol Chem 267:6999-7002; 1992.
    • (1992) J Biol Chem , vol.267 , pp. 6999-7002
    • Chau, C.A.1    Evans, M.J.2    Scarpulla, R.C.3
  • 137
    • 0027135555 scopus 로고
    • NRF-1, an activator involved in nuclear-mitochondrial interactions, utilizes a new DNA binding domain conserved in a family of developmental regulators
    • CA Virbasius, JV Virbasius, RC Scarpulla. NRF-1, an activator involved in nuclear-mitochondrial interactions, utilizes a new DNA binding domain conserved in a family of developmental regulators. Genes Dev 7:2431-2436; 1993.
    • (1993) Genes Dev , vol.7 , pp. 2431-2436
    • Virbasius, C.A.1    Virbasius, J.V.2    Scarpulla, R.C.3
  • 138
    • 0033551701 scopus 로고    scopus 로고
    • Coordinate induction of energy gene expression in tissues of mitochondrial disease patients
    • A Heddi, G Stepien, PJ Benke, DC Wallace. Coordinate induction of energy gene expression in tissues of mitochondrial disease patients. J Biol Chem 274:22968-22976; 1999.
    • (1999) J Biol Chem , vol.274 , pp. 22968-22976
    • Heddi, A.1    Stepien, G.2    Benke, P.J.3    Wallace, D.C.4
  • 139
    • 0030624426 scopus 로고    scopus 로고
    • Mitochondrial gene expression in rat heart and liver during growth and development
    • J Marin-Garcia, R Ananthakrishnan, MJ Goldenthal. Mitochondrial gene expression in rat heart and liver during growth and development. Biochem Cell Biol 75:137-142; 1997.
    • (1997) Biochem Cell Biol , vol.75 , pp. 137-142
    • Marin-Garcia, J.1    Ananthakrishnan, R.2    Goldenthal, M.J.3
  • 140
    • 0029586075 scopus 로고
    • Mt mRNA stability regulates the expression of the mitochondrial genome during liver development
    • LK Ostronoff, JM Izquierdo, JM Cuezva. Mt mRNA stability regulates the expression of the mitochondrial genome during liver development. Biochem Biophys Res Com 217:1094-1098; 1995.
    • (1995) Biochem Biophys Res Com , vol.217 , pp. 1094-1098
    • Ostronoff, L.K.1    Izquierdo, J.M.2    Cuezva, J.M.3
  • 141
    • 0029971074 scopus 로고    scopus 로고
    • Transient activation of mitochondrial translation regulates the expression of the mitochondrial genome during mammalian mitochondrial differentiation
    • LK Ostronoff, JM Izquierdo, JA Enriquez, J Montoya, JM Cuezva. Transient activation of mitochondrial translation regulates the expression of the mitochondrial genome during mammalian mitochondrial differentiation. Biochem J316:183-191; 1996.
    • (1996) Biochem J , vol.316 , pp. 183-191
    • Ostronoff, L.K.1    Izquierdo, J.M.2    Enriquez, J.A.3    Montoya, J.4    Cuezva, J.M.5
  • 142
    • 0028948840 scopus 로고
    • Changing patterns of transcriptional and post-transcriptional control of ß-F1 ATP synthase gene expression during mitochondrial biogenesis in liver
    • JM Izquierdo, J Ricart, LK Ostronoff, G Egea, JM Cuezva. Changing patterns of transcriptional and post-transcriptional control of ß-F1 ATP synthase gene expression during mitochondrial biogenesis in liver. J Biol Chem 270:10342-10350; 1995.
    • (1995) J Biol Chem , vol.270 , pp. 10342-10350
    • Izquierdo, J.M.1    Ricart, J.2    Ostronoff, L.K.3    Egea, G.4    Cuezva, J.M.5
  • 143
    • 0027389311 scopus 로고
    • Translational regulation of mitochondrial differentiation in neonatal rat liver: Specific increase in the translational efficiency of the nuclear-encoded mitochondrial ß-F1-ATPase mRNA
    • AM Luis, JM Izquierdo, LK Ostronoff, M Salinas, JF Santaren, JM Cuezva. Translational regulation of mitochondrial differentiation in neonatal rat liver: Specific increase in the translational efficiency of the nuclear-encoded mitochondrial ß-F1-ATPase mRNA. J Biol Chem 268:1868-1875; 1993.
    • (1993) J Biol Chem , vol.268 , pp. 1868-1875
    • Luis, A.M.1    Izquierdo, J.M.2    Ostronoff, L.K.3    Salinas, M.4    Santaren, J.F.5    Cuezva, J.M.6
  • 144
    • 0030849697 scopus 로고    scopus 로고
    • Control of the translational efficiency of ß-F1-ATPase mRNA depends on the regulation of a protein that binds the 3' untranslated region of the mRNA
    • JM Izquierdo, JM Cuezva. Control of the translational efficiency of ß-F1-ATPase mRNA depends on the regulation of a protein that binds the 3' untranslated region of the mRNA. Mol Cell Biol 17:5255-5268; 1997.
    • (1997) Mol Cell Biol , vol.17 , pp. 5255-5268
    • Izquierdo, J.M.1    Cuezva, J.M.2
  • 146
    • 0033053905 scopus 로고    scopus 로고
    • Mitochondrial function in human skeletal muscle is not impaired by high intensity exercise
    • M Tonkonogi, B Walsh, T Tiivel, V Saks, K Sahlin. Mitochondrial function in human skeletal muscle is not impaired by high intensity exercise. Pflugers Arch 437:562-568; 1999.
    • (1999) Pflugers Arch , vol.437 , pp. 562-568
    • Tonkonogi, M.1    Walsh, B.2    Tiivel, T.3    Saks, V.4    Sahlin, K.5
  • 147
    • 0142132820 scopus 로고    scopus 로고
    • Mitochondrial DNA and maximum oxygen consumption
    • MB Brearley, S Zhou. Mitochondrial DNA and maximum oxygen consumption. Sport Sci 5:1-3; 2001.
    • (2001) Sport Sci , vol.5 , pp. 1-3
    • Brearley, M.B.1    Zhou, S.2
  • 150
    • 0034214103 scopus 로고    scopus 로고
    • Increase of mitochondria and mitochondrial DNA in response to oxidative stress in human cells
    • H-C Lee, P-H Yin, C-Y Lu, Y-H Wei. Increase of mitochondria and mitochondrial DNA in response to oxidative stress in human cells. Biochem J 348:425-432; 2000.
    • (2000) Biochem J , vol.348 , pp. 425-432
    • Lee, H.-C.1    P-H Yin, C.-Y.L.2    Wei, Y.-H.3
  • 151
    • 0037013087 scopus 로고    scopus 로고
    • Skeletal muscle mitochondrial function and exercise capacity in HIV-infected patients with lipodystrophy and elevated p-lactate levels
    • BT Rogea, JAL Calbetb, K Mollera, H Ulluma, HW Hendelc, J Gerstofta, BK Pedersena. Skeletal muscle mitochondrial function and exercise capacity in HIV-infected patients with lipodystrophy and elevated p-lactate levels. AIDS 16:973-982; 2002.
    • (2002) AIDS , vol.16 , pp. 973-982
    • Rogea, B.T.1    Calbetb, J.A.L.2    Mollera, K.3    Ulluma, H.4    Hendelc, H.W.5    Gerstofta, J.6    Pedersena, B.K.7
  • 152
    • 0036089078 scopus 로고    scopus 로고
    • Endurance training induces muscle-specific changes in mitochondrial function in skinned muscle fibers
    • BY Hochachka. Endurance training induces muscle-specific changes in mitochondrial function in skinned muscle fibers. J Appl Physiol 92:2429-2438; 2002.
    • (2002) J Appl Physiol , vol.92 , pp. 2429-2438
    • Hochachka, B.Y.1
  • 153
    • 0025262019 scopus 로고
    • Coupling of mitochondrial metabolism and protein synthesis in heart mitochondria
    • EE McKee, BL Grier, GS Thompson, ACF Leung, JD McCourt. Coupling of mitochondrial metabolism and protein synthesis in heart mitochondria. Am J Physiol 258:E503-E510; 1990.
    • (1990) Am J Physiol , vol.258 , pp. E503-E510
    • McKee, E.E.1    Grier, B.L.2    Thompson, G.S.3    Leung, A.C.F.4    McCourt, J.D.5
  • 155
    • 0028301098 scopus 로고
    • Stoichiometry of mitochondrial transcripts and regulation of gene expression by mitochondrial transcription factor A
    • HL Garstka, M Facke, JR Escribano, RJ Wiesner. Stoichiometry of mitochondrial transcripts and regulation of gene expression by mitochondrial transcription factor A. BBRC200:619-626; 1994.
    • (1994) BBRC , vol.200 , pp. 619-626
    • Garstka, H.L.1    Facke, M.2    Escribano, J.R.3    Wiesner, R.J.4
  • 157
    • 0028223609 scopus 로고
    • Low levels of mitochondrial transcription factor A in mitochondrial depletion
    • N-G Larsson, A Oldfors, E Holme, DA Clayton. Low levels of mitochondrial transcription factor A in mitochondrial depletion. Biochem Biophys Res Commun 200:1374-1378; 1994.
    • (1994) Biochem Biophys Res Commun , vol.200 , pp. 1374-1378
    • Larsson, N.-G.1    Oldfors, A.2    Holme, E.3    Clayton, D.A.4
  • 158
    • 0030809575 scopus 로고    scopus 로고
    • Regulation of mitochondrial transcription by mitochondrial transcription factor A
    • J Montoya, A Perez-Martos, HL Garstka, RJ Wiesner. Regulation of mitochondrial transcription by mitochondrial transcription factor A. Mol Cell Biochem 174:227-230; 1997.
    • (1997) Mol Cell Biochem , vol.174 , pp. 227-230
    • Montoya, J.1    Perez-Martos, A.2    Garstka, H.L.3    Wiesner, R.J.4
  • 159
    • 0025232644 scopus 로고
    • Mitochondrial protein synthesis during thyroxine-induced cardiac hypertrophy
    • ACF Leung, EE McKee. Mitochondrial protein synthesis during thyroxine-induced cardiac hypertrophy. Am J Physiol 258: E511-E518; 1990.
    • (1990) Am J Physiol , vol.258 , pp. E511-E518
    • Leung, A.1    McKee, E.E.2
  • 160
    • 0019302901 scopus 로고
    • The effect of thyroid hormone on mitochondrial biogenesis and cellular hyperplasia
    • WL Wooten, J Cascarano. The effect of thyroid hormone on mitochondrial biogenesis and cellular hyperplasia. J Bioenergetics Biomembranes 12:1-12; 1980.
    • (1980) J Bioenergetics Biomembranes , vol.12 , pp. 1-12
    • Wooten, W.L.1    Cascarano, J.2
  • 161
    • 0023811680 scopus 로고
    • Role of hyperthyroidism in increased thermogenesis in the cold acclimated Syrian hamster
    • SL Sigurdson, J Hims Hagen. Role of hyperthyroidism in increased thermogenesis in the cold acclimated Syrian hamster. Can J Physiol Pharm 66:826-829; 1987.
    • (1987) Can J Physiol Pharm , vol.66 , pp. 826-829
    • Sigurdson, S.L.1    Hims Hagen, J.2
  • 162
    • 0035016557 scopus 로고    scopus 로고
    • T3 increases mitochondrial ATP production in oxidative muscle despite increased expression of UCP2 and 3
    • KR Short, J Nygren, R Barazzoni, J Levine, KS Nair. T3 increases mitochondrial ATP production in oxidative muscle despite increased expression of UCP2 and 3. Am J Physiol Endocrinol Metab 280:E761-E769; 2001.
    • (2001) Am J Physiol Endocrinol Metab , vol.280 , pp. E761-E769
    • Short, K.R.1    Nygren, J.2    Barazzoni, R.3    Levine, J.4    Nair, K.S.5
  • 163
    • 0030028507 scopus 로고    scopus 로고
    • Triiodothyronine induces the transcription of the uncoupling prot-tein genes and stabilizes its mRNA in fetal brown adipocyte primary cultures
    • C Guerra, C Roncero, A Porras, M Fernandez, M Benito. Triiodothyronine induces the transcription of the uncoupling prot-tein genes and stabilizes its mRNA in fetal brown adipocyte primary cultures. J Biol Chem 271:2076-2081; 1996.
    • (1996) J Biol Chem , vol.271 , pp. 2076-2081
    • Guerra, C.1    Roncero, C.2    Porras, A.3    Fernandez, M.4    Benito, M.5
  • 164
    • 0020313059 scopus 로고
    • Role of thyroid hormone in cold induced changes in rat brown adipose tissue mitochondria
    • J Triandafillou, C Gwilliam, J Hims-Hagen. Role of thyroid hormone in cold induced changes in rat brown adipose tissue mitochondria. Can J Biochem 60:530-537; 1982.
    • (1982) Can J Biochem , vol.60 , pp. 530-537
    • Triandafillou, J.1    Gwilliam, C.2    Hims-Hagen, J.3
  • 165
    • 0027260708 scopus 로고
    • Thyroid hormone action on mitochondrial energy transfer
    • S Soboll. Thyroid hormone action on mitochondrial energy transfer. Biochem Biophys Acta 1144:1-16; 1993.
    • (1993) Biochem Biophys Acta , vol.1144 , pp. 1-16
    • Soboll, S.1
  • 166
    • 0023260277 scopus 로고
    • Thyroid hormone action at the cellular level
    • P De Nayer. Thyroid hormone action at the cellular level. Hormone Res 26:48-57; 1987.
    • (1987) Hormone Res , vol.26 , pp. 48-57
    • De Nayer, P.1
  • 167
    • 0024542134 scopus 로고
    • Studies on the mechanism of inhibition of nuclear triiodothyronine binding by fatty acids
    • FRM van der Klis, WM Wiersinger, JJM de Vijlder. Studies on the mechanism of inhibition of nuclear triiodothyronine binding by fatty acids. FEB 246:6-12; 1989.
    • (1989) FEB , vol.246 , pp. 6-12
    • Van Der Klis, F.1    Wiersinger, W.M.2    De Vijlder, J.J.M.3
  • 168
    • 0029085076 scopus 로고
    • Hypothyroidism affects the expression of the B-F1-ATP synthase gene and limits mitochondrial proliferation in rat liver at all stages of development
    • JM Izquierdo, E Jimenez, JM Cuezva. Hypothyroidism affects the expression of the B-F1-ATP synthase gene and limits mitochondrial proliferation in rat liver at all stages of development. Eur J Biochem 232:344-350; 1995.
    • (1995) Eur J Biochem , vol.232 , pp. 344-350
    • Izquierdo, J.M.1    Jimenez, E.2    Cuezva, J.M.3
  • 169
    • 0013591263 scopus 로고
    • Thyroid hormone binding by a component of mitochondrial membrane
    • K Sterling, PO Milch. Thyroid hormone binding by a component of mitochondrial membrane. Proc Nat Acad Sci USA72:3225-3229; 1975.
    • (1975) Proc Nat Acad Sci USA , vol.72 , pp. 3225-3229
    • Sterling, K.1    Milch, P.O.2
  • 172
    • 0029736922 scopus 로고    scopus 로고
    • Changes in mitochondrial activity during avian myoblast differentiation: Influence of triiodothyronine or v-erb A expression
    • P Rochard, I Cassar-Malek, S Marchal, C Wrutniakk, G Cabello. Changes in mitochondrial activity during avian myoblast differentiation: Influence of triiodothyronine or v-erb A expression. J Cell Physiol 168:239-247; 1996.
    • (1996) J Cell Physiol , vol.168 , pp. 239-247
    • Rochard, P.1    Cassar-Malek, I.2    Marchal, S.3    Wrutniakk, C.4    Cabello, G.5
  • 174
    • 0030894299 scopus 로고    scopus 로고
    • Thyroid hormone and gene expression in the regulation of mitochondrial respiratory function
    • TM Pillar, HJ Seitz. Thyroid hormone and gene expression in the regulation of mitochondrial respiratory function. Eur J Endocrinol 136:231-239; 1997.
    • (1997) Eur J Endocrinol , vol.136 , pp. 231-239
    • Pillar, T.M.1    Seitz, H.J.2
  • 175
    • 0028896912 scopus 로고
    • Modulation of thyroid hormone action by mutant thyroid hormone receptors, c-erb Aa2 and peroxisome proliferator-activated receptor: Evidence for different mechanisms of inhibition
    • SC Meier-Heusler, X Zhu, C Juge-Aubry, A Pernin, AG Burger, S-Y Cheng, CA Meier. Modulation of thyroid hormone action by mutant thyroid hormone receptors, c-erb Aa2 and peroxisome proliferator-activated receptor: Evidence for different mechanisms of inhibition. Mol Cell Endocrinol 107:55-66; 1995.
    • (1995) Mol Cell Endocrinol , vol.107 , pp. 55-66
    • Meier-Heusler, S.C.1    Zhu, X.2    Juge-Aubry, C.3    Pernin, A.4    Burger, A.G.5    Cheng, S.-Y.6    Meier, C.A.7
  • 176
    • 0035066653 scopus 로고    scopus 로고
    • Actions and interactions of thyroid hormone and zinc status in growing rats
    • HC Freake, KE Govoni, K Guda, C Huang, SA Zinn. Actions and interactions of thyroid hormone and zinc status in growing rats. J Nutr 131:1135-1141; 2001.
    • (2001) J Nutr , vol.131 , pp. 1135-1141
    • Freake, H.C.1    Govoni, K.E.2    Guda, K.3    Huang, C.4    Zinn, S.A.5
  • 178
    • 0028083131 scopus 로고
    • Mitochondrial biogenesis and development of respiratory chain enzymes in kidney cells: Role of glucocorticoids
    • F Djoudi, J Bastin, T Gilbert, A Rotig, P Rustin, C Merlet-Ben-ichou. Mitochondrial biogenesis and development of respiratory chain enzymes in kidney cells: Role of glucocorticoids. Am J Physiol 267:C245-C254; 1994.
    • (1994) Am J Physiol , vol.267 , pp. C245-C254
    • Djoudi, F.1    Bastin, J.2    Gilbert, T.3    Rotig, A.4    Rustin, P.5    Merlet-Ben-Ichou, C.6
  • 179
    • 0027504734 scopus 로고
    • Mitochondrial-genome-encoded RNAs: Differential regulation by corticotropin in bovine adrenocortical cells
    • M Raikhinstein, I Hanukoglu. Mitochondrial-genome-encoded RNAs: Differential regulation by corticotropin in bovine adrenocortical cells. Proc Nat Acad Sci USA 90:10509-10513; 1993.
    • (1993) Proc Nat Acad Sci USA , vol.90 , pp. 10509-10513
    • Raikhinstein, M.1    Hanukoglu, I.2
  • 181
    • 0034064334 scopus 로고    scopus 로고
    • Beta cell mitochondria in the regulation of insulin secretion: A new culprit in type II diabetes
    • CB Wolheim. Beta cell mitochondria in the regulation of insulin secretion: A new culprit in type II diabetes. Diabetologia43:265-277; 2000.
    • (2000) Diabetologia , vol.43 , pp. 265-277
    • Wolheim, C.B.1
  • 183
    • 0035856942 scopus 로고    scopus 로고
    • Mitochondrial function in normal and diabetic beta cells
    • P Maechler, CB Wolheim. Mitochondrial function in normal and diabetic beta cells. Nature 414:807-812; 2001.
    • (2001) Nature , vol.414 , pp. 807-812
    • Maechler, P.1    Wolheim, C.B.2
  • 185
    • 0023483399 scopus 로고
    • A human retinoic acid receptor which belongs to the family of nuclear receptors
    • M Petkovich, NJ Brand, A Krust, P Chambon. A human retinoic acid receptor which belongs to the family of nuclear receptors. Nature 220:444-450; 1987.
    • (1987) Nature , vol.220 , pp. 444-450
    • Petkovich, M.1    Brand, N.J.2    Krust, A.3    Chambon, P.4
  • 186
    • 0025270737 scopus 로고
    • Nuclear receptor that identifies a novel retinoic acid response pathway
    • DJ Mangelsdorf, ES Ong, JA Dyke, RM Evans. Nuclear receptor that identifies a novel retinoic acid response pathway. Nature 345:224-229; 1990.
    • (1990) Nature , vol.345 , pp. 224-229
    • Mangelsdorf, D.J.1    Ong, E.S.2    Dyke, J.A.3    Evans, R.M.4
  • 189
    • 0025721940 scopus 로고
    • Mouse retinoic acid receptor y2 isoform is transcribed from a promoter that contains a retinoic acid response element
    • P LeRoy, H Nakshatri, P Chambon. Mouse retinoic acid receptor y2 isoform is transcribed from a promoter that contains a retinoic acid response element. Proc Natl Acad Sci USA, 88:10138-10142; 1991.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10138-10142
    • Leroy, P.1    Nakshatri, H.2    Chambon, P.3
  • 190
    • 0025354926 scopus 로고
    • Identification of a novel isoform of the retinoic acid receptor y expressed in the mouse embryo
    • V Giguere, M Shago, R Zirngibl, P Tate, J Rossant, S Varmuza. Identification of a novel isoform of the retinoic acid receptor y expressed in the mouse embryo. Mol Cell Biol 10:2335-2340; 1990.
    • (1990) Mol Cell Biol , vol.10 , pp. 2335-2340
    • Giguere, V.1    Shago, M.2    Zirngibl, R.3    Tate, P.4    Rossant, J.5    Varmuza, S.6
  • 191
    • 0026065677 scopus 로고
    • Genomic organization of the retinoic acid receptor gamma gene
    • JM Lehmann, B Hoffman, M Pfahl. Genomic organization of the retinoic acid receptor gamma gene. Nucl Acids Res 19: 573-578; 1991.
    • (1991) Nucl Acids Res , vol.19 , pp. 573-578
    • Lehmann, J.M.1    Hoffman, B.2    Pfahl, M.3
  • 192
    • 0028419153 scopus 로고
    • The retinoid signaling pathway: Molecular and genetic analyses
    • P Chambon. The retinoid signaling pathway: Molecular and genetic analyses. Cell Biol 5:115-125; 1994.
    • (1994) Cell Biol , vol.5 , pp. 115-125
    • Chambon, P.1
  • 193
    • 0030585311 scopus 로고    scopus 로고
    • Retinoic acid differentially up-regulates the gene expression of retinoic acid receptor a and p isoforms in embryo and adult rats
    • K Takeyama, R Kojima, T Ohashi, T Sato, H Mano, S Masushige, S Kato. Retinoic acid differentially up-regulates the gene expression of retinoic acid receptor a and p isoforms in embryo and adult rats. Biochem Biophys Res Commun222:395-400; 1996.
    • (1996) Biochem Biophys Res Commun , vol.222 , pp. 395-400
    • Takeyama, K.1    Kojima, R.2    Ohashi, T.3    Sato, T.4    Mano, H.5    Masushige, S.6    Kato, S.7
  • 194
    • 0025776140 scopus 로고
    • Retinoic acid affects the expression of nuclear retinoic acid receptors in tissues of retinol-deficient rats
    • R-U Haq, M Pfahl, F Chytil. Retinoic acid affects the expression of nuclear retinoic acid receptors in tissues of retinol-deficient rats. Proc Natl Acad Sci USA 88:8272-8276; 1991.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8272-8276
    • Haq, R.-U.1    Pfahl, M.2    Chytil, F.3
  • 196
    • 0028168007 scopus 로고
    • Genetic analysis of RXR developmental function: Convergence of RXR and RAR signaling pathways in heart and eye morphogenesis
    • P Kastner, JM Grondona, M Mark, A Gansmuller, M LeMeur, D Decimo, J-L Vonesch, P Dolle, P Chambon. Genetic analysis of RXR developmental function: Convergence of RXR and RAR signaling pathways in heart and eye morphogenesis. Cell78:987-1003; 1994.
    • (1994) Cell , vol.78 , pp. 987-1003
    • Kastner, P.1    Grondona, J.M.2    Mark, M.3    Gansmuller, A.4    Lemeur, M.5    Decimo, D.6    Vonesch, J.-L.7    Dolle, P.8    Chambon, P.9
  • 200
    • 0029584593 scopus 로고
    • Nonsteroid nuclear receptors: What are genetic studies telling us about their role in real life?
    • P Kastner, M Mark, P Chambon. Nonsteroid nuclear receptors: What are genetic studies telling us about their role in real life?Cell 83:859-869; 1995.
    • (1995) Cell , vol.83 , pp. 859-869
    • Kastner, P.1    Mark, M.2    Chambon, P.3
  • 201
    • 0036592019 scopus 로고    scopus 로고
    • Nutrient-gene interactions: Dietary vitamin A and mitochondrial gene expression
    • HB Everts, DO Claassen, CL Hermoyian, CD Berdanier. Nutrient-gene interactions: Dietary vitamin A and mitochondrial gene expression. IUBMB Life 53:295-301; 2002.
    • (2002) IUBMB Life , vol.53 , pp. 295-301
    • Everts, H.B.1    Claassen, D.O.2    Hermoyian, C.L.3    Berdanier, C.D.4
  • 202
    • 0034731398 scopus 로고    scopus 로고
    • Cellular retinoic acid binding protein is associated with mitochondria
    • SJ Ruff, DE Ong. Cellular retinoic acid binding protein is associated with mitochondria. FEBS Letters 487:282-286; 2000.
    • (2000) FEBS Letters , vol.487 , pp. 282-286
    • Ruff, S.J.1    Ong, D.E.2
  • 203
    • 0028132832 scopus 로고
    • Expression of a retinoic acid-inducible mitochondrial ND5 gene is regulated by cell density in bovine papillomavirus DNA-transformed mouse C127 cells but not in revertant cells
    • G Li, Y Liu, SS Tsang. Expression of a retinoic acid-inducible mitochondrial ND5 gene is regulated by cell density in bovine papillomavirus DNA-transformed mouse C127 cells but not in revertant cells. Int J Oncol 5:301-307; 1994.
    • (1994) Int J Oncol , vol.5 , pp. 301-307
    • Li, G.1    Liu, Y.2    Tsang, S.S.3
  • 204
    • 0031965927 scopus 로고    scopus 로고
    • Isolation and characterization of all-trans-retinoic acid-responsive genes in the rat testis
    • IC Gaemers, AMM Van Pelt, APN, Themmen, DG De Rooij. Isolation and characterization of all-trans-retinoic acid-responsive genes in the rat testis. Mol Reprod Dev 50:1-6; 1998.
    • (1998) Mol Reprod Dev , vol.50 , pp. 1-6
    • Gaemers, I.C.1    Van Pelt, A.M.M.2    Themmen, A.P.N.3    De Rooij, D.G.4
  • 207
    • 0028851540 scopus 로고
    • Tissue specific regulation by vitamin D status of nuclear and mitochondrial gene expression in kidney and intestine
    • SY Chou, SS Hannah, KE Lowe, AW Norman, HL Henry. Tissue specific regulation by vitamin D status of nuclear and mitochondrial gene expression in kidney and intestine. Endocrinology 136:5520-5526; 1995.
    • (1995) Endocrinology , vol.136 , pp. 5520-5526
    • Chou, S.Y.1    Hannah, S.S.2    Lowe, K.E.3    Norman, A.W.4    Henry, H.L.5
  • 208
    • 0031666638 scopus 로고    scopus 로고
    • Alteration of mitochondrial DNA and RNA levels in human fibroblasts with impaired vitamin B12 coenzyme synthesis
    • P Cantatore, V Petruzzella, C Nicoletti, F Papadia, F Fracasso, P Rustin, MN Gadaleta. Alteration of mitochondrial DNA and RNA levels in human fibroblasts with impaired vitamin B12 coenzyme synthesis. FEBS Lett 432:173-178; 1998.
    • (1998) FEBS Lett , vol.432 , pp. 173-178
    • Cantatore, P.1    Petruzzella, V.2    Nicoletti, C.3    Papadia, F.4    Fracasso, F.5    Rustin, P.6    Gadaleta, M.N.7
  • 209
    • 0342954789 scopus 로고    scopus 로고
    • Iron II induces changes in the conformation of mammalian mitochondrial DNA resulting in a reduction of its transcriptional rate
    • J Asin, A Perez-Martos, P Silva-Fernandez-Silva, J Montoya, AL Andreu. Iron II induces changes in the conformation of mammalian mitochondrial DNA resulting in a reduction of its transcriptional rate. FEBS Lett 480:161-164; 2000.
    • (2000) FEBS Lett , vol.480 , pp. 161-164
    • Asin, J.1    Perez-Martos, A.2    Silva-Fernandez-Silva, P.3    Montoya, J.4    Andreu, A.L.5
  • 210
    • 0028893889 scopus 로고
    • Oxidative damage to lipids and DNA concurrent with decrease of antioxidants in rat testes after acute iron intoxication
    • F Lucesoli, CG Fraga. Oxidative damage to lipids and DNA concurrent with decrease of antioxidants in rat testes after acute iron intoxication. Arch Biochem Biophys 316:567-571; 1995.
    • (1995) Arch Biochem Biophys , vol.316 , pp. 567-571
    • Lucesoli, F.1    Fraga, C.G.2
  • 211
    • 0027502430 scopus 로고
    • Sources and role of iron in lipid peroxidation
    • G Minotti. Sources and role of iron in lipid peroxidation. Chem Res Toxicol 6:134-146; 1992.
    • (1992) Chem Res Toxicol , vol.6 , pp. 134-146
    • Minotti, G.1
  • 212
    • 0025183784 scopus 로고
    • Two types of receptors for iron in mitochondria
    • J Weaver, S Pollack. Two types of receptors for iron in mitochondria. Biochem J 271:463-466; 1990.
    • (1990) Biochem J , vol.271 , pp. 463-466
    • Weaver, J.1    Pollack, S.2
  • 213
    • 0024817944 scopus 로고
    • Impaired control of respiration in iron deficient muscle mitochondria
    • WT Willis, PR Dallman. Impaired control of respiration in iron deficient muscle mitochondria. Am J Physiol257:C1080-C1085; 1989.
    • (1989) Am J Physiol , vol.257 , pp. C1080-C1085
    • Willis, W.T.1    Dallman, P.R.2
  • 215
    • 0032549811 scopus 로고    scopus 로고
    • A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis
    • P Puigserver, Z Wu, CW Park, R Graves, M Wright, BM Spiegelman. A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis. Cell 92:829-839; 1998.
    • (1998) Cell , vol.92 , pp. 829-839
    • Puigserver, Z.W.1    Park, C.W.2    Graves, R.3    Wright, M.4    Spiegelman, B.M.5
  • 216
    • 0027369217 scopus 로고
    • Evidence of post-transcriptional regulation in mammalian mitochondrial biogenesis
    • JM Izquierdo, JM Cueza. Evidence of post-transcriptional regulation in mammalian mitochondrial biogenesis. Biochem Biophys Res Commun 196:55-60; 1993.
    • (1993) Biochem Biophys Res Commun , vol.196 , pp. 55-60
    • Izquierdo, J.M.1    Cueza, J.M.2
  • 217
    • 0026725099 scopus 로고
    • Differential regulation of the transcript levels of some nuclear-encoded and mitochondrial-encoded respiratory-chain components in response to growth activation
    • K Luciakova, R Li, BD Nelson. Differential regulation of the transcript levels of some nuclear-encoded and mitochondrial-encoded respiratory-chain components in response to growth activation. Eur J Biochem 207:253-257; 1992.
    • (1992) Eur J Biochem , vol.207 , pp. 253-257
    • Luciakova, K.1    Li, R.2    Nelson, B.D.3
  • 218
    • 0028969786 scopus 로고
    • Effect of hypothyroidism on the expression of cytochrome c and cytochrome c oxidase in heart and muscle during development
    • RJ Stevens, ML Nishio, DA Hood. Effect of hypothyroidism on the expression of cytochrome c and cytochrome c oxidase in heart and muscle during development. Mol Cell Biochem143:119-127; 1995.
    • (1995) Mol Cell Biochem , vol.143 , pp. 119-127
    • Stevens, R.J.1    Nishio, M.L.2    Hood, D.A.3
  • 219
    • 0029060046 scopus 로고
    • The role of thyroid hormone and promoter diversity in the regulation of nuclear encoded mitochondrial proteins
    • BD Nelson, K Luciakova, R Li, S Betina. The role of thyroid hormone and promoter diversity in the regulation of nuclear encoded mitochondrial proteins. Biochim Biophys Acta1271:85-91; 1995.
    • (1995) Biochim Biophys Acta , vol.1271 , pp. 85-91
    • Nelson, B.D.1    Luciakova, K.2    Li, R.3    Betina, S.4
  • 220
    • 0026769571 scopus 로고
    • Transcript levels for nuclear-encoded mammalian mitochondrial respiratory chain components are regulated by thyroid hormone in an uncoordinated fashion
    • K Luciakova, BD Nelson. Transcript levels for nuclear-encoded mammalian mitochondrial respiratory chain components are regulated by thyroid hormone in an uncoordinated fashion. Eur J Biochem 207:247-251; 1992.
    • (1992) Eur J Biochem , vol.207 , pp. 247-251
    • Luciakova, K.1    Nelson, B.D.2
  • 221
    • 0029085076 scopus 로고
    • Hypothyroidism affects the expression of the ß-F1-ATP synthase gene and limits mitochondrial proliferation in rat liver at all stages of development
    • JM Izquierdo, E Jimenez, JM Cuezva. Hypothyroidism affects the expression of the ß-F1-ATP synthase gene and limits mitochondrial proliferation in rat liver at all stages of development. Eur J Biochem 232:344-350; 1995.
    • (1995) Eur J Biochem , vol.232 , pp. 344-350
    • Izquierdo, J.M.1    Jimenez, E.2    Cuezva, J.M.3
  • 222
    • 0345493790 scopus 로고    scopus 로고
    • Autonomous regulation in mammalian mitochondrial DNA transcriptions
    • JA Enriquez, P Fernadez-Silva, J Montoya. Autonomous regulation in mammalian mitochondrial DNA transcriptions. J Biol Chem 380:737-747; 1999.
    • (1999) J Biol Chem , vol.380 , pp. 737-747
    • Enriquez, J.A.1    Fernadez-Silva, P.2    Montoya, J.3
  • 223
    • 0030048586 scopus 로고    scopus 로고
    • Thyromi-metic action of the peroxisome proliferators Clofibrate, perflu-orooctanoic acid and acetylsalicyclic acid includes changes in mRNA levels for certain genes involved in mitochondrial biogenesis
    • Y Cai, BD Nelson, R Li, K Luciakova, JW DePierre. Thyromi-metic action of the peroxisome proliferators Clofibrate, perflu-orooctanoic acid and acetylsalicyclic acid includes changes in mRNA levels for certain genes involved in mitochondrial biogenesis. Arch Biochem Biophys 325:107-112; 1996.
    • (1996) Arch Biochem Biophys , vol.325 , pp. 107-112
    • Cai, Y.1    Nelson, B.D.2    Li, R.3    Luciakova, K.4    Depierre, J.W.5
  • 224
    • 0022776787 scopus 로고
    • Precise assignment of the light-strand promoter of mouse mitochondrial DNA: A functional promoter consists of multiple upstream domains
    • DD Chang, DA Clayton. Precise assignment of the light-strand promoter of mouse mitochondrial DNA: A functional promoter consists of multiple upstream domains. Mol Cell Biol6:3253-3261; 1986.
    • (1986) Mol Cell Biol , vol.6 , pp. 3253-3261
    • Chang, D.D.1    Clayton, D.A.2
  • 225
    • 0023029785 scopus 로고
    • Precise assignment of the heavy-strand promoter of mouse mitochondrial DNA: Cognate start sites are not required for transcriptional initiation
    • DD Chang, DA Clayton. Precise assignment of the heavy-strand promoter of mouse mitochondrial DNA: Cognate start sites are not required for transcriptional initiation. Mol Cell Biol 6:3262-3267; 1986.
    • (1986) Mol Cell Biol , vol.6 , pp. 3262-3267
    • Chang, D.D.1    Clayton, D.A.2
  • 226
    • 0021165948 scopus 로고
    • Identification of a promoter for transcription of the heavy strand mtDNA: In vitro transcription and deletion mutagenesis
    • DF Bogenhagen, EF Applegate, BK Yoza. Identification of a promoter for transcription of the heavy strand mtDNA: In vitro transcription and deletion mutagenesis. Cell 36:1105-1113; 1984.
    • (1984) Cell , vol.36 , pp. 1105-1113
    • Bogenhagen, D.F.1    Applegate, E.F.2    Yoza, B.K.3
  • 227
    • 0021112314 scopus 로고
    • DNA sequence of the Xenopus Laevis mitochondrial heavy and light strand replication origins and flanking tRNA genes
    • JFH Wong, DP Ma, RK Wilson, BA Roe. DNA sequence of the Xenopus Laevis mitochondrial heavy and light strand replication origins and flanking tRNA genes. Nucleic Acids Res11:4977-4995; 1983.
    • (1983) Nucleic Acids Res , vol.11 , pp. 4977-4995
    • Wong, J.1    Ma, D.P.2    Wilson, R.K.3    Roe, B.A.4
  • 228
    • 0025812291 scopus 로고
    • Direct repeats as selective response elements for the thyroid hormone, retinoic acid, and vitamin D3 receptors
    • K Umesono, KK Murakami, CC Thompson, RM Evans. Direct repeats as selective response elements for the thyroid hormone, retinoic acid, and vitamin D3 receptors. Cell 65:1255-1266; 1991.
    • (1991) Cell , vol.65 , pp. 1255-1266
    • Umesono, K.1    Murakami, K.K.2    Thompson, C.C.3    Evans, R.M.4
  • 229
    • 0025860708 scopus 로고
    • The orientation and spacing of core DNA-binding motifs dictate selective transcriptional responses to three nuclear receptors
    • AM Naar, JM Boutin, SM Lipkin, VC Yu, JM Holloway, CK Glass, MG Rosenfeld. The orientation and spacing of core DNA-binding motifs dictate selective transcriptional responses to three nuclear receptors. Cell 65:1267-1279; 1991.
    • (1991) Cell , vol.65 , pp. 1267-1279
    • Naar, A.M.1    Boutin, J.M.2    Sm Lipkin, V.Y.3    Holloway, J.M.4    Glass, C.K.5    Rosenfeld, M.G.6
  • 232
    • 0033614441 scopus 로고    scopus 로고
    • Oxidative stress and upregulation of mitochondria;l biogenesis genes in mitochondrial DNA depleted HeLa cells
    • S Miranda, R Foncea, J Guerrero, F Leighton. Oxidative stress and upregulation of mitochondria;l biogenesis genes in mitochondrial DNA depleted HeLa cells. Biochem Biophys Res Commun 258:44-49; 1999.
    • (1999) Biochem Biophys Res Commun , vol.258 , pp. 44-49
    • Miranda, S.1    Foncea, R.2    Guerrero, J.3    Leighton, F.4
  • 233
    • 0028301098 scopus 로고
    • Stoichiometry of mitochondrial transcripts and regulation of gene expression by mitochonrial transcription factor A
    • HL Garstka, M Facke, JR Escribano, RJ Wiesner. Stoichiometry of mitochondrial transcripts and regulation of gene expression by mitochonrial transcription factor A. Biochem Biophys Res Commun 200:619-626; 1994.
    • (1994) Biochem Biophys Res Commun , vol.200 , pp. 619-626
    • Garstka, H.L.1    Facke, M.2    Escribano, J.R.3    Wiesner, R.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.