메뉴 건너뛰기




Volumn 1604, Issue 2, 2003, Pages 77-94

Intrinsic and extrinsic uncoupling of oxidative phosphorylation

Author keywords

ATP synthase; Cytochrome c oxidase; Membrane potential; Protein phosphorylation; Proton pumping; ROS production; Thyroid hormone; Uncoupling of oxidative phosphorylation

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; CYCLIC AMP; CYTOCHROME C OXIDASE; FATTY ACID; ISOENZYME; MEMBRANE PROTEIN; PALMITIC ACID; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; REACTIVE OXYGEN METABOLITE; THYROID HORMONE; UNCOUPLING PROTEIN 1; UNCOUPLING PROTEIN 2;

EID: 0037726805     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2728(03)00027-6     Document Type: Review
Times cited : (416)

References (209)
  • 1
    • 0028114231 scopus 로고
    • Structure at 2.8 Å resolution of F-ATPase from bovine heart mitochondria
    • Abrahams J.P., Leslie A.G.W., Lutter R., Walker J.E. Structure at 2.8 Å resolution of F-ATPase from bovine heart mitochondria. Nature. 370:1994;621-628.
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.W.2    Lutter, R.3    Walker, J.E.4
  • 3
    • 0030898875 scopus 로고    scopus 로고
    • 0-ATP synthases: Glimpses of interacting parts in a dynamic molecular machine
    • 0-ATP synthases: glimpses of interacting parts in a dynamic molecular machine. J. Exp. Biol. 200:1997;217-224.
    • (1997) J. Exp. Biol. , vol.200 , pp. 217-224
    • Fillingame, R.H.1
  • 4
    • 0030715561 scopus 로고    scopus 로고
    • ATP synthase: An electrochemical transducer with rotatory mechanics
    • Junge W., Lill H., Engelbrecht S. ATP synthase: an electrochemical transducer with rotatory mechanics. Trends Biochem. Sci. 22:1997;420-423.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 420-423
    • Junge, W.1    Lill, H.2    Engelbrecht, S.3
  • 5
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock D., Leslie A.G.W., Walker J.E. Molecular architecture of the rotary motor in ATP synthase. Science. 286:1999;1700-1705.
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.W.2    Walker, J.E.3
  • 6
    • 0034738113 scopus 로고    scopus 로고
    • 0 motor of the ATP synthase
    • 0 motor of the ATP synthase. Biochim. Biophys. Acta. 1458:2000;374-386.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 374-386
    • Dimroth, P.1
  • 7
    • 0010049951 scopus 로고    scopus 로고
    • Structure of fumarate reductase from Wolinella siccinogenes at 2.2 Å resolution
    • Lancaster C.R., Kröger A., Auer M., Michel H. Structure of fumarate reductase from Wolinella siccinogenes at 2.2 Å resolution. Nature. 402:1999;377-385.
    • (1999) Nature , vol.402 , pp. 377-385
    • Lancaster, C.R.1    Kröger, A.2    Auer, M.3    Michel, H.4
  • 8
    • 0033580880 scopus 로고    scopus 로고
    • Structure of the Escherichia coli fumarate reductase respiratory complex
    • Iverson T.M., Luna-Chavez C., Cecchini G., Rees D.C. Structure of the Escherichia coli fumarate reductase respiratory complex. Science. 284:1999;1941-1942.
    • (1999) Science , vol.284 , pp. 1941-1942
    • Iverson, T.M.1    Luna-Chavez, C.2    Cecchini, G.3    Rees, D.C.4
  • 9
    • 0034660152 scopus 로고    scopus 로고
    • Structure at 2.3 Å resolution of the cytochrome bc(1) complex from the yeast Saccharose cerevisiae co-crystallized with an antibody Fv fragment
    • Hunte C., Koepke J., Lange C., Rossmanith T., Michel H. Structure at 2.3 Å resolution of the cytochrome bc(1) complex from the yeast Saccharose cerevisiae co-crystallized with an antibody Fv fragment. Structure Fold. Des. 8:2000;669-684.
    • (2000) Structure Fold. Des. , vol.8 , pp. 669-684
    • Hunte, C.1    Koepke, J.2    Lange, C.3    Rossmanith, T.4    Michel, H.5
  • 10
    • 0037022594 scopus 로고    scopus 로고
    • Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c
    • Lange C., Hunte C. Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c. Proc. Natl. Acad. Sci. U. S. A. 99:2002;2800-2805.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 2800-2805
    • Lange, C.1    Hunte, C.2
  • 14
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S., Ostermeier C., Ludwig B., Michel H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature. 376:1995;660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 15
    • 0030886203 scopus 로고    scopus 로고
    • Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment
    • Ostermeier C., Harrenga A., Ermler U., Michel H. Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment. Proc. Natl. Acad. Sci. U. S. A. 94:1997;10547-10553.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 10547-10553
    • Ostermeier, C.1    Harrenga, A.2    Ermler, U.3    Michel, H.4
  • 19
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemiosmotic type of mechanism
    • Mitchell P. Coupling of phosphorylation to electron and hydrogen transfer by a chemiosmotic type of mechanism. Nature. 191:1961;144-148.
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P.1
  • 20
    • 0013942130 scopus 로고
    • Chemiosmotic coupling in oxidative and photosynthetic phosphorylation
    • Mitchell P. Chemiosmotic coupling in oxidative and photosynthetic phosphorylation. Biol. Rev. 41:1966;445-502.
    • (1966) Biol. Rev. , vol.41 , pp. 445-502
    • Mitchell, P.1
  • 22
    • 0025876396 scopus 로고
    • Mechanistic stoichiometry of mitochondrial oxidative phosphorylation
    • Hinkle P.C., Kumar M.A., Resetar A., Harris D.L. Mechanistic stoichiometry of mitochondrial oxidative phosphorylation. Biochemistry. 30:1991;3576-3582.
    • (1991) Biochemistry , vol.30 , pp. 3576-3582
    • Hinkle, P.C.1    Kumar, M.A.2    Resetar, A.3    Harris, D.L.4
  • 23
    • 0026624980 scopus 로고
    • Diseases of the mitochondrial DNA
    • Wallace D.C. Diseases of the mitochondrial DNA. Annu. Rev. Biochem. 61:1992;1175-1212.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 1175-1212
    • Wallace, D.C.1
  • 24
    • 0024541837 scopus 로고
    • Mitochondrial DNA mutations as an important contributor to ageing and degenerative diseases
    • Linnane A.W., Marzuki T., Ozawa T., Tanaka M. Mitochondrial DNA mutations as an important contributor to ageing and degenerative diseases. Lancet. 1:1989;642-645.
    • (1989) Lancet , vol.1 , pp. 642-645
    • Linnane, A.W.1    Marzuki, T.2    Ozawa, T.3    Tanaka, M.4
  • 25
    • 0026587335 scopus 로고
    • Mitochondrial genetics: A paradigm for aging and degenerative diseases?
    • Wallace D.C. Mitochondrial genetics: a paradigm for aging and degenerative diseases? Science. 256:1992;628-632.
    • (1992) Science , vol.256 , pp. 628-632
    • Wallace, D.C.1
  • 27
    • 0019142414 scopus 로고
    • Uncouplers of oxidative phosphorylation
    • Heytler P.G. Uncouplers of oxidative phosphorylation. Pharmacol. Ther. 10:1980;461-472.
    • (1980) Pharmacol. Ther. , vol.10 , pp. 461-472
    • Heytler, P.G.1
  • 28
    • 0025046339 scopus 로고
    • Uncouplers of oxidative phosphorylation
    • Terada H. Uncouplers of oxidative phosphorylation. Environ. Health Perspect. 87:1990;213-218.
    • (1990) Environ. Health Perspect. , vol.87 , pp. 213-218
    • Terada, H.1
  • 29
    • 0027374015 scopus 로고
    • A threshold membrane potential accounts for controversial effects of fatty acids on mitochondrial oxidative phosphorylation
    • Köhnke D., Ludwig B., Kadenbach B. A threshold membrane potential accounts for controversial effects of fatty acids on mitochondrial oxidative phosphorylation. FEBS Lett. 336:1993;90-94.
    • (1993) FEBS Lett. , vol.336 , pp. 90-94
    • Köhnke, D.1    Ludwig, B.2    Kadenbach, B.3
  • 30
    • 0030995005 scopus 로고    scopus 로고
    • The physiological significance of mitochondrial proton leak in animal cells and tissues
    • Rolfe D.F.S., Brand M.D. The physiological significance of mitochondrial proton leak in animal cells and tissues. Biosci. Rep. 17:1997;9-16.
    • (1997) Biosci. Rep. , vol.17 , pp. 9-16
    • Rolfe, D.F.S.1    Brand, M.D.2
  • 31
    • 0021322138 scopus 로고
    • Thermogenic mechanisms in brown fat
    • Nicholls D.G., Locke R.M. Thermogenic mechanisms in brown fat. Physiol. Rev. 64:1984;1-64.
    • (1984) Physiol. Rev. , vol.64 , pp. 1-64
    • Nicholls, D.G.1    Locke, R.M.2
  • 32
    • 0021981298 scopus 로고
    • The biochemistry of an inefficient tissue: Brown adipose tissue
    • Cannon B., Nedergaard J. The biochemistry of an inefficient tissue: brown adipose tissue. Essays Biochem. 20:1985;110-164.
    • (1985) Essays Biochem. , vol.20 , pp. 110-164
    • Cannon, B.1    Nedergaard, J.2
  • 33
    • 0025062409 scopus 로고
    • Mechanism and evolution of the uncoupling protein of brown adipose tissue
    • Klingenberg M. Mechanism and evolution of the uncoupling protein of brown adipose tissue. Trends Biochem. Sci. 15:1990;108-112.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 108-112
    • Klingenberg, M.1
  • 35
    • 0032827410 scopus 로고    scopus 로고
    • Mitochondrial transport of cations: Channels, exchangers, and permeability transition
    • Bernardi P. Mitochondrial transport of cations: channels, exchangers, and permeability transition. Physiol. Rev. 79:1999;1127-1155.
    • (1999) Physiol. Rev. , vol.79 , pp. 1127-1155
    • Bernardi, P.1
  • 36
    • 0035477049 scopus 로고    scopus 로고
    • Chimers of two fused ADP/ATP carrier monomers indicate a single channel for ADP/ATP transport
    • Huang S.G., Odoy S., Klingenberg M. Chimers of two fused ADP/ATP carrier monomers indicate a single channel for ADP/ATP transport. Arch. Biochem. Biophys. 394:2001;67-75.
    • (2001) Arch. Biochem. Biophys. , vol.394 , pp. 67-75
    • Huang, S.G.1    Odoy, S.2    Klingenberg, M.3
  • 37
    • 0032575612 scopus 로고    scopus 로고
    • Expression in Escherichia coli, functional characterization, and tissue distribution of isoforms A and B of the phosphate carrier from bovine mitochondria
    • Fiermonte G., Dolce V., Palmieri F. Expression in Escherichia coli, functional characterization, and tissue distribution of isoforms A and B of the phosphate carrier from bovine mitochondria. J. Biol. Chem. 273:1998;22782-22787.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22782-22787
    • Fiermonte, G.1    Dolce, V.2    Palmieri, F.3
  • 40
    • 0025801060 scopus 로고
    • Evolution of energy metabolism. Proton permeability of the inner membrane of liver mitochondria is greater in a mammal than in a reptile
    • Brand M.D., Couture P., Else P.L., Withers K.W., Hulbert A.J. Evolution of energy metabolism. Proton permeability of the inner membrane of liver mitochondria is greater in a mammal than in a reptile. Biochem. J. 275:1991;81-86.
    • (1991) Biochem. J. , vol.275 , pp. 81-86
    • Brand, M.D.1    Couture, P.2    Else, P.L.3    Withers, K.W.4    Hulbert, A.J.5
  • 41
    • 0007160570 scopus 로고
    • Degree of coupling and its relation to efficiency of energy conversion
    • Kedem O., Kaplan S.R. Degree of coupling and its relation to efficiency of energy conversion. Trans. Faraday Soc. 61:1965;1897-1911.
    • (1965) Trans. Faraday Soc. , vol.61 , pp. 1897-1911
    • Kedem, O.1    Kaplan, S.R.2
  • 42
    • 0019048027 scopus 로고
    • The optimal efficiency and the economic degrees of coupling of oxidative phosphorylation
    • Stucki J.W. The optimal efficiency and the economic degrees of coupling of oxidative phosphorylation. Eur. J. Biochem. 109:1980;269-283.
    • (1980) Eur. J. Biochem. , vol.109 , pp. 269-283
    • Stucki, J.W.1
  • 43
    • 0016294206 scopus 로고
    • The influence of respiration and ATP hydrolysis on the proton-electrochemical gradient across the inner membrane of rat-liver mitochondria as determined by ion distribution
    • Nicholls D.G. The influence of respiration and ATP hydrolysis on the proton-electrochemical gradient across the inner membrane of rat-liver mitochondria as determined by ion distribution. Eur. J. Biochem. 50:1974;305-315.
    • (1974) Eur. J. Biochem. , vol.50 , pp. 305-315
    • Nicholls, D.G.1
  • 47
    • 0030044236 scopus 로고    scopus 로고
    • Calcium activation of mitochondrial glycerol phosphate dehydrogenase restudied
    • MacDonald M.J., Brown L.J. Calcium activation of mitochondrial glycerol phosphate dehydrogenase restudied. Arch. Biochem. Biophys. 326:1996;79-84.
    • (1996) Arch. Biochem. Biophys. , vol.326 , pp. 79-84
    • MacDonald, M.J.1    Brown, L.J.2
  • 48
    • 0031945504 scopus 로고    scopus 로고
    • Rat mitochondrial glycerol-1-phosphate dehydrogenase gene: Multiple promotors, high levels in brown adipose tissue, and testis-specific regulation by thyroid hormone
    • Gong D.W., Weintraub B.D., Reitman M. Rat mitochondrial glycerol-1-phosphate dehydrogenase gene: multiple promotors, high levels in brown adipose tissue, and testis-specific regulation by thyroid hormone. DNA Cell Biol. 17:1998;301-309.
    • (1998) DNA Cell Biol. , vol.17 , pp. 301-309
    • Gong, D.W.1    Weintraub, B.D.2    Reitman, M.3
  • 50
    • 0025738869 scopus 로고
    • 3 from Paracoccus denitrificans. Comparison with the 13-subunit beef heart enzyme
    • 3 from Paracoccus denitrificans. Comparison with the 13-subunit beef heart enzyme. Biophys. J. 60:1991;408-414.
    • (1991) Biophys. J. , vol.60 , pp. 408-414
    • Pardhasaradhi, K.1    Ludwig, B.2    Hendler, R.W.3
  • 51
    • 0019891622 scopus 로고
    • On the function of multiple subunits of cytochrome c oxidase from higher eucaryotes
    • Kadenbach B., Merle P. On the function of multiple subunits of cytochrome c oxidase from higher eucaryotes. FEBS Lett. 135:1981;1-11.
    • (1981) FEBS Lett. , vol.135 , pp. 1-11
    • Kadenbach, B.1    Merle, P.2
  • 53
    • 0029670481 scopus 로고    scopus 로고
    • - stoichiometry of cytochrome c oxidase from bovine heart by intraliposomal ATP/ADP ratios
    • - stoichiometry of cytochrome c oxidase from bovine heart by intraliposomal ATP/ADP ratios. FEBS Lett. 382:1996;121-124.
    • (1996) FEBS Lett. , vol.382 , pp. 121-124
    • Frank, V.1    Kadenbach, B.2
  • 54
    • 0030848050 scopus 로고    scopus 로고
    • Cell respiration is controlled by ATP, an allosteric inhibitor of cytochrome c oxidase
    • Arnold S., Kadenbach B. Cell respiration is controlled by ATP, an allosteric inhibitor of cytochrome c oxidase. Eur. J. Biochem. 249:1997;350-354.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 350-354
    • Arnold, S.1    Kadenbach, B.2
  • 55
    • 0032031485 scopus 로고    scopus 로고
    • 3,5-Diiodothyronine binds to subunit Va of cytochrome c oxidase and abolishes the allosteric inhibition of respiration by ATP
    • Arnold S., Goglia F., Kadenbach B. 3,5-Diiodothyronine binds to subunit Va of cytochrome c oxidase and abolishes the allosteric inhibition of respiration by ATP. Eur. J. Biochem. 252:1998;325-330.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 325-330
    • Arnold, S.1    Goglia, F.2    Kadenbach, B.3
  • 56
    • 0035659756 scopus 로고    scopus 로고
    • Priority Paper. Palmitate decreases proton pumping of liver-type cytochrome c oxidase
    • Lee I., Kadenbach B. Priority Paper. Palmitate decreases proton pumping of liver-type cytochrome c oxidase. Eur. J. Biochem. 268:2001;6329-6334.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6329-6334
    • Lee, I.1    Kadenbach, B.2
  • 58
    • 0030770323 scopus 로고    scopus 로고
    • ATP and ADP bind to cytochrome c oxidase and regulate its activity
    • Napiwotzki J., Shinzawa-Itoh K., Yoshikawa S., Kadenbach B. ATP and ADP bind to cytochrome c oxidase and regulate its activity. Biol. Chem. 378:1997;1013-1021.
    • (1997) Biol. Chem. , vol.378 , pp. 1013-1021
    • Napiwotzki, J.1    Shinzawa-Itoh, K.2    Yoshikawa, S.3    Kadenbach, B.4
  • 59
    • 0031924141 scopus 로고    scopus 로고
    • Extramitochondrial ATP/ADP-ratios regulate cytochrome c oxidase activity via binding to the cytosolic domain of subunit IV
    • Napiwotzki J., Kadenbach B. Extramitochondrial ATP/ADP-ratios regulate cytochrome c oxidase activity via binding to the cytosolic domain of subunit IV. Biol. Chem. 379:1998;335-339.
    • (1998) Biol. Chem. , vol.379 , pp. 335-339
    • Napiwotzki, J.1    Kadenbach, B.2
  • 61
    • 0000379911 scopus 로고
    • Oxidative phosphorylation: Role of inorganic phosphate and acceptor systems in control of metabolic rates
    • Lardy H.A., Wellman H. Oxidative phosphorylation: role of inorganic phosphate and acceptor systems in control of metabolic rates. J. Biol. Chem. 195:1952;215-224.
    • (1952) J. Biol. Chem. , vol.195 , pp. 215-224
    • Lardy, H.A.1    Wellman, H.2
  • 62
    • 77049249588 scopus 로고
    • Respiratory enzymes in oxidative phosphorylation: III. The steady state
    • Chance B., Williams C.M. Respiratory enzymes in oxidative phosphorylation: III. The steady state. J. Biol. Chem. 217:1955;405-427.
    • (1955) J. Biol. Chem. , vol.217 , pp. 405-427
    • Chance, B.1    Williams, C.M.2
  • 63
    • 0032970653 scopus 로고    scopus 로고
    • Minireview. A second mechanism of respiratory control
    • Kadenbach B., Arnold S. Minireview. A second mechanism of respiratory control. FEBS Lett. 447:1999;131-134.
    • (1999) FEBS Lett. , vol.447 , pp. 131-134
    • Kadenbach, B.1    Arnold, S.2
  • 64
    • 0033033002 scopus 로고    scopus 로고
    • Intramitochondrial ATP/ADP-ratios control cytochrome c oxidase activity allosterically
    • Arnold S., Kadenbach B. Intramitochondrial ATP/ADP-ratios control cytochrome c oxidase activity allosterically. FEBS Lett. 443:1999;105-108.
    • (1999) FEBS Lett. , vol.443 , pp. 105-108
    • Arnold, S.1    Kadenbach, B.2
  • 65
    • 0035702819 scopus 로고    scopus 로고
    • Minireview-hypothesis. New control of mitochondrial membrane potential and ROS-formation
    • Lee I., Bender E., Arnold S., Kadenbach B. Minireview-hypothesis. New control of mitochondrial membrane potential and ROS-formation. Biol. Chem. 382:2001;1629-1633.
    • (2001) Biol. Chem. , vol.382 , pp. 1629-1633
    • Lee, I.1    Bender, E.2    Arnold, S.3    Kadenbach, B.4
  • 66
    • 0031708941 scopus 로고    scopus 로고
    • Cytochrome c oxidase from eucaryotes but not from procaryotes is allosterically inhibited by ATP
    • Follmann K., Arnold S., Ferguson-Miller S., Kadenbach B. Cytochrome c oxidase from eucaryotes but not from procaryotes is allosterically inhibited by ATP. Biochem. Mol. Biol. Int. 45:1998;1047-1055.
    • (1998) Biochem. Mol. Biol. Int. , vol.45 , pp. 1047-1055
    • Follmann, K.1    Arnold, S.2    Ferguson-Miller, S.3    Kadenbach, B.4
  • 67
    • 0033040623 scopus 로고    scopus 로고
    • Minireview. Action of thyroid hormones at the cellular level: The mitochondrial target
    • Goglia F., Moreno M., Lanni A. Minireview. Action of thyroid hormones at the cellular level: the mitochondrial target. FEBS Lett. 452:1999;115-120.
    • (1999) FEBS Lett. , vol.452 , pp. 115-120
    • Goglia, F.1    Moreno, M.2    Lanni, A.3
  • 68
    • 0034964207 scopus 로고    scopus 로고
    • Physiological and molecular basis of thyroid hormone action
    • Yen P.M. Physiological and molecular basis of thyroid hormone action. Physiol. Rev. 81:2001;1097-1142.
    • (2001) Physiol. Rev. , vol.81 , pp. 1097-1142
    • Yen, P.M.1
  • 69
    • 0013772889 scopus 로고
    • Differential action of thyroid hormones on enzyme levels of the DPN and TPN specific isocitrate dehydrogenase
    • Kadenbach B., Goebell G., Klingenberg M. Differential action of thyroid hormones on enzyme levels of the DPN and TPN specific isocitrate dehydrogenase. Biochem. Biophys. Res. Commun. 14:1963;335-339.
    • (1963) Biochem. Biophys. Res. Commun. , vol.14 , pp. 335-339
    • Kadenbach, B.1    Goebell, G.2    Klingenberg, M.3
  • 70
    • 0027260708 scopus 로고
    • Review. Thyroid hormone action on mitochondrial energy transfer
    • Soboll S. Review. Thyroid hormone action on mitochondrial energy transfer. Biochim. Biophys. Acta. 1144:1993;1-16.
    • (1993) Biochim. Biophys. Acta , vol.1144 , pp. 1-16
    • Soboll, S.1
  • 72
    • 0031821079 scopus 로고    scopus 로고
    • 3,5-Diiodo-L-thyronine and 3,5,5′-triiodo-L-thyronine both improve the cold tolerance of hypothyroid rats, but possibly via different mechanisms
    • Lanni A., Moreno M., Lombardi A., Goglia F. 3,5-Diiodo-L-thyronine and 3,5,5′-triiodo-L-thyronine both improve the cold tolerance of hypothyroid rats, but possibly via different mechanisms. Pflügers Arch. 436:1998;407-414.
    • (1998) Pflügers Arch. , vol.436 , pp. 407-414
    • Lanni, A.1    Moreno, M.2    Lombardi, A.3    Goglia, F.4
  • 73
    • 0036191639 scopus 로고    scopus 로고
    • Biochemistry, cellular and molecular biology, and physiological roles of the iodothyronine selenodeiodinases
    • Bianco A.C., Salvatore D., Gereben B., Berry M.J., Larsen P.R. Biochemistry, cellular and molecular biology, and physiological roles of the iodothyronine selenodeiodinases. Endocr. Rev. 23:2002;38-89.
    • (2002) Endocr. Rev. , vol.23 , pp. 38-89
    • Bianco, A.C.1    Salvatore, D.2    Gereben, B.3    Berry, M.J.4    Larsen, P.R.5
  • 75
    • 0031680036 scopus 로고    scopus 로고
    • Role of mitochondrial calcium transport in the control of substrate oxidation
    • Hansford R.G., Zorov D. Role of mitochondrial calcium transport in the control of substrate oxidation. Mol. Cell. Biochem. 184:1998;359-369.
    • (1998) Mol. Cell. Biochem. , vol.184 , pp. 359-369
    • Hansford, R.G.1    Zorov, D.2
  • 76
    • 0035923443 scopus 로고    scopus 로고
    • Cyclic adenosine monophosphate-dependent phosphorylation of mammalian mitochondrial proteins: Enzyme and substrate characterization and functional role
    • Technikova-Dobrova Z., Sardanelli A.M., Speranza F., Scacco S., Signorile A., Lorusso V., Papa S. Cyclic adenosine monophosphate-dependent phosphorylation of mammalian mitochondrial proteins: enzyme and substrate characterization and functional role. Biochemistry. 40:2001;13941-13947.
    • (2001) Biochemistry , vol.40 , pp. 13941-13947
    • Technikova-Dobrova, Z.1    Sardanelli, A.M.2    Speranza, F.3    Scacco, S.4    Signorile, A.5    Lorusso, V.6    Papa, S.7
  • 77
    • 0036183196 scopus 로고    scopus 로고
    • Evidence of undiscovered cell regulatory mechanisms: Phosphoproteins and protein kinases in mitochondria
    • Thomson M. Evidence of undiscovered cell regulatory mechanisms: phosphoproteins and protein kinases in mitochondria. Cell. Mol. Life Sci. 59:2002;213-219.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 213-219
    • Thomson, M.1
  • 78
    • 0034625326 scopus 로고    scopus 로고
    • CAMP-dependent phosphorylation of the nuclear encoded 18-kDa (IP) subunit of respiratory complex I and activation of the complex in serum-starved mouse fibroblast cultures
    • Scacco S., Vergari R., Scarpulla R.C., Technikova-Dobrova Z., Sardanella A., Lambo R., Lorusso V., Papa S. cAMP-dependent phosphorylation of the nuclear encoded 18-kDa (IP) subunit of respiratory complex I and activation of the complex in serum-starved mouse fibroblast cultures. J. Biol. Chem. 275:2000;17578-17582.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17578-17582
    • Scacco, S.1    Vergari, R.2    Scarpulla, R.C.3    Technikova-Dobrova, Z.4    Sardanella, A.5    Lambo, R.6    Lorusso, V.7    Papa, S.8
  • 80
    • 0033965893 scopus 로고    scopus 로고
    • The allosteric ATP-inhibition of cytochrome c oxidase is reversibly switched on by cAMP-dependent phosphorylation
    • Bender E., Kadenbach B. The allosteric ATP-inhibition of cytochrome c oxidase is reversibly switched on by cAMP-dependent phosphorylation. FEBS Lett. 466:2000;130-134.
    • (2000) FEBS Lett. , vol.466 , pp. 130-134
    • Bender, E.1    Kadenbach, B.2
  • 81
    • 0021426610 scopus 로고
    • The current-voltage relationships of liposomes and mitochondria
    • O'Shea P.S., Petrone G., Casey R.P., Azzi A. The current-voltage relationships of liposomes and mitochondria. Biochem. J. 219:1984;719-726.
    • (1984) Biochem. J. , vol.219 , pp. 719-726
    • O'Shea, P.S.1    Petrone, G.2    Casey, R.P.3    Azzi, A.4
  • 82
    • 0025983605 scopus 로고
    • The rate of ATP synthesis as a function of ΔΨ catalyzed by the active, reduced H+-ATPase from chloroplasts
    • Junesch U., Gräber P. The rate of ATP synthesis as a function of ΔΨ catalyzed by the active, reduced H+-ATPase from chloroplasts. FEBS Lett. 294:1991;275-278.
    • (1991) FEBS Lett. , vol.294 , pp. 275-278
    • Junesch, U.1    Gräber, P.2
  • 83
    • 0026035079 scopus 로고
    • ATP synthesis in chromatophores driven by artificially induced ion gradients
    • Turina P., Melandri B.A., Gräber P. ATP synthesis in chromatophores driven by artificially induced ion gradients. Eur. J. Biochem. 196:1991;225-229.
    • (1991) Eur. J. Biochem. , vol.196 , pp. 225-229
    • Turina, P.1    Melandri, B.A.2    Gräber, P.3
  • 85
    • 0033517144 scopus 로고    scopus 로고
    • ATP synthesis by F-type ATP synthase is obligatorily dependent on the transmembrane voltage
    • Kaim G., Dimroth P. ATP synthesis by F-type ATP synthase is obligatorily dependent on the transmembrane voltage. EMBO J. 18:1999;4118-4127.
    • (1999) EMBO J. , vol.18 , pp. 4118-4127
    • Kaim, G.1    Dimroth, P.2
  • 86
    • 0013866046 scopus 로고
    • ATP formation caused by acid-base transition of spinach chloroplasts
    • Jagendorf A.T., Uribe E. ATP formation caused by acid-base transition of spinach chloroplasts. Proc. Natl. Acad. Sci. U. S. A. 55:1966;170-177.
    • (1966) Proc. Natl. Acad. Sci. U. S. A. , vol.55 , pp. 170-177
    • Jagendorf, A.T.1    Uribe, E.2
  • 89
    • 0033590122 scopus 로고    scopus 로고
    • The role of calcium in pre- and postmitochondrial events in tributyltin-induced T-cell apoptosis
    • Stridh H., Gigliotti D., Orrenius S., Cotgreave I. The role of calcium in pre- and postmitochondrial events in tributyltin-induced T-cell apoptosis. Biochem. Biophys. Res. Commun. 266:1999;460-465.
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 460-465
    • Stridh, H.1    Gigliotti, D.2    Orrenius, S.3    Cotgreave, I.4
  • 90
    • 0024240359 scopus 로고
    • Altered relationship between proton motive force and respiration rate in non-phosphorylating liver mitochondria isolated from rats of different thyroid hormone status
    • Hafner R.P., Nobes C.D., McGown A.D., Brand M.D. Altered relationship between proton motive force and respiration rate in non-phosphorylating liver mitochondria isolated from rats of different thyroid hormone status. Eur. J. Biochem. 178:1988;511-518.
    • (1988) Eur. J. Biochem. , vol.178 , pp. 511-518
    • Hafner, R.P.1    Nobes, C.D.2    McGown, A.D.3    Brand, M.D.4
  • 91
    • 0025858290 scopus 로고
    • Influence of N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline modification on proton translocation and membrane potential of reconstituted cytochrome c oxidase support "proton slippage"
    • Steverding D., Kadenbach B. Influence of N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline modification on proton translocation and membrane potential of reconstituted cytochrome c oxidase support "proton slippage" J. Biol. Chem. 266:1991;8097-8101.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8097-8101
    • Steverding, D.1    Kadenbach, B.2
  • 92
    • 0027481132 scopus 로고
    • Proton slippage in cytochrome c oxidase of Paracoccus denitrificans. Membrane potential measurements with the two- and three-subunit enzyme
    • Steverding D., Köhnke D., Ludwig B., Kadenbach B. Proton slippage in cytochrome c oxidase of Paracoccus denitrificans. Membrane potential measurements with the two- and three-subunit enzyme. Eur. J. Biochem. 212:1993;827-831.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 827-831
    • Steverding, D.1    Köhnke, D.2    Ludwig, B.3    Kadenbach, B.4
  • 93
    • 0027254547 scopus 로고
    • Effects of cardiac work on electrical potential gradient across mitochondrial membrane in perfused rat hearts
    • Wan B., Doumen C., Duszynski J., Salama G., Vary T.C., LaNoue K.F. Effects of cardiac work on electrical potential gradient across mitochondrial membrane in perfused rat hearts. Am. J. Physiol. 265:1993;H453-H460.
    • (1993) Am. J. Physiol. , vol.265
    • Wan, B.1    Doumen, C.2    Duszynski, J.3    Salama, G.4    Vary, T.C.5    LaNoue, K.F.6
  • 95
    • 0022409022 scopus 로고
    • Electron spin resonance studies of intact mammalian skeletal muscle
    • Jackson M.J., Edwards R.H., Symons M.C. Electron spin resonance studies of intact mammalian skeletal muscle. Biochim. Biophys. Acta. 847:1985;185-190.
    • (1985) Biochim. Biophys. Acta , vol.847 , pp. 185-190
    • Jackson, M.J.1    Edwards, R.H.2    Symons, M.C.3
  • 96
    • 0030722043 scopus 로고    scopus 로고
    • Generating, partitioning, targeting and functioning of superoxide in mitochondria
    • Liu S.S. Generating, partitioning, targeting and functioning of superoxide in mitochondria. Biosci. Rep. 17:1997;259-272.
    • (1997) Biosci. Rep. , vol.17 , pp. 259-272
    • Liu, S.S.1
  • 97
    • 0033381362 scopus 로고    scopus 로고
    • Cooperation of a "reactive oxygen cycle" with the Q cycle and the proton cycle in the respiratory chain - Superoxide generating and cycling mechanism in mitochondria
    • Liu S.S. Cooperation of a "reactive oxygen cycle" with the Q cycle and the proton cycle in the respiratory chain - superoxide generating and cycling mechanism in mitochondria. J. Bioenerg. Biomembr. 31:1999;367-376.
    • (1999) J. Bioenerg. Biomembr. , vol.31 , pp. 367-376
    • Liu, S.S.1
  • 98
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • Korshunov S.S., Skulachev V.P., Starkov A.A. High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett. 416:1997;15-18.
    • (1997) FEBS Lett. , vol.416 , pp. 15-18
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov, A.A.3
  • 99
    • 0037125237 scopus 로고    scopus 로고
    • Mitochondria hyperpolarization is an early event in oxidized low-density lipoprotein-induced apoptosis in Caco-2 intestinal cells
    • Giovannini C., Matarrese P., Scazzocchio B., Sanchez M., Masella R., Malorni W. Mitochondria hyperpolarization is an early event in oxidized low-density lipoprotein-induced apoptosis in Caco-2 intestinal cells. FEBS Lett. 523:2002;200-206.
    • (2002) FEBS Lett. , vol.523 , pp. 200-206
    • Giovannini, C.1    Matarrese, P.2    Scazzocchio, B.3    Sanchez, M.4    Masella, R.5    Malorni, W.6
  • 101
    • 0037100275 scopus 로고    scopus 로고
    • Persistent mitochondrial hyperpolarization, increased reactive oxygen intermediate production, and cytoplasmic alkalinization characterize altered IL-10 signaling in patients with systemic lupus erythematosus
    • Gergely P. Jr., Niland B., Gonchoroff N., Pullmann R. Jr., Phillips P.E., Perl A. Persistent mitochondrial hyperpolarization, increased reactive oxygen intermediate production, and cytoplasmic alkalinization characterize altered IL-10 signaling in patients with systemic lupus erythematosus. J. Immunol. 169:2002;1092-1101.
    • (2002) J. Immunol. , vol.169 , pp. 1092-1101
    • Gergely P., Jr.1    Niland, B.2    Gonchoroff, N.3    Pullmann R., Jr.4    Phillips, P.E.5    Perl, A.6
  • 102
    • 0008152693 scopus 로고    scopus 로고
    • Production of reactive oxygen species in mitochondria and age-associated pathophysiology: A reality check
    • E. Cadenas, & L. Packer. New York: Marcel Dekker, Inc.
    • Forman H.J., Azzi A. Production of reactive oxygen species in mitochondria and age-associated pathophysiology: a reality check. Cadenas E., Packer L. Understanding the Process of Aging. The Roles of Mitochondria, Free Radicals, and Antioxidants. 1999;73-94 Marcel Dekker, Inc. New York.
    • (1999) Understanding the Process of Aging. The Roles of Mitochondria, Free Radicals, and Antioxidants , pp. 73-94
    • Forman, H.J.1    Azzi, A.2
  • 106
    • 0026743031 scopus 로고
    • Reactive oxygen and DNA damage in mitochondria
    • Richter C. Reactive oxygen and DNA damage in mitochondria. Mutat. Res. 275:1992;249-255.
    • (1992) Mutat. Res. , vol.275 , pp. 249-255
    • Richter, C.1
  • 108
    • 0034468736 scopus 로고    scopus 로고
    • Role of reactive oxygen species (ROS) in apoptosis induction
    • Simon H.U., Haj-Yehia A., Levi-Schaffer F. Role of reactive oxygen species (ROS) in apoptosis induction. Apoptosis. 5:2000;415-418.
    • (2000) Apoptosis , vol.5 , pp. 415-418
    • Simon, H.U.1    Haj-Yehia, A.2    Levi-Schaffer, F.3
  • 109
    • 0034991034 scopus 로고    scopus 로고
    • Signalling apoptosis: A radical approach
    • Carmody R.J., Cotter T.G. Signalling apoptosis: a radical approach. Redox Rep. 6:2001;77-90.
    • (2001) Redox Rep. , vol.6 , pp. 77-90
    • Carmody, R.J.1    Cotter, T.G.2
  • 110
    • 0028882764 scopus 로고
    • Mitochondrial production of reactive oxygen species in corticol neurons following exposure to N-methyl-D-aspartate
    • Dugan L.L., Sensi S.L., Canzoniero L.M., Handran S.M., Lin T.S., Goldberg M.P., Choi D.W. Mitochondrial production of reactive oxygen species in corticol neurons following exposure to N-methyl-D-aspartate. J. Neurosci. 15:1995;6377-6388.
    • (1995) J. Neurosci. , vol.15 , pp. 6377-6388
    • Dugan, L.L.1    Sensi, S.L.2    Canzoniero, L.M.3    Handran, S.M.4    Lin, T.S.5    Goldberg, M.P.6    Choi, D.W.7
  • 111
    • 0029064518 scopus 로고
    • Glutamate induces the production of reactive oxygen species in cultured forebrain neurons following NMDA receptor activation
    • Reynolds I.J., Hastings T.G. Glutamate induces the production of reactive oxygen species in cultured forebrain neurons following NMDA receptor activation. J. Neurosci. 15:1995;3318-3327.
    • (1995) J. Neurosci. , vol.15 , pp. 3318-3327
    • Reynolds, I.J.1    Hastings, T.G.2
  • 112
    • 0030008052 scopus 로고    scopus 로고
    • Superoxide production in rat hippocampal neurons: Selective imaging with hydroethidine
    • Bindokas V.P., Jordan J., Lee C.C., Miller R.J. Superoxide production in rat hippocampal neurons: selective imaging with hydroethidine. J. Neurosci. 16:1996;1324-1336.
    • (1996) J. Neurosci. , vol.16 , pp. 1324-1336
    • Bindokas, V.P.1    Jordan, J.2    Lee, C.C.3    Miller, R.J.4
  • 113
    • 0000236120 scopus 로고    scopus 로고
    • In vitro ischemia promotes glutamate-mediated free radical generation and intracellular calcium accumulation in hippocampal pyramidal neurons
    • Velazquez J.L.P., Frantseva M.V., Carlen P.L. In vitro ischemia promotes glutamate-mediated free radical generation and intracellular calcium accumulation in hippocampal pyramidal neurons. J. Neurosci. 17:1997;9085-9094.
    • (1997) J. Neurosci. , vol.17 , pp. 9085-9094
    • Velazquez, J.L.P.1    Frantseva, M.V.2    Carlen, P.L.3
  • 114
    • 0032535275 scopus 로고    scopus 로고
    • Mitochondrial control of acute glutamate excitotoxicity in cultured cerebellar granule cells
    • Castilho R.F., Hansson O., Ward M.W., Budd S.L., Nicholls D.G. Mitochondrial control of acute glutamate excitotoxicity in cultured cerebellar granule cells. J. Neurosci. 18:1998;10277-10286.
    • (1998) J. Neurosci. , vol.18 , pp. 10277-10286
    • Castilho, R.F.1    Hansson, O.2    Ward, M.W.3    Budd, S.L.4    Nicholls, D.G.5
  • 115
    • 0031869004 scopus 로고    scopus 로고
    • NMDA-induced superoxide production and neurotoxicity in cultured rat hippocampal neurons: Role of mitochondria
    • Sengpiel B., Preis E., Krieglstein J., Prehn J.H. NMDA-induced superoxide production and neurotoxicity in cultured rat hippocampal neurons: role of mitochondria. Eur. J. Neurosci. 10:1998;1903-1910.
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 1903-1910
    • Sengpiel, B.1    Preis, E.2    Krieglstein, J.3    Prehn, J.H.4
  • 117
    • 0035865259 scopus 로고    scopus 로고
    • Exploration of the role of reactive oxygen species in glutamate neurotoxicity in rat hippocampal neurones in culture
    • Vergun O., Sobolevsky A.I., Yelshansky M.V., Keelan J., Khodorov B.I., Duchen M.R. Exploration of the role of reactive oxygen species in glutamate neurotoxicity in rat hippocampal neurones in culture. J. Physiol. 531:2001;147-163.
    • (2001) J. Physiol. , vol.531 , pp. 147-163
    • Vergun, O.1    Sobolevsky, A.I.2    Yelshansky, M.V.3    Keelan, J.4    Khodorov, B.I.5    Duchen, M.R.6
  • 118
    • 0030983228 scopus 로고    scopus 로고
    • A possible role of slips in cytochrome c oxidase in the antioxygen defense system of the cell
    • Papa S., Guerrieri F., Capitanio N. A possible role of slips in cytochrome c oxidase in the antioxygen defense system of the cell. Biosci. Rep. 17:1997;23-31.
    • (1997) Biosci. Rep. , vol.17 , pp. 23-31
    • Papa, S.1    Guerrieri, F.2    Capitanio, N.3
  • 120
    • 84958039680 scopus 로고
    • Reversible inhibition of the coupling between phosphorylation and oxidation
    • Loomis W.F., Lipman F. Reversible inhibition of the coupling between phosphorylation and oxidation. J. Biol. Chem. 173:1948;807-808.
    • (1948) J. Biol. Chem. , vol.173 , pp. 807-808
    • Loomis, W.F.1    Lipman, F.2
  • 121
    • 0014676185 scopus 로고
    • Mechanism of action of reagents that uncouple oxidative phosphorylation
    • Weinbach E.C., Garbus J. Mechanism of action of reagents that uncouple oxidative phosphorylation. Nature. 221:1969;1016-1018.
    • (1969) Nature , vol.221 , pp. 1016-1018
    • Weinbach, E.C.1    Garbus, J.2
  • 122
    • 0017102422 scopus 로고
    • Biological applications of ionophores
    • Pressman B.C. Biological applications of ionophores. Annu. Rev. Biochem. 45:1976;501-530.
    • (1976) Annu. Rev. Biochem. , vol.45 , pp. 501-530
    • Pressman, B.C.1
  • 123
    • 0017293611 scopus 로고
    • Effect of long-chain fatty acids and acyl-CoA on mitochondrial permeability, transport, and energy-coupling processes
    • Wojtczak L. Effect of long-chain fatty acids and acyl-CoA on mitochondrial permeability, transport, and energy-coupling processes. J. Bioenerg. Biomembr. 8:1976;293-311.
    • (1976) J. Bioenerg. Biomembr. , vol.8 , pp. 293-311
    • Wojtczak, L.1
  • 124
    • 0025340005 scopus 로고
    • Decoupling of oxidative phosphorylation and photophosphorylation
    • Rottenberg H. Decoupling of oxidative phosphorylation and photophosphorylation. Biochim. Biophys. Acta. 1018:1990;1-17.
    • (1990) Biochim. Biophys. Acta , vol.1018 , pp. 1-17
    • Rottenberg, H.1
  • 125
    • 0342614207 scopus 로고    scopus 로고
    • The mechanisms of fatty acid-induced proton permeability of the inner mitochondrial membrane
    • Wojtczak L., Wieckowski M.R. The mechanisms of fatty acid-induced proton permeability of the inner mitochondrial membrane. J. Bioenerg. Biomembr. 31:1999;447-455.
    • (1999) J. Bioenerg. Biomembr. , vol.31 , pp. 447-455
    • Wojtczak, L.1    Wieckowski, M.R.2
  • 126
    • 0032564864 scopus 로고    scopus 로고
    • Uncoupling: New approaches to an old problem of bioenergetics
    • Skulachev V.P. Uncoupling: new approaches to an old problem of bioenergetics. Biochim. Biophys. Acta. 1363:1998;100-124.
    • (1998) Biochim. Biophys. Acta , vol.1363 , pp. 100-124
    • Skulachev, V.P.1
  • 127
    • 0026437584 scopus 로고
    • PH gradients across phospholipid membranes caused by fast flip-flop on unionized fatty acids
    • Kamp F., Hamilton J.A. pH gradients across phospholipid membranes caused by fast flip-flop on unionized fatty acids. Proc. Natl. Acad. Sci. U. S. A. 89:1992;11367-11370.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 11367-11370
    • Kamp, F.1    Hamilton, J.A.2
  • 128
    • 0025930608 scopus 로고
    • Hypothesis. Fatty acid circuit as a physiological mechanism of uncoupling of oxidative phosphorylation
    • Skulachev V.P. Hypothesis. Fatty acid circuit as a physiological mechanism of uncoupling of oxidative phosphorylation. FEBS Lett. 294:1991;158-162.
    • (1991) FEBS Lett. , vol.294 , pp. 158-162
    • Skulachev, V.P.1
  • 129
    • 0025282623 scopus 로고
    • Does the function of adenine nucleotide translocase in fatty acid uncoupling depend on the type of mitochondria?
    • Schönfeld P. Does the function of adenine nucleotide translocase in fatty acid uncoupling depend on the type of mitochondria? FEBS Lett. 264:1990;246-248.
    • (1990) FEBS Lett. , vol.264 , pp. 246-248
    • Schönfeld, P.1
  • 130
    • 0026039964 scopus 로고
    • Interaction of adenine nucleotides with the adenine nucleotide translocase regulates the developmental changes in proton conductance of the inner mitochondrial membrane
    • Valcarce C., Cuezva J.M. Interaction of adenine nucleotides with the adenine nucleotide translocase regulates the developmental changes in proton conductance of the inner mitochondrial membrane. FEBS Lett. 294:1991;225-228.
    • (1991) FEBS Lett. , vol.294 , pp. 225-228
    • Valcarce, C.1    Cuezva, J.M.2
  • 131
    • 0028308019 scopus 로고
    • ATP/ADP antiporter is involved in uncoupling of plant mitochondria induced by low concentrations of palmitate
    • Vianello A., Petrussa E., Macri F. ATP/ADP antiporter is involved in uncoupling of plant mitochondria induced by low concentrations of palmitate. FEBS Lett. 347:1994;239-242.
    • (1994) FEBS Lett. , vol.347 , pp. 239-242
    • Vianello, A.1    Petrussa, E.2    Macri, F.3
  • 132
    • 0029830055 scopus 로고    scopus 로고
    • Photomodification of mitochondrial proteins by azido fatty acids and its effect on mitochondrial energetics. Further evidence for the role of the ADP/ATP carrier in fatty-acid-mediated uncoupling
    • Schönfeld P., Jezek P., Belyaeva E.A., Borecky J., Slyshenkov V.S., Wieckowski M.R., Wojczak V.P. Photomodification of mitochondrial proteins by azido fatty acids and its effect on mitochondrial energetics. Further evidence for the role of the ADP/ATP carrier in fatty-acid-mediated uncoupling. Eur. J. Biochem. 240:1996;387-393.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 387-393
    • Schönfeld, P.1    Jezek, P.2    Belyaeva, E.A.3    Borecky, J.4    Slyshenkov, V.S.5    Wieckowski, M.R.6    Wojczak, V.P.7
  • 133
    • 0027945163 scopus 로고
    • + transport by free fatty acids, which is further stimulated by mersalyl
    • + transport by free fatty acids, which is further stimulated by mersalyl. J. Biol. Chem. 269:1994;27329-27336.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27329-27336
    • Brustovetsky, N.N.1    Klingenberg, M.2
  • 134
    • 0024388778 scopus 로고
    • Long-chain fatty acids act as protonophoric uncouplers of oxidative phosphorylation in rat liver mitochondria
    • Schönfeld P., Schild L., Kunz W. Long-chain fatty acids act as protonophoric uncouplers of oxidative phosphorylation in rat liver mitochondria. Biochim. Biophys. Acta. 977:1989;266-272.
    • (1989) Biochim. Biophys. Acta , vol.977 , pp. 266-272
    • Schönfeld, P.1    Schild, L.2    Kunz, W.3
  • 137
    • 0028896925 scopus 로고
    • Cytoplasmic fatty acid-binding proteins: Their structure and genes
    • Veerkamp J.H., Maatman R.G. Cytoplasmic fatty acid-binding proteins: their structure and genes. Prog. Lipid Res. 34:1995;17-52.
    • (1995) Prog. Lipid Res. , vol.34 , pp. 17-52
    • Veerkamp, J.H.1    Maatman, R.G.2
  • 139
    • 0024576657 scopus 로고
    • On the role of fatty acid binding proteins in fatty acid transport and metabolism
    • Spener F., Börchers T., Mukherjea M. On the role of fatty acid binding proteins in fatty acid transport and metabolism. FEBS Lett. 244:1989;1-5.
    • (1989) FEBS Lett. , vol.244 , pp. 1-5
    • Spener, F.1    Börchers, T.2    Mukherjea, M.3
  • 140
    • 0032901360 scopus 로고    scopus 로고
    • Structure and function of the uncoupling protein from brown adipose tissue
    • Klingenberg M., Huang S.-G. Structure and function of the uncoupling protein from brown adipose tissue. Biochim. Biophys. Acta. 1415:1999;271-296.
    • (1999) Biochim. Biophys. Acta , vol.1415 , pp. 271-296
    • Klingenberg, M.1    Huang, S.-G.2
  • 142
    • 0022461282 scopus 로고
    • Quantification of fatty acid activation of the uncoupling protein in brown adipocytes and mitochondria from guinea-pig
    • Cunningham S.A., Wiesinger H., Nicholls D.G. Quantification of fatty acid activation of the uncoupling protein in brown adipocytes and mitochondria from guinea-pig. Eur. J. Biochem. 157:1986;415-420.
    • (1986) Eur. J. Biochem. , vol.157 , pp. 415-420
    • Cunningham, S.A.1    Wiesinger, H.2    Nicholls, D.G.3
  • 143
    • 0021041042 scopus 로고
    • Brown-adipose-tissue mitochondria: The regulation of the 32 000-Mr uncoupling protein by fatty acids and purine nucleotides
    • Rial E., Poustie A., Nicholls D.G. Brown-adipose-tissue mitochondria: the regulation of the 32. 000-Mr uncoupling protein by fatty acids and purine nucleotides Eur. J. Biochem. 137:1983;197-203.
    • (1983) Eur. J. Biochem. , vol.137 , pp. 197-203
    • Rial, E.1    Poustie, A.2    Nicholls, D.G.3
  • 144
    • 0027980820 scopus 로고
    • + transport activity of the reconstituted uncoupling protein
    • + transport activity of the reconstituted uncoupling protein. J. Biol. Chem. 269:1994;2508-2515.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2508-2515
    • Winkler, E.1    Klingenberg, M.2
  • 145
    • 0034735799 scopus 로고    scopus 로고
    • Coenzyme Q is an obligatory cofactor for uncoupling protein function
    • Echtay K.S., Winkler E., Klingenberg M. Coenzyme Q is an obligatory cofactor for uncoupling protein function. Nature. 408:2000;609-613.
    • (2000) Nature , vol.408 , pp. 609-613
    • Echtay, K.S.1    Winkler, E.2    Klingenberg, M.3
  • 146
    • 0343900275 scopus 로고    scopus 로고
    • The uncoupling protein UCP1 does not increase the proton conductance of the inner mitochondrial membrane by functioning as a fatty acid anion transporter
    • González-Barroso M.M., Fleury C., Bouillaud F., Nicholls D.G., Rial E. The uncoupling protein UCP1 does not increase the proton conductance of the inner mitochondrial membrane by functioning as a fatty acid anion transporter. J. Biol. Chem. 273:1998;15528-15532.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15528-15532
    • González-Barroso, M.M.1    Fleury, C.2    Bouillaud, F.3    Nicholls, D.G.4    Rial, E.5
  • 150
    • 0031560941 scopus 로고    scopus 로고
    • UCP3: An uncoupling protein homologue expressed preferentially and abundantly in skeletal muscle and brown adipose tissue
    • Vidal-Puig A., Solanes G., Grujic D., Flier J.S., Lowell B.B. UCP3: an uncoupling protein homologue expressed preferentially and abundantly in skeletal muscle and brown adipose tissue. Biochem. Biophys. Res. Commun. 235:1997;79-82.
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 79-82
    • Vidal-Puig, A.1    Solanes, G.2    Grujic, D.3    Flier, J.S.4    Lowell, B.B.5
  • 151
    • 0032998265 scopus 로고    scopus 로고
    • UCP4, a novel brain-specific mitochondrial protein that reduces membrane potential in mammalian cells
    • Mao W., Yu X.X., Zhong A., Li W., Brush J., Sherwood S.W., Adams S.H., Pan G. UCP4, a novel brain-specific mitochondrial protein that reduces membrane potential in mammalian cells. FEBS Lett. 443:1999;326-330.
    • (1999) FEBS Lett. , vol.443 , pp. 326-330
    • Mao, W.1    Yu, X.X.2    Zhong, A.3    Li, W.4    Brush, J.5    Sherwood, S.W.6    Adams, S.H.7    Pan, G.8
  • 153
    • 0035091326 scopus 로고    scopus 로고
    • Genetic and physiological analysis of the role of uncoupling proteins in human energy homeostasis
    • Pecqueur C., Couplan E., Bouillaud F., Ricquier D. Genetic and physiological analysis of the role of uncoupling proteins in human energy homeostasis. J. Mol. Med. 79:2001;48-56.
    • (2001) J. Mol. Med. , vol.79 , pp. 48-56
    • Pecqueur, C.1    Couplan, E.2    Bouillaud, F.3    Ricquier, D.4
  • 155
    • 0035206376 scopus 로고    scopus 로고
    • Perspectives on the biology of uncoupling protein (UCP) homologues
    • Adams S.H., Pan G., Yu X.X. Perspectives on the biology of uncoupling protein (UCP) homologues. Biochem. Soc. Trans. 29:2001;798-802.
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 798-802
    • Adams, S.H.1    Pan, G.2    Yu, X.X.3
  • 156
    • 0036584365 scopus 로고    scopus 로고
    • Uncoupling proteins and thermoregulation
    • Argyropoulos G., Harper M.E. Uncoupling proteins and thermoregulation. J. Appl. Physiol. 92:2002;2187-2198.
    • (2002) J. Appl. Physiol. , vol.92 , pp. 2187-2198
    • Argyropoulos, G.1    Harper, M.E.2
  • 157
    • 0037135559 scopus 로고    scopus 로고
    • No evidence for a basal, retinoic or superoxide-induced uncoupling activity of the UCP2 present in spleen or lung mitochondria
    • Couplan E., Gonzalez-Barroso M., Alves-Guerra M.C., Ricquier D., Goubern M., Bouillaud F. No evidence for a basal, retinoic or superoxide-induced uncoupling activity of the UCP2 present in spleen or lung mitochondria. J. Biol. Chem. 277:2002;26268-26275.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26268-26275
    • Couplan, E.1    Gonzalez-Barroso, M.2    Alves-Guerra, M.C.3    Ricquier, D.4    Goubern, M.5    Bouillaud, F.6
  • 159
    • 0030712088 scopus 로고    scopus 로고
    • Enhanced expression of uncoupling protein 2 gene in rat white adipose tissue and skeletal muscle following chronic treatment with thyroid hormone
    • Masaki T., Yoshimatsu H., Kakume T., Hidaka S., Kurokawa M., Sakata T. Enhanced expression of uncoupling protein 2 gene in rat white adipose tissue and skeletal muscle following chronic treatment with thyroid hormone. FEBS Lett. 418:1997;323-326.
    • (1997) FEBS Lett. , vol.418 , pp. 323-326
    • Masaki, T.1    Yoshimatsu, H.2    Kakume, T.3    Hidaka, S.4    Kurokawa, M.5    Sakata, T.6
  • 160
    • 12444333890 scopus 로고    scopus 로고
    • Uncoupling protein-3 is a molecular determinant for the regulation of resting metabolic rate by thyroid hormone
    • De Lange P., Lanni A., Beneduce L., Moreno M., Lombardi A., Silvestri E., Goglia F. Uncoupling protein-3 is a molecular determinant for the regulation of resting metabolic rate by thyroid hormone. Endocrinology. 143:2001;504-510.
    • (2001) Endocrinology , vol.143 , pp. 504-510
    • De Lange, P.1    Lanni, A.2    Beneduce, L.3    Moreno, M.4    Lombardi, A.5    Silvestri, E.6    Goglia, F.7
  • 161
    • 0030869755 scopus 로고    scopus 로고
    • Uncoupling protein-3 is a mediator of thermogenesis regulated by thyroid hormone, beta3-adrenergic agonists, and leptin
    • Gong D.W., He Y., Karas M., Reitman M. Uncoupling protein-3 is a mediator of thermogenesis regulated by thyroid hormone, beta3-adrenergic agonists, and leptin. J. Biol. Chem. 272:1997;24129-24132.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24129-24132
    • Gong, D.W.1    He, Y.2    Karas, M.3    Reitman, M.4
  • 162
    • 0027344935 scopus 로고
    • Influence of hyperthyroidism on superoxide radical and hydrogen peroxide production by rat liver submitochondrial particles
    • Videla L.A., Fernandez V. Influence of hyperthyroidism on superoxide radical and hydrogen peroxide production by rat liver submitochondrial particles. Free Radic. Res. Commun. 18:1993;329-335.
    • (1993) Free Radic. Res. Commun. , vol.18 , pp. 329-335
    • Videla, L.A.1    Fernandez, V.2
  • 163
    • 0023221581 scopus 로고
    • Variable stoichiometry of proton pumping by the mitochondrial respiratory chain
    • Murphy M.P., Brand M.D. Variable stoichiometry of proton pumping by the mitochondrial respiratory chain. Nature. 329:1987;170-172.
    • (1987) Nature , vol.329 , pp. 170-172
    • Murphy, M.P.1    Brand, M.D.2
  • 164
    • 0024276134 scopus 로고
    • 1 complex of mitochondria at high membrane potential
    • 1 complex of mitochondria at high membrane potential. Eur. J. Biochem. 173:1988;645-651.
    • (1988) Eur. J. Biochem. , vol.173 , pp. 645-651
    • Murphy, M.P.1    Brand, M.D.2
  • 165
    • 0028010091 scopus 로고
    • Experimental discrimination between proton leak and redox slip during mitochondrial electron transport
    • Brand M.D., Chien L.-F., Diolet P. Experimental discrimination between proton leak and redox slip during mitochondrial electron transport. Biochem. J. 297:1994;27-29.
    • (1994) Biochem. J. , vol.297 , pp. 27-29
    • Brand, M.D.1    Chien, L.-F.2    Diolet, P.3
  • 167
    • 0033785071 scopus 로고    scopus 로고
    • Uncoupling to survive? The role of mitochondrial inefficiency in ageing
    • Brand M.D. Uncoupling to survive? The role of mitochondrial inefficiency in ageing. Exp. Gerontol. 35:2000;811-820.
    • (2000) Exp. Gerontol. , vol.35 , pp. 811-820
    • Brand, M.D.1
  • 170
    • 0034012499 scopus 로고    scopus 로고
    • Intrinsic metabolic depression in cells isolated from the hepatopancreas of estivating snails
    • Guppy M., Reeves D.C., Bishop T., Withers P., Buckingham J.A., Brand M.D. Intrinsic metabolic depression in cells isolated from the hepatopancreas of estivating snails. FASEB J. 14:2000;999-1004.
    • (2000) FASEB J. , vol.14 , pp. 999-1004
    • Guppy, M.1    Reeves, D.C.2    Bishop, T.3    Withers, P.4    Buckingham, J.A.5    Brand, M.D.6
  • 172
    • 0034597633 scopus 로고    scopus 로고
    • ATP synthase: What dictates the size of a ring?
    • Ferguson S.J. ATP synthase: what dictates the size of a ring? Curr. Biol. 10:2000;R804-R808.
    • (2000) Curr. Biol. , vol.10
    • Ferguson, S.J.1
  • 173
    • 0035942281 scopus 로고    scopus 로고
    • The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10
    • Jiang W., Hermolin J., Fillingame R.H. The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10. Proc. Natl. Acad. Sci. U. S. A. 98:2001;4966-4971.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 4966-4971
    • Jiang, W.1    Hermolin, J.2    Fillingame, R.H.3
  • 176
    • 0037207875 scopus 로고    scopus 로고
    • Bioenergetic properties of the thermoalkaliphilic Bacillus sp. strain TA2.A1
    • Olsson K., Keis S., Morgan H.W., Dimroth P., Cook G.M. Bioenergetic properties of the thermoalkaliphilic Bacillus sp. strain TA2.A1. J. Bacteriol. 185:2003;461-465.
    • (2003) J. Bacteriol. , vol.185 , pp. 461-465
    • Olsson, K.1    Keis, S.2    Morgan, H.W.3    Dimroth, P.4    Cook, G.M.5
  • 177
    • 0021755472 scopus 로고
    • Pumping of protons from the mitochondrial matrix by cytochrome c oxidase
    • Wikström M. Pumping of protons from the mitochondrial matrix by cytochrome c oxidase. Nature. 308:1984;558-560.
    • (1984) Nature , vol.308 , pp. 558-560
    • Wikström, M.1
  • 178
    • 0023013877 scopus 로고
    • Upper and lower limits of the proton stoichiometry of cytochrome c oxidation in rat liver mitoplasts
    • Reynafarje B., Costa L.E., Lehninger A.L. Upper and lower limits of the proton stoichiometry of cytochrome c oxidation in rat liver mitoplasts. J. Biol. Chem. 261:1986;8254-8262.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8254-8262
    • Reynafarje, B.1    Costa, L.E.2    Lehninger, A.L.3
  • 179
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respiration
    • Babcock G.T., Wikström M. Oxygen activation and the conservation of energy in cell respiration. Nature. 356:1992;301-309.
    • (1992) Nature , vol.356 , pp. 301-309
    • Babcock, G.T.1    Wikström, M.2
  • 180
  • 183
    • 0025799527 scopus 로고
    • - stoichiometry of mitochondrial cytochrome complexes reconstituted in liposomes. Rate-dependent changes of the stoichiometry in the cytochrome c oxidase vesicles
    • - stoichiometry of mitochondrial cytochrome complexes reconstituted in liposomes. Rate-dependent changes of the stoichiometry in the cytochrome c oxidase vesicles. FEBS Lett. 288:1991;179-182.
    • (1991) FEBS Lett. , vol.288 , pp. 179-182
    • Capitanio, N.1    Capitanio, G.2    De Nitto, E.3    Billani, G.4    Papa, S.5
  • 185
    • 0035909801 scopus 로고    scopus 로고
    • Carboxyl residues in the iron-sulfur protein are involved in the proton pumping activity of P. denitrificans bc (1) complex
    • Cocco T., Cutecchia G., Ludwig B., Korn M., Papa S., Lorusso M. Carboxyl residues in the iron-sulfur protein are involved in the proton pumping activity of P. denitrificans bc (1) complex. Biochemistry. 40:2001;15396-15402.
    • (2001) Biochemistry , vol.40 , pp. 15396-15402
    • Cocco, T.1    Cutecchia, G.2    Ludwig, B.3    Korn, M.4    Papa, S.5    Lorusso, M.6
  • 187
    • 0033741298 scopus 로고    scopus 로고
    • X-ray structure and the reaction mechanism of bovine heart cytochrome c oxidase
    • Yoshikawa S., Shinzawa-Itoh K., Tsukihara T. X-ray structure and the reaction mechanism of bovine heart cytochrome c oxidase. J. Inorg. Biochem. 82:2000;1-7.
    • (2000) J. Inorg. Biochem. , vol.82 , pp. 1-7
    • Yoshikawa, S.1    Shinzawa-Itoh, K.2    Tsukihara, T.3
  • 188
    • 0033576277 scopus 로고    scopus 로고
    • Cytochrome c oxidase: Catalytic cycle and mechanisms of proton pumping - A discussion
    • Michel H. Cytochrome c oxidase: catalytic cycle and mechanisms of proton pumping - a discussion. Biochemistry. 38:1999;15129-15140.
    • (1999) Biochemistry , vol.38 , pp. 15129-15140
    • Michel, H.1
  • 189
    • 0001397720 scopus 로고    scopus 로고
    • The role of magnesium and its associated water channel in activity and regulation of cytochrome c oxidase
    • G. Peschek, W. Loeffelhardt, & G. Schmetterer. New York: Kluwer Academic/Plenum Press
    • Florens L., Hoganson C., McCracken J., Fetter J., Mills D., Babcock G.T., Ferguson-Miller S. The role of magnesium and its associated water channel in activity and regulation of cytochrome c oxidase. Peschek G., Loeffelhardt W., Schmetterer G. The Phototropic Procaryotes. 1999;329-339 Kluwer Academic/Plenum Press, New York.
    • (1999) The Phototropic Procaryotes , pp. 329-339
    • Florens, L.1    Hoganson, C.2    McCracken, J.3    Fetter, J.4    Mills, D.5    Babcock, G.T.6    Ferguson-Miller, S.7
  • 190
    • 0034640452 scopus 로고    scopus 로고
    • Mechanism of proton translocation by cytochrome c oxidase: A new four-stroke histidine cycle
    • Wikström M. Mechanism of proton translocation by cytochrome c oxidase: a new four-stroke histidine cycle. Biochim. Biophys. Acta. 1458:2000;188-198.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 188-198
    • Wikström, M.1
  • 192
    • 0023321462 scopus 로고
    • On the role of subunit III in proton translocation in cytochrome c oxidase
    • Prochaska L.J., Fink P.S. On the role of subunit III in proton translocation in cytochrome c oxidase. J. Bioenerg. Biomembr. 19:1987;143-166.
    • (1987) J. Bioenerg. Biomembr. , vol.19 , pp. 143-166
    • Prochaska, L.J.1    Fink, P.S.2
  • 193
    • 0024422115 scopus 로고
    • Slip and leak in mitochondrial oxidative phosphorylation
    • Murphy M.P. Slip and leak in mitochondrial oxidative phosphorylation. Biochim. Biophys. Acta. 977:1989;123-141.
    • (1989) Biochim. Biophys. Acta , vol.977 , pp. 123-141
    • Murphy, M.P.1
  • 195
    • 0034696637 scopus 로고    scopus 로고
    • Mutations in the putative H-channel in the cytochrome c oxidase from Rhodobacter sphaeroides show that this channel is not important for proton conduction but reveal modulation of the properties of heme a
    • Lee H.-M., Das T.K., Rousseau D.L., Mills D.A., Ferguson-Miller S., Gennis R.B. Mutations in the putative H-channel in the cytochrome c oxidase from Rhodobacter sphaeroides show that this channel is not important for proton conduction but reveal modulation of the properties of heme a. Biochemistry. 39:2000;2989-2996.
    • (2000) Biochemistry , vol.39 , pp. 2989-2996
    • Lee, H.-M.1    Das, T.K.2    Rousseau, D.L.3    Mills, D.A.4    Ferguson-Miller, S.5    Gennis, R.B.6
  • 196
    • 0034640504 scopus 로고    scopus 로고
    • Proton pumping by cytochrome oxidase: Progress, problems and postulates
    • Zaslavsky D., Gennis R.B. Proton pumping by cytochrome oxidase: progress, problems and postulates. Biochim. Biophys. Acta. 1458:2000;164-179.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 164-179
    • Zaslavsky, D.1    Gennis, R.B.2
  • 197
    • 0037014585 scopus 로고    scopus 로고
    • Plasticity of proton pathways in haem-copper oxygen reductases
    • Pereira M.M., Gomes C.M., Teixeira M. Plasticity of proton pathways in haem-copper oxygen reductases. FEBS Lett. 522:2002;14-18.
    • (2002) FEBS Lett. , vol.522 , pp. 14-18
    • Pereira, M.M.1    Gomes, C.M.2    Teixeira, M.3
  • 199
    • 0037054811 scopus 로고    scopus 로고
    • Relocation of an internal proton donor in cytochrome c oxidase results in an altered pK(a) and a non-integer pumping stoichiometry
    • Gilderson G., Aagaard A., Brzezinski P. Relocation of an internal proton donor in cytochrome c oxidase results in an altered pK(a) and a non-integer pumping stoichiometry. Biophys. Chem. 98:2002;105-114.
    • (2002) Biophys. Chem. , vol.98 , pp. 105-114
    • Gilderson, G.1    Aagaard, A.2    Brzezinski, P.3
  • 200
    • 0030590493 scopus 로고    scopus 로고
    • Fatty acids stimulate activity and restore respiratory control in a proton channel mutant of cytochrome c oxidase
    • Fetter J., Sharpe M., Qian J., Mills D., Ferguson-Miller S., Nicholls P. Fatty acids stimulate activity and restore respiratory control in a proton channel mutant of cytochrome c oxidase. FEBS Lett. 393:1996;155-160.
    • (1996) FEBS Lett. , vol.393 , pp. 155-160
    • Fetter, J.1    Sharpe, M.2    Qian, J.3    Mills, D.4    Ferguson-Miller, S.5    Nicholls, P.6
  • 201
  • 202
    • 0037056047 scopus 로고    scopus 로고
    • Influence of structure, pH, and membrane potential on proton movement in cytochrome c oxidase
    • Mills D.A., Ferguson-Miller S. Influence of structure, pH, and membrane potential on proton movement in cytochrome c oxidase. Biochim. Biophys. Acta. 1555:2002;96-100.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 96-100
    • Mills, D.A.1    Ferguson-Miller, S.2
  • 203
    • 0031004868 scopus 로고    scopus 로고
    • Review. Nuclear genes for cytochrome c oxidase
    • Grossman L.I., Lomax M.I. Review. Nuclear genes for cytochrome c oxidase. Biochim. Biophys. Acta. 1352:1997;174-192.
    • (1997) Biochim. Biophys. Acta , vol.1352 , pp. 174-192
    • Grossman, L.I.1    Lomax, M.I.2
  • 204
    • 0035804655 scopus 로고    scopus 로고
    • Mammalian subunit IV isoforms of cytochrome c oxidase
    • Hüttemann M., Kadenbach B., Grossman L.I. Mammalian subunit IV isoforms of cytochrome c oxidase. Gene. 267:2001;111-123.
    • (2001) Gene , vol.267 , pp. 111-123
    • Hüttemann, M.1    Kadenbach, B.2    Grossman, L.I.3
  • 205
    • 0034113813 scopus 로고    scopus 로고
    • Turkey cytochrome c oxidase contains subunit VIa of the liver-type associated with low efficiency of energy transduction
    • Hüttemann M., Arnold S., Lee I., Mühlenbein N., Linder D., Lottspeich F., Kadenbach B. Turkey cytochrome c oxidase contains subunit VIa of the liver-type associated with low efficiency of energy transduction. Eur. J. Biochem. 267:2000;2098-2104.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2098-2104
    • Hüttemann, M.1    Arnold, S.2    Lee, I.3    Mühlenbein, N.4    Linder, D.5    Lottspeich, F.6    Kadenbach, B.7
  • 206
    • 0033618860 scopus 로고    scopus 로고
    • The possible role of isoforms of cytochrome c oxidase subunit VIa in mammalian thermogenesis
    • Hüttemann M., Frank V., Kadenbach B. The possible role of isoforms of cytochrome c oxidase subunit VIa in mammalian thermogenesis. Cell. Mol. Life Sci. 55:1999;1482-1490.
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 1482-1490
    • Hüttemann, M.1    Frank, V.2    Kadenbach, B.3
  • 207
    • 0027406438 scopus 로고
    • Tissue-specific regulation of bovine heart cytochrome c oxidase by ADP via interaction with subunit VIa
    • Anthony G., Reimann A., Kadenbach B. Tissue-specific regulation of bovine heart cytochrome c oxidase by ADP via interaction with subunit VIa. Proc. Natl. Acad. Sci. U. S. A. 90:1993;1652-1656.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 1652-1656
    • Anthony, G.1    Reimann, A.2    Kadenbach, B.3
  • 208
    • 0027166168 scopus 로고
    • Tissue-specific regulation of cytochrome c oxidase efficiency by nucleotides
    • Rohdich F., Kadenbach B. Tissue-specific regulation of cytochrome c oxidase efficiency by nucleotides. Biochemistry. 32:1993;8499-8503.
    • (1993) Biochemistry , vol.32 , pp. 8499-8503
    • Rohdich, F.1    Kadenbach, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.