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Volumn 86, Issue 7, 2010, Pages 667-693

ATP synthase: From single molecule to human bioenergetics

Author keywords

Bioenergetics; Cytoplasts; FoF1; Mitochondria; Molecular motor; Omics

Indexed keywords

ADENOSINE TRIPHOSPHATE; MITOCHONDRIAL DNA; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 77957862465     PISSN: 03862208     EISSN: 13492896     Source Type: Journal    
DOI: 10.2183/pjab.86.667     Document Type: Review
Times cited : (12)

References (118)
  • 1
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemiosmotic type of mechanism
    • Mitchell, P. (1961) Coupling of phosphorylation to electron and hydrogen transfer by a chemiosmotic type of mechanism. Nature 191, 144-148.
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P.1
  • 2
    • 0001728083 scopus 로고
    • Partial resolution of the enzymes catalyzing oxidative phosphorylation. I. Purification and properties of soluble, dinitrophenol-stimulated adenosine triphosphatase
    • Pullman, M.E., Penefsky, H.S., Datta, A. and Racker, E. (1960) Partial resolution of the enzymes catalyzing oxidative phosphorylation. I. Purification and properties of soluble, dinitrophenol-stimulated adenosine triphosphatase. J. Biol. Chem. 235, 3322-3329.
    • (1960) J. Biol. Chem. , vol.235 , pp. 3322-3329
    • Pullman, M.E.1    Penefsky, H.S.2    Datta, A.3    Racker, E.4
  • 3
    • 0015493839 scopus 로고
    • Reconstitution of oxidative phosphorylation
    • Kagawa, Y. (1972) Reconstitution of oxidative phosphorylation. Biochim. Biophys. Acta 265, 297-338.
    • (1972) Biochim. Biophys. Acta , vol.265 , pp. 297-338
    • Kagawa, Y.1
  • 4
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase-a splendid molecular machine
    • Boyer, P.D. (1997) The ATP synthase-a splendid molecular machine. Annu. Rev. Biochem. 66, 717-749.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 6
    • 0019025914 scopus 로고
    • Nucleotide binding to isolated alpha and beta subunits of proton-translocating adenosine triphosphatase with circular dichroism
    • Ohta, S., Tsuboi, M., Oshima, T., Yoshida, M. and Kagawa, Y. (1980) Nucleotide binding to isolated alpha and beta subunits of proton-translocating adenosine triphosphatase with circular dichroism. J. Biochem. 87, 1609-1617.
    • (1980) J. Biochem. , vol.87 , pp. 1609-1617
    • Ohta, S.1    Tsuboi, M.2    Oshima, T.3    Yoshida, M.4    Kagawa, Y.5
  • 7
    • 0032819656 scopus 로고    scopus 로고
    • Biophysical studies on ATP synthase
    • Kagawa, Y. (1999) Biophysical studies on ATP synthase. Adv. Biophys. 36, 1-25.
    • (1999) Adv. Biophys. , vol.36 , pp. 1-25
    • Kagawa, Y.1
  • 8
    • 20444462741 scopus 로고    scopus 로고
    • 1-ATPase with functional complementation in yeast Saccharomyces cerevisiae
    • 1-ATPase with functional complementation in yeast Saccharomyces cerevisiae. J. Biol. Chem. 280, 22418-22424.
    • (2005) J. Biol. Chem. , vol.280 , pp. 22418-22424
    • Puri, N.1    Lai-Zhang, J.2    Meier, S.3    Mueller, D.M.4
  • 10
    • 0029807877 scopus 로고    scopus 로고
    • 3 oligomer fixed by OSCP-b stator via the (DELSEED sequence
    • 3 oligomer fixed by OSCP-b stator via the (DELSEED sequence. J. Bioenerg. Biomembr. 28, 421-431.
    • (1996) J. Bioenerg. Biomembr. , vol.28 , pp. 421-431
    • Kagawa, Y.1    Hamamoto, T.2
  • 14
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock, D., Leslie, A.G.W. and Walker, J.E. (1999) Molecular architecture of the rotary motor in ATP synthase. Science 286, 1700-1705.
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.W.2    Walker, J.E.3
  • 18
    • 0024354291 scopus 로고
    • +-ATPase): results by combined biochemical and molecular biological approaches
    • +-ATPase): results by combined biochemical and molecular biological approaches. Annu. Rev. Biochem. 58, 111-136.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 111-136
    • Futai, M.1    Noumi, T.2    Maeda, M.3
  • 19
    • 0022803186 scopus 로고
    • Stable structure of thermophilic proton ATPase beta subunit
    • Kagawa, Y., Ishizuka, M., Saishu, T. and Nakao, S. (1986) Stable structure of thermophilic proton ATPase beta subunit. J. Biochem. 100, 923-934.
    • (1986) J. Biochem. , vol.100 , pp. 923-934
    • Kagawa, Y.1    Ishizuka, M.2    Saishu, T.3    Nakao, S.4
  • 20
    • 0024299835 scopus 로고
    • Site-directed mutagenesis of stable adenosine triphosphate synthase
    • Yohda, M., Ohta, S., Hisabori, T. and Kagawa, Y. (1988) Site-directed mutagenesis of stable adenosine triphosphate synthase. Biochim. Biophys. Acta 933, 156-164.
    • (1988) Biochim. Biophys. Acta , vol.933 , pp. 156-164
    • Yohda, M.1    Ohta, S.2    Hisabori, T.3    Kagawa, Y.4
  • 22
    • 2642608683 scopus 로고    scopus 로고
    • Nuclear-recessive mutations of factors involved in mitochondrial translation are responsible for age-related respiration deficiency of human skin fibroblasts
    • Isobe, K., Ito, S., Hosaka, H., Iwamura, Y., Kondo, H., Kagawa, Y. et al. (1998) Nuclear-recessive mutations of factors involved in mitochondrial translation are responsible for age-related respiration deficiency of human skin fibroblasts. J. Biol. Chem. 273, 4601-4606.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4601-4606
    • Isobe, K.1    Ito, S.2    Hosaka, H.3    Iwamura, Y.4    Kondo, H.5    Kagawa, Y.6
  • 23
    • 18444418534 scopus 로고    scopus 로고
    • Single nucleotide polymorphism of thrifty genes for energy metabolism: evolutionary origins and prospects for intervention to prevent obesityrelated diseases
    • Kagawa, Y., Yanagisawa, Y., Hasegawa, K., Suzuki, H., Yasuda, K., Kudo, H. et al. (2002) Single nucleotide polymorphism of thrifty genes for energy metabolism: evolutionary origins and prospects for intervention to prevent obesityrelated diseases. Biochem. Biophys. Res. Commun. 295, 207-222.
    • (2002) Biochem. Biophys. Res. Commun. , vol.295 , pp. 207-222
    • Kagawa, Y.1    Yanagisawa, Y.2    Hasegawa, K.3    Suzuki, H.4    Yasuda, K.5    Kudo, H.6
  • 25
    • 33745713048 scopus 로고    scopus 로고
    • The peripheral stalk of the mitochondrial ATP synthase
    • Walker, J.E. and Dickson, V.K. (2006) The peripheral stalk of the mitochondrial ATP synthase. Biochim. Biophys. Acta 1757, 286-296.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 286-296
    • Walker, J.E.1    Dickson, V.K.2
  • 27
    • 0027428777 scopus 로고
    • Gene structure of human mitochondrial ATP synthase gamma-subunit Tissue specificity produced by alternative RNA splicing
    • Matsuda, C., Endo, H., Ohta, S. and Kagawa, Y. (1993) Gene structure of human mitochondrial ATP synthase gamma-subunit. Tissue specificity produced by alternative RNA splicing. J. Biol. Chem. 268, 24950-24958.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24950-24958
    • Matsuda, C.1    Endo, H.2    Ohta, S.3    Kagawa, Y.4
  • 28
    • 0023762184 scopus 로고
    • Gene structure of the human mitochondrial adenosine triphosphate synthase beta subunit
    • Ohta, S., Tomura, H., Matsuda, K. and Kagawa, Y. (1988) Gene structure of the human mitochondrial adenosine triphosphate synthase beta subunit. J. Biol. Chem. 263, 11257-11262.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11257-11262
    • Ohta, S.1    Tomura, H.2    Matsuda, K.3    Kagawa, Y.4
  • 31
    • 3843147327 scopus 로고    scopus 로고
    • Mitochondrial ATP synthasome: three-dimensional structure by electron microscopy of the ATP synthase in complex formation with carriers for Pi and ADP/ATP
    • Chen, C., Ko, Y., Delannoy, M., Ludtke, S.J., Chiu, W. and Pedersen, P.L. (2004) Mitochondrial ATP synthasome: three-dimensional structure by electron microscopy of the ATP synthase in complex formation with carriers for Pi and ADP/ATP. J. Biol. Chem. 279, 31761-31768.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31761-31768
    • Chen, C.1    Ko, Y.2    Delannoy, M.3    Ludtke, S.J.4    Chiu, W.5    Pedersen, P.L.6
  • 32
    • 0034717310 scopus 로고    scopus 로고
    • Differential regulation of exonic regulatory elements for muscle-specific alternative splicing during myogenesis and cardiogenesis
    • Ichida, M., Hakamata, Y., Hayakawa, M., Ueno, E., Ikeda, U., Shimada, K. et al. (2000) Differential regulation of exonic regulatory elements for muscle-specific alternative splicing during myogenesis and cardiogenesis. J. Biol. Chem. 275, 15992-16001.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15992-16001
    • Ichida, M.1    Hakamata, Y.2    Hayakawa, M.3    Ueno, E.4    Ikeda, U.5    Shimada, K.6
  • 33
    • 0028216544 scopus 로고
    • Nuclear but not mitochondrial genome involvement in human age-related mitochondrial dysfunction Functional integrity of mitochondrial DNA from aged subjects
    • Hayashi, J., Ohta, S., Kagawa, Y., Kondo, H., Kaneda, H., Yonekawa, H. et al. (1994) Nuclear but not mitochondrial genome involvement in human age-related mitochondrial dysfunction. Functional integrity of mitochondrial DNA from aged subjects. J. Biol. Chem. 269, 6878-6883.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6878-6883
    • Hayashi, J.1    Ohta, S.2    Kagawa, Y.3    Kondo, H.4    Kaneda, H.5    Yonekawa, H.6
  • 34
    • 0003310658 scopus 로고
    • Studies of the electron transfer system XLVII. The role of phospholipids in electron transfer
    • Fleischer, S., Brierley, G., Klouwen, H. and Slautterback, D.B. (1962) Studies of the electron transfer system. XLVII. The role of phospholipids in electron transfer. J. Biol. Chem. 237, 3264-3272.
    • (1962) J. Biol. Chem. , vol.237 , pp. 3264-3272
    • Fleischer, S.1    Brierley, G.2    Klouwen, H.3    Slautterback, D.B.4
  • 35
    • 77957862607 scopus 로고
    • The significance of lipoids in the oxygen consuming activity of tissues 1. The oxygen consuming activity of tissue and the mitochondrial structure
    • Kakiuchi, S. (1927) The significance of lipoids in the oxygen consuming activity of tissues. 1. The oxygen consuming activity of tissue and the mitochondrial structure. J. Biochem. 7, 263-265.
    • (1927) J. Biochem. , vol.7 , pp. 263-265
    • Kakiuchi, S.1
  • 36
    • 77957866548 scopus 로고
    • Ueber die Rolle der Diaphorase in der Wechsel-wirkung zwischen dem Cytochrom b und dem Dehydrasesystem
    • Okunuki, K. (1940) Ueber die Rolle der Diaphorase in der Wechsel-wirkung zwischen dem Cytochrom b und dem Dehydrasesystem. Proc. Imp. Acad. (Tokyo) 16, 144-148.
    • (1940) Proc. Imp. Acad. (Tokyo) , vol.16 , pp. 144-148
    • Okunuki, K.1
  • 37
    • 11244283831 scopus 로고
    • The mitochondrion and biochemical machines
    • Green, D.E. and Hatefi, Y. (1961) The mitochondrion and biochemical machines. Science 133, 13-19.
    • (1961) Science , vol.133 , pp. 13-19
    • Green, D.E.1    Hatefi, Y.2
  • 38
    • 0014008391 scopus 로고
    • The biophysics of lipidic associates I The ternary systems lecithin-bile salt-water. Biochim
    • Small, D.M., Bourges, M.C. and Dervichian, D.G. (1966) The biophysics of lipidic associates I. The ternary systems lecithin-bile salt-water. Biochim. Biophys. Acta 125, 563-581.
    • (1966) Biophys. Acta , vol.125 , pp. 563-581
    • Small, D.M.1    Bourges, M.C.2    Dervichian, D.G.3
  • 39
    • 0001506921 scopus 로고
    • 32Pi-adenosine triphosphate exchange
    • 32Pi-adenosine triphosphate exchange. J. Biol. Chem. 246, 5477-5487.
    • (1971) J. Biol. Chem. , vol.246 , pp. 5477-5487
    • Kagawa, Y.1    Racker, E.2
  • 40
    • 0015935065 scopus 로고
    • Partial resolution of the enzymes catalyzing oxidative phosphorylation XXVI. Specificity of phospholipids required for energy transfer reactions
    • Kagawa, Y., Kandrach, A. and Racker, E. (1973) Partial resolution of the enzymes catalyzing oxidative phosphorylation. XXVI. Specificity of phospholipids required for energy transfer reactions. J. Biol. Chem. 248, 676-684.
    • (1973) J. Biol. Chem. , vol.248 , pp. 676-684
    • Kagawa, Y.1    Kandrach, A.2    Racker, E.3
  • 41
    • 0014027485 scopus 로고
    • Partial resolution of the enzymes catalyzing oxidative phosphorylation VIII. Properties of a factor conferring oligomycin sensitivity on mitochondrial adenosine triphosphatase
    • Kagawa, Y. and Racker, E. (1966) Partial resolution of the enzymes catalyzing oxidative phosphorylation. VIII. Properties of a factor conferring oligomycin sensitivity on mitochondrial adenosine triphosphatase. J. Biol. Chem. 241, 2461-2466.
    • (1966) J. Biol. Chem. , vol.241 , pp. 2461-2466
    • Kagawa, Y.1    Racker, E.2
  • 42
    • 0014027518 scopus 로고
    • Partial resolution of the enzymes catalyzing oxidative phosphorylation IX. Reconstruction of oligomycin-sensitiveadenosine triphosphatase
    • Kagawa, Y. and Racker, E. (1966) Partial resolution of the enzymes catalyzing oxidative phosphorylation. IX. Reconstruction of oligomycin-sensitiveadenosine triphosphatase. J. Biol. Chem. 241, 2467-2474.
    • (1966) J. Biol. Chem. , vol.241 , pp. 2467-2474
    • Kagawa, Y.1    Racker, E.2
  • 43
    • 0014027487 scopus 로고
    • Partial resolution of the enzymes catalyzing oxidative phosphorylation X. Correlation of morphology and function in submitochondrial particles
    • Kagawa, Y. and Racker, E. (1966) Partial resolution of the enzymes catalyzing oxidative phosphorylation. X. Correlation of morphology and function in submitochondrial particles. J. Biol. Chem. 241, 2475-2482.
    • (1966) J. Biol. Chem. , vol.241 , pp. 2475-2482
    • Kagawa, Y.1    Racker, E.2
  • 44
    • 0016747666 scopus 로고
    • A highly stable adenosine triphosphatase from a thermophilic bacterium. Purification, properties and reconstitution
    • Yoshida, M., Sone, N., Hirata, H. and Kagawa, Y. (1975) A highly stable adenosine triphosphatase from a thermophilic bacterium. Purification, properties and reconstitution. J. Biol. Chem. 250, 7910-7916.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7910-7916
    • Yoshida, M.1    Sone, N.2    Hirata, H.3    Kagawa, Y.4
  • 45
    • 0016710768 scopus 로고
    • Purification, properties of a dicyclohexylcarbodiimide-sensitive adenosine triphosphatase from a thermophilic bacterium
    • Sone, N., Yoshida, M., Hirata, H. and Kagawa, Y. (1975) Purification, properties of a dicyclohexylcarbodiimide-sensitive adenosine triphosphatase from a thermophilic bacterium. J. Biol. Chem. 250, 7917-7923.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7917-7923
    • Sone, N.1    Yoshida, M.2    Hirata, H.3    Kagawa, Y.4
  • 46
    • 0017405283 scopus 로고
    • Adenosine triphosphate synthesis by electrochemical proton gradient in vesicles reconstituted from purified adenosine triphosphatase and phospholipids of thermophilic bacterium
    • Sone, N., Yoshida, M., Hirata, H. and Kagawa, Y. (1977) Adenosine triphosphate synthesis by electrochemical proton gradient in vesicles reconstituted from purified adenosine triphosphatase and phospholipids of thermophilic bacterium. J. Biol. Chem. 252, 2956-2960.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2956-2960
    • Sone, N.1    Yoshida, M.2    Hirata, H.3    Kagawa, Y.4
  • 47
    • 0014125846 scopus 로고
    • Acid-base transitions and phosphorylation by chloroplasts
    • Jagendorf, A.T. (1967) Acid-base transitions and phosphorylation by chloroplasts. Fed. Proc. 26, 1361-1369.
    • (1967) Fed. Proc. , vol.26 , pp. 1361-1369
    • Jagendorf, A.T.1
  • 48
    • 0017109063 scopus 로고
    • Membrane-bound ATP synthesis generated by an external electrical field
    • Witt, H.T., Schlodder, E. and Gräber, P. (1976) Membrane-bound ATP synthesis generated by an external electrical field. FEBS Lett. 69, 272-276.
    • (1976) FEBS Lett , vol.69 , pp. 272-276
    • Witt, H.T.1    Schlodder, E.2    Gräber, P.3
  • 49
    • 0017669547 scopus 로고
    • Purified proton conductor in proton translocating adenosine triphosphatase of a thermophilic bacterium
    • Okamoto, H., Sone, N., Hirata, H., Yoshida, M. and Kagawa, Y. (1977) Purified proton conductor in proton translocating adenosine triphosphatase of a thermophilic bacterium. J. Biol. Chem. 252, 6125-6131.
    • (1977) J. Biol. Chem. , vol.252 , pp. 6125-6131
    • Okamoto, H.1    Sone, N.2    Hirata, H.3    Yoshida, M.4    Kagawa, Y.5
  • 52
    • 0019320774 scopus 로고
    • Mitochondrial outer membrane contains a protein producing nonspecific diffusion channels
    • Zalman, L.S., Nikaido, H. and Kagawa, Y. (1980) Mitochondrial outer membrane contains a protein producing nonspecific diffusion channels. J. Biol. Chem. 255, 1771-1774.
    • (1980) J. Biol. Chem. , vol.255 , pp. 1771-1774
    • Zalman, L.S.1    Nikaido, H.2    Kagawa, Y.3
  • 53
    • 0017404152 scopus 로고
    • Reconstitution of adenosine triphosphatase of thermophilic bacterium from purified individual subunits
    • Yoshida, M., Sone, N., Hirata, H. and Kagawa, Y. (1977) Reconstitution of adenosine triphosphatase of thermophilic bacterium from purified individual subunits. J. Biol. Chem. 252, 3480-3485.
    • (1977) J. Biol. Chem. , vol.252 , pp. 3480-3485
    • Yoshida, M.1    Sone, N.2    Hirata, H.3    Kagawa, Y.4
  • 57
    • 0029047825 scopus 로고
    • 1-ATPase shows non-cooperative ATPase activity inherent in a single catalytic site with a Km 70 μM
    • Saika, K. and Yoshida, M. (1995) A minimum catalytic unit of F1-ATPase shows non-cooperative ATPase activity inherent in a single catalytic site with a Km 70 μM. FEBS Lett. 368, 207-210.
    • (1995) FEBS Lett , vol.368 , pp. 207-210
    • Saika, K.1    Yoshida, M.2
  • 61
    • 0022824129 scopus 로고
    • The loose coupling mechanism in molecular machines of living cells
    • Oosawa, F. and Hayashi, S. (1986) The loose coupling mechanism in molecular machines of living cells. Adv. Biophys. 22, 151-183.
    • (1986) Adv. Biophys. , vol.22 , pp. 151-183
    • Oosawa, F.1    Hayashi, S.2
  • 63
    • 34548503612 scopus 로고    scopus 로고
    • 1-ATPase rotates by an asymmetric, sequential mechanism using all three catalytic subunits
    • 1-ATPase rotates by an asymmetric, sequential mechanism using all three catalytic subunits. Nat. Struct. Mol. Biol. 14, 841-846.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 841-846
    • Ariga, T.1    Muneyuki, E.2    Yoshida, M.3
  • 65
    • 77957870234 scopus 로고    scopus 로고
    • Futai, M., Wada, Y. and Kaplan, J.H. (eds.) Wiley-VCH, Germany
    • Futai, M., Wada, Y. and Kaplan, J.H. (eds.) (2004) Handbook of ATPases. Wiley-VCH, Germany. pp. 1-468.
    • (2004) Handbook of ATPases , pp. 1-468
  • 66
    • 0021326794 scopus 로고
    • High guanine plus cytosine content in the third letter of codons of an extreme thermophile DNA sequence of the isopropylmalate dehydrogenase of Thermus thermophilus
    • Kagawa, Y., Nojima, H., Nukiwa, N., Ishizuka, M., Nakajima, T., Yasuhara, T. et al. (1984) High guanine plus cytosine content in the third letter of codons of an extreme thermophile. DNA sequence of the isopropylmalate dehydrogenase of Thermus thermophilus. J. Biol. Chem. 259, 2956-2960.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2956-2960
    • Kagawa, Y.1    Nojima, H.2    Nukiwa, N.3    Ishizuka, M.4    Nakajima, T.5    Yasuhara, T.6
  • 67
    • 0023669076 scopus 로고
    • 3, containing glutamine in place of glutamic acid in positions 190 or 201 assembles with the (andγ subunits to produce inactive complexes
    • 3, containing glutamine in place of glutamic acid in positions 190 or 201 assembles with the (andγ subunits to produce inactive complexes. Biochem. Biophys. Res. Commun. 146, 705-710.
    • (1987) Biochem. Biophys. Res. Commun. , vol.146 , pp. 705-710
    • Ohtsubo, M.1    Yoshida, M.2    Ohta, S.3    Kagawa, Y.4    Yohda, M.5    Date, T.6
  • 72
    • 67650546998 scopus 로고    scopus 로고
    • Structure of the c14 rotor ring of the proton translocating chloroplast ATP synthase
    • Vollmar, M., Schlieper, D., Winn, M., Büchner, C. and Groth, G. (2009) Structure of the c14 rotor ring of the proton translocating chloroplast ATP synthase. J. Biol. Chem. 284, 18228-18235.
    • (2009) J. Biol. Chem. , vol.284 , pp. 18228-18235
    • Vollmar, M.1    Schlieper, D.2    Winn, M.3    Büchner, C.4    Groth, G.5
  • 73
  • 80
    • 51849137794 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer in single enzyme molecules with a quantum dot as donor
    • Galvez, E.M., Zimmermann, B., Rombach-Riegraf, V., Bienert, R. and Gräber, P. (2007) Fluorescence resonance energy transfer in single enzyme molecules with a quantum dot as donor. Eur. Biophys. J. 37, 1367-1371.
    • (2007) Eur. Biophys. J. , vol.37 , pp. 1367-1371
    • Galvez, E.M.1    Zimmermann, B.2    Rombach-Riegraf, V.3    Bienert, R.4    Gräber, P.5
  • 84
    • 0027979086 scopus 로고
    • Gene structure and cell typespecific expression of the human ATP synthase alpha subunit
    • Akiyama, S., Endo, H., Inohara, N., Ohta, S. and Kagawa, Y. (1994) Gene structure and cell typespecific expression of the human ATP synthase alpha subunit. Biochim. Biophys. Acta 1219, 129-140.
    • (1994) Biochim. Biophys. Acta , vol.1219 , pp. 129-140
    • Akiyama, S.1    Endo, H.2    Inohara, N.3    Ohta, S.4    Kagawa, Y.5
  • 85
    • 0025230267 scopus 로고
    • Novel regulatory enhancer in the nuclear gene of the human mitochondrial ATP synthase beta-subunit
    • Tomura, H., Endo, H., Kagawa, Y. and Ohta, S. (1990) Novel regulatory enhancer in the nuclear gene of the human mitochondrial ATP synthase beta-subunit. J. Biol. Chem. 265, 6525-6527.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6525-6527
    • Tomura, H.1    Endo, H.2    Kagawa, Y.3    Ohta, S.4
  • 86
    • 0025195369 scopus 로고
    • Regulation of mitochondrial ATP synthesis in mammalian cells by transcriptional control
    • Kagawa, Y. and Ohta, S. (1990) Regulation of mitochondrial ATP synthesis in mammalian cells by transcriptional control. Int. J. Biochem. 22, 219-229.
    • (1990) Int. J. Biochem. , vol.22 , pp. 219-229
    • Kagawa, Y.1    Ohta, S.2
  • 87
  • 88
    • 75649090482 scopus 로고    scopus 로고
    • Novel role of ATPase subunit c targeting peptide beyond mitochondrial import
    • Vives-Bauza, C., Magrane, J., Andreu, A.L. and Manfredi, G. (2010) Novel role of ATPase subunit c targeting peptide beyond mitochondrial import. Mol. Biol. Cell 21, 131-139.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 131-139
    • Vives-Bauza, C.1    Magrane, J.2    Andreu, A.L.3    Manfredi, G.4
  • 89
    • 57049167019 scopus 로고    scopus 로고
    • Regulation of oxidative phosphorylation, the mitochondrial membrane potential, and their role in human disease
    • Hüttemann, M., Lee, I., Pecinova, A., Pecina, P., Przyklenk, K. and Doan, J.W. (2008) Regulation of oxidative phosphorylation, the mitochondrial membrane potential, and their role in human disease. J. Bioenerg. Biomembr. 40, 445-456.
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 445-456
    • Hüttemann, M.1    Lee, I.2    Pecinova, A.3    Pecina, P.4    Przyklenk, K.5    Doan, J.W.6
  • 90
    • 0036510738 scopus 로고    scopus 로고
    • Muscle-specific exonic splicing silencer for exon exclusion in human ATP synthase gamma-subunit pre-mRNA
    • Hayakawa, M., Sakashita, E., Ueno, E., Tominaga, S., Hamamoto, T., Kagawa, Y. et al. (2002) Muscle-specific exonic splicing silencer for exon exclusion in human ATP synthase gamma-subunit pre-mRNA. J. Biol. Chem. 277, 6974-6984.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6974-6984
    • Hayakawa, M.1    Sakashita, E.2    Ueno, E.3    Tominaga, S.4    Hamamoto, T.5    Kagawa, Y.6
  • 91
    • 67650675654 scopus 로고    scopus 로고
    • Post-translational modifications of ATP synthase in the heart: biology and function
    • Kane, L.A. and Van Eyk, J.E. (2009) Post-translational modifications of ATP synthase in the heart: biology and function. J. Bioenerg. Biomembr. 41, 145-150.
    • (2009) J. Bioenerg. Biomembr. , vol.41 , pp. 145-150
    • Kane, L.A.1    Van Eyk, J.E.2
  • 93
    • 0037147103 scopus 로고    scopus 로고
    • Rates of behavior and aging specified by mitochondrial function during development
    • Dillin, A., Hsu, A.L., Arantes-Oliveira, N., Lehrer-Graiwer, J., Hsin, H., Fraser, A.G. et al. (2002) Rates of behavior and aging specified by mitochondrial function during development. Science 298, 2398-2401.
    • (2002) Science , vol.298 , pp. 2398-2401
    • Dillin, A.1    Hsu, A.L.2    Arantes-Oliveira, N.3    Lehrer-Graiwer, J.4    Hsin, H.5    Fraser, A.G.6
  • 94
    • 0033515075 scopus 로고    scopus 로고
    • Functional integrity of mitochondrial genomes in human platelets and autopsied brain tissues from elderly patients with Alzheimer's disease
    • Ito, S., Ohta, S., Nishimaki, K., Kagawa, Y., Soma, R., Kuno, S.Y. et al. (1999) Functional integrity of mitochondrial genomes in human platelets and autopsied brain tissues from elderly patients with Alzheimer's disease. Proc. Natl. Acad. Sci. USA 95, 2099-2103.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2099-2103
    • Ito, S.1    Ohta, S.2    Nishimaki, K.3    Kagawa, Y.4    Soma, R.5    Kuno, S.Y.6
  • 95
    • 0026770725 scopus 로고
    • Upstream region of a genomic gene for human mitochondrial transcription factor 1
    • Tominaga, K., Akiyama, S., Kagawa, Y. and Ohta, S. (1992) Upstream region of a genomic gene for human mitochondrial transcription factor 1. Biochim. Biophys. Acta 1131, 217-219.
    • (1992) Biochim. Biophys. Acta , vol.1131 , pp. 217-219
    • Tominaga, K.1    Akiyama, S.2    Kagawa, Y.3    Ohta, S.4
  • 97
    • 0031018828 scopus 로고    scopus 로고
    • Gene therapy of mitochondrial diseases using human cytoplasts
    • Kagawa, Y. and Hayashi, J.-I. (1997) Gene therapy of mitochondrial diseases using human cytoplasts. Gene Ther. 4, 6-10.
    • (1997) Gene Ther , vol.4 , pp. 6-10
    • Kagawa, Y.1    Hayashi, J.-I.2
  • 98
    • 0037427529 scopus 로고    scopus 로고
    • Differential sublocalization of the dynamin-related protein OPA1 isoforms in mitochondria
    • Satoh, M., Hamamoto, T., Seo, N., Kagawa, Y. and Endo, H. (2003) Differential sublocalization of the dynamin-related protein OPA1 isoforms in mitochondria. Biochem. Biophys. Res. Commun. 300, 482-493.
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , pp. 482-493
    • Satoh, M.1    Hamamoto, T.2    Seo, N.3    Kagawa, Y.4    Endo, H.5
  • 99
    • 46349087708 scopus 로고    scopus 로고
    • The study of the pathogenic mechanism of mitochondrial diseases provides information on basic bioenergetics
    • Solaini, G., Harris, D.A., Lenaz, G., Sgarbi, G. and Baracca, A. (2008) The study of the pathogenic mechanism of mitochondrial diseases provides information on basic bioenergetics. Biochim. Biophys. Acta 1777, 941-945.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 941-945
    • Solaini, G.1    Harris, D.A.2    Lenaz, G.3    Sgarbi, G.4    Baracca, A.5
  • 100
    • 4444293380 scopus 로고    scopus 로고
    • Accumulation of pathogenic DeltamtDNA induced deafness but not diabetic phenotypes in mito-mice
    • Nakada, K., Sato, A., Sone, H., Kasahara, A., Ikeda, K., Kagawa, Y. et al. (2004) Accumulation of pathogenic DeltamtDNA induced deafness but not diabetic phenotypes in mito-mice. Biochem. Biophys. Res. Commun. 323, 175-184.
    • (2004) Biochem. Biophys. Res. Commun. , vol.323 , pp. 175-184
    • Nakada, K.1    Sato, A.2    Sone, H.3    Kasahara, A.4    Ikeda, K.5    Kagawa, Y.6
  • 101
    • 59649090730 scopus 로고    scopus 로고
    • Potential mechanisms of muscle mitochondrial dysfunction in aging and obesity and cellular consequences
    • Chanséaume, E. and Morio, B. (2009) Potential mechanisms of muscle mitochondrial dysfunction in aging and obesity and cellular consequences. Int. J. Mol. Sci. 10, 306-324.
    • (2009) Int. J. Mol. Sci. , vol.10 , pp. 306-324
    • Chanséaume, E.1    Morio, B.2
  • 103
    • 33845970253 scopus 로고    scopus 로고
    • Mitochondrial functions and estrogen receptor-dependent nuclear translocation of pleiotropic human prohibitin 2
    • Kasashima, K., Ohta, E., Kagawa, Y. and Endo, H. (2006) Mitochondrial functions and estrogen receptor-dependent nuclear translocation of pleiotropic human prohibitin 2. J. Biol. Chem. 281, 36401-36410.
    • (2006) J. Biol. Chem. , vol.281 , pp. 36401-36410
    • Kasashima, K.1    Ohta, E.2    Kagawa, Y.3    Endo, H.4
  • 104
    • 35349015148 scopus 로고    scopus 로고
    • Rows of ATP synthase dimers in native mitochondrial inner membranes
    • Buzhynskyy, N., Sens, P., Prima, V., Sturgis, J.N. and Scheuring, S. (2007) Rows of ATP synthase dimers in native mitochondrial inner membranes. Biophys. J. 93, 2870-2876.
    • (2007) Biophys. J. , vol.93 , pp. 2870-2876
    • Buzhynskyy, N.1    Sens, P.2    Prima, V.3    Sturgis, J.N.4    Scheuring, S.5
  • 106
    • 33749247963 scopus 로고    scopus 로고
    • o ATP synthase: a new paradigm?
    • o ATP synthase: a new paradigm? Ann. Med. 38, 429-438.
    • (2006) Ann. Med. , vol.38 , pp. 429-438
    • Chi, S.L.1    Pizzo, S.V.2
  • 107
    • 34447283107 scopus 로고    scopus 로고
    • +-ATP synthase as a potential molecular target for anti-obesity drugs
    • +-ATP synthase as a potential molecular target for anti-obesity drugs. FEBS Lett. 581, 3405-3409.
    • (2007) FEBS Lett , vol.581 , pp. 3405-3409
    • Arakaki, N.1    Kita, T.2    Shibata, H.3    Higuti, T.4
  • 109
    • 67650976561 scopus 로고    scopus 로고
    • Mitochondrial haplogroups associated with Japanese centenarians, Alzheimer's patients, Parkinson's patients, type 2 diabetic patients and healthy non-obese young males
    • Takasaki, S. (2009) Mitochondrial haplogroups associated with Japanese centenarians, Alzheimer's patients, Parkinson's patients, type 2 diabetic patients and healthy non-obese young males. J. Genet. Genomics 36, 425-434.
    • (2009) J. Genet. Genomics , vol.36 , pp. 425-434
    • Takasaki, S.1
  • 110
    • 66649084619 scopus 로고    scopus 로고
    • Short-term exercise training does not stimulate skeletal muscle ATP synthesis in relatives of humans with type 2 diabetes
    • Kacerovsky-Bielesz, G., Chmelik, M., Ling, C., Pokan, R., Szendroedi, J., Farukuoye, M. et al. (2009) Short-term exercise training does not stimulate skeletal muscle ATP synthesis in relatives of humans with type 2 diabetes. Diabetes 58, 1333-1341.
    • (2009) Diabetes , vol.58 , pp. 1333-1341
    • Kacerovsky-Bielesz, G.1    Chmelik, M.2    Ling, C.3    Pokan, R.4    Szendroedi, J.5    Farukuoye, M.6
  • 111
    • 33751294565 scopus 로고    scopus 로고
    • Inhibitors of the catalytic domain of mitochondrial ATP synthase
    • Gledhill, J.R. and Walker, J.E. (2006) Inhibitors of the catalytic domain of mitochondrial ATP synthase. Biochem. Soc. Trans. 34, 989-992.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 989-992
    • Gledhill, J.R.1    Walker, J.E.2
  • 112
    • 67650914230 scopus 로고    scopus 로고
    • AMPK in Health and Disease
    • Steinberg, G.R. and Kemp, B.E. (2009) AMPK in Health and Disease. Physiol. Rev. 89, 1025-1078.
    • (2009) Physiol. Rev. , vol.89 , pp. 1025-1078
    • Steinberg, G.R.1    Kemp, B.E.2
  • 113
    • 67650683346 scopus 로고    scopus 로고
    • MitoKATP activity in healthy and ischemic hearts
    • Costa, A.D. and Garlid, K.D. (2009) MitoKATP activity in healthy and ischemic hearts. J. Bioenerg. Biomembr. 41, 123-126.
    • (2009) J. Bioenerg. Biomembr. , vol.41 , pp. 123-126
    • Costa, A.D.1    Garlid, K.D.2
  • 114
    • 67650868959 scopus 로고    scopus 로고
    • Mitochondrial dynamics in mammalian health and disease
    • Liesa, M., Palacín, M. and Zorzan, A. (2009) Mitochondrial dynamics in mammalian health and disease. Physiol. Rev. 89, 799-845.
    • (2009) Physiol. Rev. , vol.89 , pp. 799-845
    • Liesa, M.1    Palacín, M.2    Zorzan, A.3
  • 115
    • 77649244994 scopus 로고    scopus 로고
    • Subjects with early-onset type 2 diabetes show defective activation of the skeletal muscle PGC-1(/mitofusin-2 regulatory pathway in response to physical activity
    • Hernández-Alvarez, M.I., Thabit, H., Burns, N., Shah, S., Brema, I., Hatunic, M. et al. (2009) Subjects with early-onset type 2 diabetes show defective activation of the skeletal muscle PGC-1(/mitofusin-2 regulatory pathway in response to physical activity. Diabetes Care 33, 645-651.
    • (2009) Diabetes Care , vol.33 , pp. 645-651
    • Hernández-Alvarez, M.I.1    Thabit, H.2    Burns, N.3    Shah, S.4    Brema, I.5    Hatunic, M.6
  • 117
    • 57549108331 scopus 로고    scopus 로고
    • ATP synthase and the actions of inhibitors utilized to study its roles in human health, disease, and other scientific areas
    • Hong, S. and Pedersen, P.L. (2008) ATP synthase and the actions of inhibitors utilized to study its roles in human health, disease, and other scientific areas. Microbiol. Mol. Biol. Rev. 72, 590-641.
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 590-641
    • Hong, S.1    Pedersen, P.L.2
  • 118
    • 55849150985 scopus 로고    scopus 로고
    • 0 ATP hydrolase inhibitor BMS-199264 in myocardial ischemia
    • 0 ATP hydrolase inhibitor BMS-199264 in myocardial ischemia. Cardiovasc. Ther. 26, 287-296.
    • (2008) Cardiovasc. Ther. , vol.26 , pp. 287-296
    • Grover, G.J.1    Malm, J.2


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