메뉴 건너뛰기




Volumn 1793, Issue 1, 2009, Pages 186-199

Mitochondrial ATP synthase disorders: Molecular mechanisms and the quest for curative therapeutic approaches

Author keywords

ATP synthase; Drug screening; Mitochondrial biogenesis; Mitochondrial diseases; NARP and MILS syndromes; Yeast

Indexed keywords

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

EID: 56349168862     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2008.06.012     Document Type: Review
Times cited : (95)

References (178)
  • 1
    • 0033525924 scopus 로고    scopus 로고
    • Oxidative phosphorylation at the fin de siecle
    • Saraste M. Oxidative phosphorylation at the fin de siecle. Science 283 (1999) 1488-1493
    • (1999) Science , vol.283 , pp. 1488-1493
    • Saraste, M.1
  • 2
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase-a splendid molecular machine
    • Boyer P.D. The ATP synthase-a splendid molecular machine. Annu. Rev. Biochem. 66 (1997) 717-749
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 3
    • 0037085010 scopus 로고    scopus 로고
    • The molecular mechanism of ATP synthesis by F1F0-ATP synthase
    • Senior A.E., Nadanaciva S., and Weber J. The molecular mechanism of ATP synthesis by F1F0-ATP synthase. Biochim. Biophys. Acta. 1553 (2002) 188-211
    • (2002) Biochim. Biophys. Acta. , vol.1553 , pp. 188-211
    • Senior, A.E.1    Nadanaciva, S.2    Weber, J.3
  • 6
    • 33644686458 scopus 로고    scopus 로고
    • Function, structure, and biogenesis of mitochondrial ATP synthase
    • Ackerman S.H., and Tzagoloff A. Function, structure, and biogenesis of mitochondrial ATP synthase. Prog. Nucleic Acid Res. Mol. Biol. 80 (2005) 95-133
    • (2005) Prog. Nucleic Acid Res. Mol. Biol. , vol.80 , pp. 95-133
    • Ackerman, S.H.1    Tzagoloff, A.2
  • 11
    • 0027936218 scopus 로고
    • Cytoplasmic transfer of the mtDNA nt 8993 T->G (ATP6) point mutation associated with Leigh syndrome into mtDNA-less cells demonstrates cosegregation with a decrease in state III respiration and ADP/O ratio
    • Trounce I., Neill S., and Wallace D.C. Cytoplasmic transfer of the mtDNA nt 8993 T->G (ATP6) point mutation associated with Leigh syndrome into mtDNA-less cells demonstrates cosegregation with a decrease in state III respiration and ADP/O ratio. Proc. Natl. Acad Sci. U S A 91 (1994) 8334-8338
    • (1994) Proc. Natl. Acad Sci. U S A , vol.91 , pp. 8334-8338
    • Trounce, I.1    Neill, S.2    Wallace, D.C.3
  • 12
    • 0035794142 scopus 로고    scopus 로고
    • Impaired ATP synthase assembly associated with a mutation in the human ATP synthase subunit 6 gene
    • Nijtmans L.G., Henderson N.S., Attardi G., and Holt I.J. Impaired ATP synthase assembly associated with a mutation in the human ATP synthase subunit 6 gene. J. Biol. Chem. 276 (2001) 6755-6762
    • (2001) J. Biol. Chem. , vol.276 , pp. 6755-6762
    • Nijtmans, L.G.1    Henderson, N.S.2    Attardi, G.3    Holt, I.J.4
  • 13
    • 36349036738 scopus 로고    scopus 로고
    • A yeast model of the neurogenic ataxia retinitis pigmentosa (NARP) T8993G mutation in the mitochondrial ATP synthase-6 gene
    • Rak M., Tetaud E., Duvezin-Caubet S., Ezkurdia N., Bietenhader M., Rytka J., and di Rago J.P. A yeast model of the neurogenic ataxia retinitis pigmentosa (NARP) T8993G mutation in the mitochondrial ATP synthase-6 gene. J. Biol. Chem. 282 (2007) 34039-34047
    • (2007) J. Biol. Chem. , vol.282 , pp. 34039-34047
    • Rak, M.1    Tetaud, E.2    Duvezin-Caubet, S.3    Ezkurdia, N.4    Bietenhader, M.5    Rytka, J.6    di Rago, J.P.7
  • 14
    • 0034672534 scopus 로고    scopus 로고
    • The T9176G mutation of human mtDNA gives a fully assembled but inactive ATP synthase when modeled in Escherichia coli
    • Carrozzo R., Murray J., Santorelli F.M., and Capaldi R.A. The T9176G mutation of human mtDNA gives a fully assembled but inactive ATP synthase when modeled in Escherichia coli. FEBS Lett 486 (2000) 297-299
    • (2000) FEBS Lett , vol.486 , pp. 297-299
    • Carrozzo, R.1    Murray, J.2    Santorelli, F.M.3    Capaldi, R.A.4
  • 15
    • 0033581879 scopus 로고    scopus 로고
    • Structural changes linked to proton translocation by subunit c of the ATP synthase
    • Rastogi V.K., and Girvin M.E. Structural changes linked to proton translocation by subunit c of the ATP synthase. Nature 402 (1999) 263-268
    • (1999) Nature , vol.402 , pp. 263-268
    • Rastogi, V.K.1    Girvin, M.E.2
  • 16
    • 27644566520 scopus 로고    scopus 로고
    • The c15 ring of the Spirulina platensis F-ATP synthase: F1/F0 symmetry mismatch is not obligatory
    • Pogoryelov D., Yu J., Meier T., Vonck J., Dimroth P., and Muller D.J. The c15 ring of the Spirulina platensis F-ATP synthase: F1/F0 symmetry mismatch is not obligatory. EMBO Rep 6 (2005) 1040-1044
    • (2005) EMBO Rep , vol.6 , pp. 1040-1044
    • Pogoryelov, D.1    Yu, J.2    Meier, T.3    Vonck, J.4    Dimroth, P.5    Muller, D.J.6
  • 18
    • 33744775373 scopus 로고    scopus 로고
    • The peripheral stalk participates in the yeast ATP synthase dimerization independently of e and g subunits
    • Fronzes R., Weimann T., Vaillier J., Velours J., and Brethes D. The peripheral stalk participates in the yeast ATP synthase dimerization independently of e and g subunits. Biochemistry 45 (2006) 6715-6723
    • (2006) Biochemistry , vol.45 , pp. 6715-6723
    • Fronzes, R.1    Weimann, T.2    Vaillier, J.3    Velours, J.4    Brethes, D.5
  • 19
    • 0038381485 scopus 로고    scopus 로고
    • The molecular neighborhood of subunit 8 of yeast mitochondrial F1F0-ATP synthase probed by cysteine scanning mutagenesis and chemical modification
    • Stephens A.N., Khan M.A., Roucou X., Nagley P., and Devenish R.J. The molecular neighborhood of subunit 8 of yeast mitochondrial F1F0-ATP synthase probed by cysteine scanning mutagenesis and chemical modification. J. Biol. Chem. 278 (2003) 17867-17875
    • (2003) J. Biol. Chem. , vol.278 , pp. 17867-17875
    • Stephens, A.N.1    Khan, M.A.2    Roucou, X.3    Nagley, P.4    Devenish, R.J.5
  • 20
    • 0033766435 scopus 로고    scopus 로고
    • The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution
    • Gibbons C., Montgomery M.G., Leslie A.G., and Walker J.E. The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution. Nat. Struct. Biol. 7 (2000) 1055-1061
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1055-1061
    • Gibbons, C.1    Montgomery, M.G.2    Leslie, A.G.3    Walker, J.E.4
  • 21
    • 0344196918 scopus 로고    scopus 로고
    • Each yeast mitochondrial F1F0-ATP synthase complex contains a single copy of subunit 8
    • Stephens A.N., Nagley P., and Devenish R.J. Each yeast mitochondrial F1F0-ATP synthase complex contains a single copy of subunit 8. Biochim. Biophys. Acta. 1607 (2003) 181-189
    • (2003) Biochim. Biophys. Acta. , vol.1607 , pp. 181-189
    • Stephens, A.N.1    Nagley, P.2    Devenish, R.J.3
  • 22
    • 0032534790 scopus 로고    scopus 로고
    • Yeast mitochondrial F1F0-ATP synthase exists as a dimer: identification of three dimer-specific subunits
    • Arnold I., Pfeiffer K., Neupert W., Stuart R.A., and Schagger H. Yeast mitochondrial F1F0-ATP synthase exists as a dimer: identification of three dimer-specific subunits. EMBO J. 17 (1998) 7170-7178
    • (1998) EMBO J. , vol.17 , pp. 7170-7178
    • Arnold, I.1    Pfeiffer, K.2    Neupert, W.3    Stuart, R.A.4    Schagger, H.5
  • 24
    • 0024392222 scopus 로고
    • An investigation of mitochondrial inner membranes by rapid-freeze deep-etch techniques
    • Allen R.D., Schroeder C.C., and Fok A.K. An investigation of mitochondrial inner membranes by rapid-freeze deep-etch techniques. J. Cell. Biol. 108 (1989) 2233-2240
    • (1989) J. Cell. Biol. , vol.108 , pp. 2233-2240
    • Allen, R.D.1    Schroeder, C.C.2    Fok, A.K.3
  • 25
    • 41949123425 scopus 로고    scopus 로고
    • Dimer ribbons of ATP synthase shape the inner mitochondrial membrane
    • Strauss M., Hofhaus G., Schröder R.R., and Kühlbrandt W. Dimer ribbons of ATP synthase shape the inner mitochondrial membrane. EMBO J 27 (2008) 1154-1160
    • (2008) EMBO J , vol.27 , pp. 1154-1160
    • Strauss, M.1    Hofhaus, G.2    Schröder, R.R.3    Kühlbrandt, W.4
  • 26
    • 0028588948 scopus 로고
    • The regulation of catalysis in ATP synthase
    • Walker J.E. The regulation of catalysis in ATP synthase. Curr. Opin. Struct. Biol. 4 (1994) 912-918
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 912-918
    • Walker, J.E.1
  • 27
    • 0036715421 scopus 로고    scopus 로고
    • ATP synthase of yeast: structural insight into the different inhibitory potencies of two regulatory peptides and identification of a new potential regulator
    • Hong S., and Pedersen P.L. ATP synthase of yeast: structural insight into the different inhibitory potencies of two regulatory peptides and identification of a new potential regulator. Arch. Biochem. Biophys. 405 (2002) 38-43
    • (2002) Arch. Biochem. Biophys. , vol.405 , pp. 38-43
    • Hong, S.1    Pedersen, P.L.2
  • 28
    • 0028114231 scopus 로고
    • Structure at 2.8A resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams J.P., Leslie A.G., Lutter R., and Walker J.E. Structure at 2.8A resolution of F1-ATPase from bovine heart mitochondria. Nature 370 (1994) 621-628
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 29
    • 0030934380 scopus 로고    scopus 로고
    • Direct observation of the rotation of F1-ATPase
    • Noji H., Yasuda R., Yoshida M., and Kinosita Jr. K. Direct observation of the rotation of F1-ATPase. Nature 386 (1997) 299-302
    • (1997) Nature , vol.386 , pp. 299-302
    • Noji, H.1    Yasuda, R.2    Yoshida, M.3    Kinosita Jr., K.4
  • 30
    • 34247877574 scopus 로고    scopus 로고
    • Aqueous access pathways in ATP synthase subunit a. Reactivity of cysteine substituted into transmembrane helices 1, 3, and 5
    • Angevine C.M., Herold K.A., Vincent O.D., and Fillingame R.H. Aqueous access pathways in ATP synthase subunit a. Reactivity of cysteine substituted into transmembrane helices 1, 3, and 5. J. Biol. Chem. 282 (2007) 9001-9007
    • (2007) J. Biol. Chem. , vol.282 , pp. 9001-9007
    • Angevine, C.M.1    Herold, K.A.2    Vincent, O.D.3    Fillingame, R.H.4
  • 31
    • 0034737966 scopus 로고    scopus 로고
    • A model for the structure of subunit a of the Escherichia coli ATP synthase and its role in proton translocation
    • Vik S.B., Long J.C., Wada T., and Zhang D. A model for the structure of subunit a of the Escherichia coli ATP synthase and its role in proton translocation. Biochim. Biophys. Acta. 1458 (2000) 457-466
    • (2000) Biochim. Biophys. Acta. , vol.1458 , pp. 457-466
    • Vik, S.B.1    Long, J.C.2    Wada, T.3    Zhang, D.4
  • 32
    • 0022760932 scopus 로고
    • Two overlapping genes in bovine mitochondrial DNA encode membrane components of ATP synthase
    • Fearnley I.M., and Walker J.E. Two overlapping genes in bovine mitochondrial DNA encode membrane components of ATP synthase. EMBO J. 5 (1986) 2003-2008
    • (1986) EMBO J. , vol.5 , pp. 2003-2008
    • Fearnley, I.M.1    Walker, J.E.2
  • 33
    • 0018890136 scopus 로고
    • Assembly of the mitochondrial membrane system: sequence analysis of a yeast mitochondrial ATPase gene containing the oli-2 and oli-4 loci
    • Macino G., and Tzagoloff A. Assembly of the mitochondrial membrane system: sequence analysis of a yeast mitochondrial ATPase gene containing the oli-2 and oli-4 loci. Cell 20 (1980) 507-517
    • (1980) Cell , vol.20 , pp. 507-517
    • Macino, G.1    Tzagoloff, A.2
  • 35
    • 0018378982 scopus 로고
    • Assembly of the mitochondrial membrane system. The DNA sequence of a mitochondrial ATPase gene in Saccharomyces cerevisiae
    • Macino G., and Tzagoloff A. Assembly of the mitochondrial membrane system. The DNA sequence of a mitochondrial ATPase gene in Saccharomyces cerevisiae. J. Biol. Chem. 254 (1979) 4617-4623
    • (1979) J. Biol. Chem. , vol.254 , pp. 4617-4623
    • Macino, G.1    Tzagoloff, A.2
  • 36
    • 33645011201 scopus 로고    scopus 로고
    • Nuclear control of respiratory gene expression in mammalian cells
    • Scarpulla R.C. Nuclear control of respiratory gene expression in mammalian cells. J. Cell. Biochem. 97 (2006) 673-683
    • (2006) J. Cell. Biochem. , vol.97 , pp. 673-683
    • Scarpulla, R.C.1
  • 38
    • 0030891066 scopus 로고    scopus 로고
    • ATP synthase subunit c expression: physiological regulation of the P1 and P2 genes
    • Andersson U., Houstek J., and Cannon B. ATP synthase subunit c expression: physiological regulation of the P1 and P2 genes. Biochem. J. 323 Pt 2 (1997) 379-385
    • (1997) Biochem. J. , vol.323 , Issue.PART 2 , pp. 379-385
    • Andersson, U.1    Houstek, J.2    Cannon, B.3
  • 39
    • 0030467551 scopus 로고    scopus 로고
    • Translational control of endogenous and recoded nuclear genes in yeast mitochondria: regulation and membrane targeting
    • Fox T.D. Translational control of endogenous and recoded nuclear genes in yeast mitochondria: regulation and membrane targeting. Experientia 52 (1996) 1130-1135
    • (1996) Experientia , vol.52 , pp. 1130-1135
    • Fox, T.D.1
  • 40
    • 0037238395 scopus 로고    scopus 로고
    • Interactions among COX1, COX2, and COX3 mRNA-specific translational activator proteins on the inner surface of the mitochondrial inner membrane of Saccharomyces cerevisiae
    • Naithani S., Saracco S.A., Butler C.A., and Fox T.D. Interactions among COX1, COX2, and COX3 mRNA-specific translational activator proteins on the inner surface of the mitochondrial inner membrane of Saccharomyces cerevisiae,. Mol. Biol. Cell. 14 (2003) 324-333
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 324-333
    • Naithani, S.1    Saracco, S.A.2    Butler, C.A.3    Fox, T.D.4
  • 41
    • 33846573772 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae ATP22 gene codes for the mitochondrial ATPase subunit 6-specific translation factor
    • Zeng X., Hourset A., and Tzagoloff A. The Saccharomyces cerevisiae ATP22 gene codes for the mitochondrial ATPase subunit 6-specific translation factor. Genetics 175 (2007) 55-63
    • (2007) Genetics , vol.175 , pp. 55-63
    • Zeng, X.1    Hourset, A.2    Tzagoloff, A.3
  • 42
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert W., and Herrmann J.M. Translocation of proteins into mitochondria. Annu. Rev. Biochem. 76 (2007) 723-749
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 43
    • 0038487808 scopus 로고    scopus 로고
    • Long mRNAs coding for yeast mitochondrial proteins of prokaryotic origin preferentially localize to the vicinity of mitochondria
    • Sylvestre J., Vialette S., Corral Debrinski M., and Jacq C. Long mRNAs coding for yeast mitochondrial proteins of prokaryotic origin preferentially localize to the vicinity of mitochondria. Genome Biol. 4 (2003) R44
    • (2003) Genome Biol. , vol.4
    • Sylvestre, J.1    Vialette, S.2    Corral Debrinski, M.3    Jacq, C.4
  • 44
    • 23644453428 scopus 로고    scopus 로고
    • Why are many mRNAs translated to the vicinity of mitochondria: a role in protein complex assembly?
    • Margeot A., Garcia M., Wang W., Tetaud E., di Rago J.P., and Jacq C. Why are many mRNAs translated to the vicinity of mitochondria: a role in protein complex assembly?. Gene 354 (2005) 64-71
    • (2005) Gene , vol.354 , pp. 64-71
    • Margeot, A.1    Garcia, M.2    Wang, W.3    Tetaud, E.4    di Rago, J.P.5    Jacq, C.6
  • 45
    • 0031059408 scopus 로고    scopus 로고
    • mRNA encoding the beta-subunit of the mitochondrial F1-ATPase complex is a localized mRNA in rat hepatocytes
    • Egea G., Izquierdo J.M., Ricart J., San Martin C., and Cuezva J.M. mRNA encoding the beta-subunit of the mitochondrial F1-ATPase complex is a localized mRNA in rat hepatocytes. Biochem J. 322 Pt 2 (1997) 557-565
    • (1997) Biochem J. , vol.322 , Issue.PART 2 , pp. 557-565
    • Egea, G.1    Izquierdo, J.M.2    Ricart, J.3    San Martin, C.4    Cuezva, J.M.5
  • 46
    • 0037121931 scopus 로고    scopus 로고
    • In Saccharomyces cerevisiae, ATP2 mRNA sorting to the vicinity of mitochondria is essential for respiratory function
    • Margeot A., Blugeon C., Sylvestre J., Vialette S., Jacq C., and Corral-Debrinski M. In Saccharomyces cerevisiae, ATP2 mRNA sorting to the vicinity of mitochondria is essential for respiratory function. EMBO J 21 (2002) 6893-6904
    • (2002) EMBO J , vol.21 , pp. 6893-6904
    • Margeot, A.1    Blugeon, C.2    Sylvestre, J.3    Vialette, S.4    Jacq, C.5    Corral-Debrinski, M.6
  • 47
    • 54949153170 scopus 로고    scopus 로고
    • Biogenesis and dynamics of mitochondria during the cell cycle: significance of 3′UTRs
    • Martinez-Diez M., Santamaria G., Ortega A.D., and Cuezva J.M. Biogenesis and dynamics of mitochondria during the cell cycle: significance of 3′UTRs. PLoS ONE 1 1 (2006) e107
    • (2006) PLoS ONE , vol.1 , Issue.1
    • Martinez-Diez, M.1    Santamaria, G.2    Ortega, A.D.3    Cuezva, J.M.4
  • 48
    • 9944223330 scopus 로고    scopus 로고
    • Epigenetic regulation of the binding activity of translation inhibitory proteins that bind the 3′ untranslated region of beta-F1-ATPase mRNA by adenine nucleotides and the redox state
    • Izquierdo J.M., and Cuezva J.M. Epigenetic regulation of the binding activity of translation inhibitory proteins that bind the 3′ untranslated region of beta-F1-ATPase mRNA by adenine nucleotides and the redox state. Arch. Biochem. Biophys. 433 (2005) 481-486
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 481-486
    • Izquierdo, J.M.1    Cuezva, J.M.2
  • 49
    • 0034530609 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae ATP synthase
    • Velours J., and Arselin G. The Saccharomyces cerevisiae ATP synthase. J. Bioenerg. Biomembr. 32 (2000) 383-390
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 383-390
    • Velours, J.1    Arselin, G.2
  • 50
    • 0345255615 scopus 로고    scopus 로고
    • The two rotor components of yeast mitochondrial ATP synthase are mechanically coupled by subunit delta
    • Duvezin-Caubet S., Caron M., Giraud M.F., Velours J., and di Rago J.P. The two rotor components of yeast mitochondrial ATP synthase are mechanically coupled by subunit delta. Proc. Natl. Acad Sci. U S A 100 (2003) 13235-13240
    • (2003) Proc. Natl. Acad Sci. U S A , vol.100 , pp. 13235-13240
    • Duvezin-Caubet, S.1    Caron, M.2    Giraud, M.F.3    Velours, J.4    di Rago, J.P.5
  • 51
    • 0024299839 scopus 로고
    • The definition of mitochondrial H+ ATPase assembly defects in mit-mutants of Saccharomyces cerevisiae with a monoclonal antibody to the enzyme complex as an assembly probe
    • Hadikusumo R.G., Meltzer S., Choo W.M., Jean-Francois M.J., Linnane A.W., and Marzuki S. The definition of mitochondrial H+ ATPase assembly defects in mit-mutants of Saccharomyces cerevisiae with a monoclonal antibody to the enzyme complex as an assembly probe. Biochim. Biophys. Acta 933 (1988) 212-222
    • (1988) Biochim. Biophys. Acta , vol.933 , pp. 212-222
    • Hadikusumo, R.G.1    Meltzer, S.2    Choo, W.M.3    Jean-Francois, M.J.4    Linnane, A.W.5    Marzuki, S.6
  • 52
    • 0025350272 scopus 로고
    • Identification of two nuclear genes (ATP11, ATP12) required for assembly of the yeast F1-ATPase
    • Ackerman S.H., and Tzagoloff A. Identification of two nuclear genes (ATP11, ATP12) required for assembly of the yeast F1-ATPase. Proc. Natl. Acad Sci. U S A 87 (1990) 4986-4990
    • (1990) Proc. Natl. Acad Sci. U S A , vol.87 , pp. 4986-4990
    • Ackerman, S.H.1    Tzagoloff, A.2
  • 53
    • 0035794147 scopus 로고    scopus 로고
    • Identification of a nuclear gene (FMC1) required for the assembly/stability of yeast mitochondrial F(1)-ATPase in heat stress conditions
    • Lefebvre-Legendre L., Vaillier J., Benabdelhak H., Velours J., Slonimski P.P., and di Rago J.P. Identification of a nuclear gene (FMC1) required for the assembly/stability of yeast mitochondrial F(1)-ATPase in heat stress conditions. J. Biol. Chem. 276 (2001) 6789-6796
    • (2001) J. Biol. Chem. , vol.276 , pp. 6789-6796
    • Lefebvre-Legendre, L.1    Vaillier, J.2    Benabdelhak, H.3    Velours, J.4    Slonimski, P.P.5    di Rago, J.P.6
  • 54
    • 0035903210 scopus 로고    scopus 로고
    • Atp11p and Atp12p are assembly factors for the F(1)-ATPase in human mitochondria
    • Wang Z.G., White P.S., and Ackerman S.H. Atp11p and Atp12p are assembly factors for the F(1)-ATPase in human mitochondria. J. Biol. Chem. 276 (2001) 30773-30778
    • (2001) J. Biol. Chem. , vol.276 , pp. 30773-30778
    • Wang, Z.G.1    White, P.S.2    Ackerman, S.H.3
  • 55
    • 0037056022 scopus 로고    scopus 로고
    • Atp11p and Atp12p are chaperones for F(1)-ATPase biogenesis in mitochondria
    • Ackerman S.H. Atp11p and Atp12p are chaperones for F(1)-ATPase biogenesis in mitochondria. Biochim. Biophys. Acta 1555 (2002) 101-105
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 101-105
    • Ackerman, S.H.1
  • 56
    • 0034599489 scopus 로고    scopus 로고
    • The alpha-subunit of the mitochondrial F(1) ATPase interacts directly with the assembly factor Atp12p
    • Wang Z.G., Sheluho D., Gatti D.L., and Ackerman S.H. The alpha-subunit of the mitochondrial F(1) ATPase interacts directly with the assembly factor Atp12p. EMBO J. 19 (2000) 1486-1493
    • (2000) EMBO J. , vol.19 , pp. 1486-1493
    • Wang, Z.G.1    Sheluho, D.2    Gatti, D.L.3    Ackerman, S.H.4
  • 57
    • 24044525272 scopus 로고    scopus 로고
    • Failure to assemble the alpha 3 beta 3 subcomplex of the ATP synthase leads to accumulation of the alpha and beta subunits within inclusion bodies and the loss of mitochondrial cristae in Saccharomyces cerevisiae
    • Lefebvre-Legendre L., Salin B., Schaeffer J., Brethes D., Dautant A., Ackerman S.H., and di Rago J.P. Failure to assemble the alpha 3 beta 3 subcomplex of the ATP synthase leads to accumulation of the alpha and beta subunits within inclusion bodies and the loss of mitochondrial cristae in Saccharomyces cerevisiae. J. Biol. Chem. 280 (2005) 18386-18392
    • (2005) J. Biol. Chem. , vol.280 , pp. 18386-18392
    • Lefebvre-Legendre, L.1    Salin, B.2    Schaeffer, J.3    Brethes, D.4    Dautant, A.5    Ackerman, S.H.6    di Rago, J.P.7
  • 58
    • 2442489927 scopus 로고    scopus 로고
    • Atp10p assists assembly of Atp6p into the F0 unit of the yeast mitochondrial ATPase
    • Tzagoloff A., Barrientos A., Neupert W., and Herrmann J.M. Atp10p assists assembly of Atp6p into the F0 unit of the yeast mitochondrial ATPase. J. Biol. Chem. 279 (2004) 19775-19780
    • (2004) J. Biol. Chem. , vol.279 , pp. 19775-19780
    • Tzagoloff, A.1    Barrientos, A.2    Neupert, W.3    Herrmann, J.M.4
  • 59
    • 33846826875 scopus 로고    scopus 로고
    • Prohibitins interact genetically with Atp23, a novel processing peptidase and chaperone for the F1Fo-ATP synthase
    • Osman C., Wilmes C., Tatsuta T., and Langer T. Prohibitins interact genetically with Atp23, a novel processing peptidase and chaperone for the F1Fo-ATP synthase. Mol. Biol. Cell. 18 (2007) 627-635
    • (2007) Mol. Biol. Cell. , vol.18 , pp. 627-635
    • Osman, C.1    Wilmes, C.2    Tatsuta, T.3    Langer, T.4
  • 60
    • 33846813499 scopus 로고    scopus 로고
    • The metalloprotease encoded by ATP23 has a dual function in processing and assembly of subunit 6 of mitochondrial ATPase
    • Zeng X., Neupert W., and Tzagoloff A. The metalloprotease encoded by ATP23 has a dual function in processing and assembly of subunit 6 of mitochondrial ATPase. Mol. Biol. Cell. 18 (2007) 617-626
    • (2007) Mol. Biol. Cell. , vol.18 , pp. 617-626
    • Zeng, X.1    Neupert, W.2    Tzagoloff, A.3
  • 61
    • 44949089613 scopus 로고    scopus 로고
    • ATP25, a new nuclear gene of Saccharomyces cerevisiae required for expression and assembly of theAtp9p subunit of mitochondrial ATPase
    • Zeng X., Barros M.H., Shulman T., and Tzagoloff A. ATP25, a new nuclear gene of Saccharomyces cerevisiae required for expression and assembly of theAtp9p subunit of mitochondrial ATPase. Mol. Biol. Cell. 19 (2008) 1366-1377
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 1366-1377
    • Zeng, X.1    Barros, M.H.2    Shulman, T.3    Tzagoloff, A.4
  • 62
    • 0024287185 scopus 로고
    • NH2-terminal sequence of the isolated yeast ATP synthase subunit 6 reveals post-translational cleavage
    • Michon T., Galante M., and Velours J. NH2-terminal sequence of the isolated yeast ATP synthase subunit 6 reveals post-translational cleavage. Eur J Biochem. 172 (1988) 621-625
    • (1988) Eur J Biochem. , vol.172 , pp. 621-625
    • Michon, T.1    Galante, M.2    Velours, J.3
  • 63
    • 37549038676 scopus 로고    scopus 로고
    • The leader peptide of yeast Atp6p is required for efficient interaction with the Atp9p ring of the mitochondrial ATPase
    • Zeng X., Kucharczyk R., di Rago J.P., and Tzagoloff A. The leader peptide of yeast Atp6p is required for efficient interaction with the Atp9p ring of the mitochondrial ATPase. J. Biol. Chem. 282 (2007) 36167-36176
    • (2007) J. Biol. Chem. , vol.282 , pp. 36167-36176
    • Zeng, X.1    Kucharczyk, R.2    di Rago, J.P.3    Tzagoloff, A.4
  • 66
    • 34548271691 scopus 로고    scopus 로고
    • Pathogenic mitochondrial DNA mutations in protein-coding genes
    • Wong L.J. Pathogenic mitochondrial DNA mutations in protein-coding genes. Muscle Nerve 36 (2007) 279-293
    • (2007) Muscle Nerve , vol.36 , pp. 279-293
    • Wong, L.J.1
  • 68
    • 0025267548 scopus 로고
    • A new mitochondrial disease associated with mitochondrial DNA heteroplasmy
    • Holt I.J., Harding A.E., Petty R.K., and Morgan-Hughes J.A. A new mitochondrial disease associated with mitochondrial DNA heteroplasmy. Am. J. Hum. Genet. 46 (1990) 428-433
    • (1990) Am. J. Hum. Genet. , vol.46 , pp. 428-433
    • Holt, I.J.1    Harding, A.E.2    Petty, R.K.3    Morgan-Hughes, J.A.4
  • 70
    • 0000376151 scopus 로고
    • Subacute necrotizing encephalomyelopathy in an infant
    • Leigh D. Subacute necrotizing encephalomyelopathy in an infant. J. Neurol. Neurosurg. Psychiatry 14 (1951) 216-221
    • (1951) J. Neurol. Neurosurg. Psychiatry , vol.14 , pp. 216-221
    • Leigh, D.1
  • 74
    • 0023136125 scopus 로고
    • Pyruvate dehydrogenase complex deficiency as a cause of subacute necrotizing encephalopathy (Leigh disease)
    • Kretzschmar H.A., DeArmond S.J., Koch T.K., Patel M.S., Newth C.J., Schmidt K.A., and Packman S. Pyruvate dehydrogenase complex deficiency as a cause of subacute necrotizing encephalopathy (Leigh disease). Pediatrics 79 (1987) 370-373
    • (1987) Pediatrics , vol.79 , pp. 370-373
    • Kretzschmar, H.A.1    DeArmond, S.J.2    Koch, T.K.3    Patel, M.S.4    Newth, C.J.5    Schmidt, K.A.6    Packman, S.7
  • 75
    • 0029122341 scopus 로고
    • A novel mitochondrial ATPase 6 point mutation in familial bilateral striatal necrosis
    • Thyagarajan D., Shanske S., Vazquez-Memije M., De Vivo D., and DiMauro S. A novel mitochondrial ATPase 6 point mutation in familial bilateral striatal necrosis. Ann. Neurol. 38 (1995) 468-472
    • (1995) Ann. Neurol. , vol.38 , pp. 468-472
    • Thyagarajan, D.1    Shanske, S.2    Vazquez-Memije, M.3    De Vivo, D.4    DiMauro, S.5
  • 76
    • 0028936818 scopus 로고
    • Correlation between the clinical symptoms and the proportion of mitochondrial DNA carrying the 8993 point mutation in the NARP syndrome
    • Makela-Bengs P., Suomalainen A., Majander A., Rapola J., Kalimo H., Nuutila A., and Pihko H. Correlation between the clinical symptoms and the proportion of mitochondrial DNA carrying the 8993 point mutation in the NARP syndrome. Pediatr. Res. 37 (1995) 634-639
    • (1995) Pediatr. Res. , vol.37 , pp. 634-639
    • Makela-Bengs, P.1    Suomalainen, A.2    Majander, A.3    Rapola, J.4    Kalimo, H.5    Nuutila, A.6    Pihko, H.7
  • 77
    • 0029006067 scopus 로고
    • Altered properties of mitochondrial ATP-synthase in patients with a T->G mutation in the ATPase 6 (subunit a) gene at position 8993 of mtDNA
    • Houstek J., Klement P., Hermanska J., Houstkova H., Hansikova H., Van den Bogert C., and Zeman J. Altered properties of mitochondrial ATP-synthase in patients with a T->G mutation in the ATPase 6 (subunit a) gene at position 8993 of mtDNA. Biochim. Biophys. Acta. 1271 (1995) 349-357
    • (1995) Biochim. Biophys. Acta. , vol.1271 , pp. 349-357
    • Houstek, J.1    Klement, P.2    Hermanska, J.3    Houstkova, H.4    Hansikova, H.5    Van den Bogert, C.6    Zeman, J.7
  • 78
    • 33645576104 scopus 로고    scopus 로고
    • Inefficient coupling between proton transport and ATP synthesis may be the pathogenic mechanism for NARP and Leigh syndrome resulting from the T8993G mutation in mtDNA
    • Sgarbi G., Baracca A., Lenaz G., Valentino L.M., Carelli V., and Solaini G. Inefficient coupling between proton transport and ATP synthesis may be the pathogenic mechanism for NARP and Leigh syndrome resulting from the T8993G mutation in mtDNA. Biochem. J. 395 (2006) 493-500
    • (2006) Biochem. J. , vol.395 , pp. 493-500
    • Sgarbi, G.1    Baracca, A.2    Lenaz, G.3    Valentino, L.M.4    Carelli, V.5    Solaini, G.6
  • 80
    • 33847702960 scopus 로고    scopus 로고
    • ATP6 homoplasmic mutations inhibit and destabilize the human F1F0-ATP synthase without preventing enzyme assembly and oligomerization
    • Cortes-Hernandez P., Vazquez-Memije M.E., and Garcia J.J. ATP6 homoplasmic mutations inhibit and destabilize the human F1F0-ATP synthase without preventing enzyme assembly and oligomerization. J. Biol. Chem. 282 (2007) 1051-1058
    • (2007) J. Biol. Chem. , vol.282 , pp. 1051-1058
    • Cortes-Hernandez, P.1    Vazquez-Memije, M.E.2    Garcia, J.J.3
  • 81
    • 0027244336 scopus 로고
    • The mitochondrial DNA mutation at 8993 associated with NARP slows the rate of ATP synthesis in isolated lymphoblast mitochondria
    • Tatuch Y., and Robinson B.H. The mitochondrial DNA mutation at 8993 associated with NARP slows the rate of ATP synthesis in isolated lymphoblast mitochondria. Biochem Biophys. Res. Commun. 192 (1993) 124-128
    • (1993) Biochem Biophys. Res. Commun. , vol.192 , pp. 124-128
    • Tatuch, Y.1    Robinson, B.H.2
  • 82
    • 0034646642 scopus 로고    scopus 로고
    • Structure, functioning, and assembly of the ATP synthase in cells from patients with the T8993G mitochondrial DNA mutation. Comparison with the enzyme in Rho(0) cells completely lacking mtdna
    • Garcia J.J., Ogilvie I., Robinson B.H., and Capaldi R.A. Structure, functioning, and assembly of the ATP synthase in cells from patients with the T8993G mitochondrial DNA mutation. Comparison with the enzyme in Rho(0) cells completely lacking mtdna. J. Biol. Chem. 275 (2000) 11075-11081
    • (2000) J. Biol. Chem. , vol.275 , pp. 11075-11081
    • Garcia, J.J.1    Ogilvie, I.2    Robinson, B.H.3    Capaldi, R.A.4
  • 83
    • 0034635388 scopus 로고    scopus 로고
    • Catalytic activities of mitochondrial ATP synthase in patients with mitochondrial DNA T8993G mutation in the ATPase 6 gene encoding subunit a
    • Baracca A., Barogi S., Carelli V., Lenaz G., and Solaini G. Catalytic activities of mitochondrial ATP synthase in patients with mitochondrial DNA T8993G mutation in the ATPase 6 gene encoding subunit a. J. Biol. Chem. 275 (2000) 4177-4182
    • (2000) J. Biol. Chem. , vol.275 , pp. 4177-4182
    • Baracca, A.1    Barogi, S.2    Carelli, V.3    Lenaz, G.4    Solaini, G.5
  • 85
    • 0028182912 scopus 로고
    • A T->C mutation at nt 8993 of mitochondrial DNA in a child with Leigh syndrome
    • Santorelli F.M., Shanske S., Jain K.D., Tick D., Schon E.A., and DiMauro S. A T->C mutation at nt 8993 of mitochondrial DNA in a child with Leigh syndrome. Neurology 44 (1994) 972-974
    • (1994) Neurology , vol.44 , pp. 972-974
    • Santorelli, F.M.1    Shanske, S.2    Jain, K.D.3    Tick, D.4    Schon, E.A.5    DiMauro, S.6
  • 93
    • 33847064731 scopus 로고    scopus 로고
    • A previously undescribed leukodystrophy in Leigh syndrome associated with T9176C mutation of the mitochondrial ATPase 6 gene
    • Hung P.C., and Wang H.S. A previously undescribed leukodystrophy in Leigh syndrome associated with T9176C mutation of the mitochondrial ATPase 6 gene. Dev. Med. Child. Neurol. 49 (2007) 65-67
    • (2007) Dev. Med. Child. Neurol. , vol.49 , pp. 65-67
    • Hung, P.C.1    Wang, H.S.2
  • 95
    • 0028810803 scopus 로고
    • Bilateral striatal necrosis with a novel point mutation in the mitochondrial ATPase 6 gene
    • De Meirleir L., Seneca S., Lissens W., Schoentjes E., and Desprechins B. Bilateral striatal necrosis with a novel point mutation in the mitochondrial ATPase 6 gene. Pediatr. Neurol. 13 (1995) 242-246
    • (1995) Pediatr. Neurol. , vol.13 , pp. 242-246
    • De Meirleir, L.1    Seneca, S.2    Lissens, W.3    Schoentjes, E.4    Desprechins, B.5
  • 96
    • 27144482439 scopus 로고    scopus 로고
    • Two new mutations in the MTATP6 gene associated with Leigh syndrome
    • Moslemi A.R., Darin N., Tulinius M., Oldfors A., and Holme E. Two new mutations in the MTATP6 gene associated with Leigh syndrome. Neuropediatrics 36 (2005) 314-318
    • (2005) Neuropediatrics , vol.36 , pp. 314-318
    • Moslemi, A.R.1    Darin, N.2    Tulinius, M.3    Oldfors, A.4    Holme, E.5
  • 100
    • 9144272333 scopus 로고    scopus 로고
    • Diminished synthesis of subunit a (ATP6) and altered function of ATP synthase and cytochrome c oxidase due to the mtDNA 2bp microdeletion of TA at positions 9205 and 9206
    • Jesina P., Tesarova M., Fornuskova D., Vojtiskova A., Pecina P., Kaplanova V., Hansikova H., Zeman J., and Houstek J. Diminished synthesis of subunit a (ATP6) and altered function of ATP synthase and cytochrome c oxidase due to the mtDNA 2bp microdeletion of TA at positions 9205 and 9206. Biochem. J. 383 (2004) 561-571
    • (2004) Biochem. J. , vol.383 , pp. 561-571
    • Jesina, P.1    Tesarova, M.2    Fornuskova, D.3    Vojtiskova, A.4    Pecina, P.5    Kaplanova, V.6    Hansikova, H.7    Zeman, J.8    Houstek, J.9
  • 102
    • 1242314743 scopus 로고    scopus 로고
    • Functional polypeptides can be synthesized from human mitochondrial transcripts lacking termination codons
    • Chrzanowska-Lightowlers Z.M., Temperley R.J., Smith P.M., Seneca S.H., and Lightowlers R.N. Functional polypeptides can be synthesized from human mitochondrial transcripts lacking termination codons. Biochem. J. 377 (2004) 725-731
    • (2004) Biochem. J. , vol.377 , pp. 725-731
    • Chrzanowska-Lightowlers, Z.M.1    Temperley, R.J.2    Smith, P.M.3    Seneca, S.H.4    Lightowlers, R.N.5
  • 103
    • 0028908634 scopus 로고
    • A mitochondrial mutation at nt 9101 in the ATP synthase 6 gene associated with deficient oxidative phosphorylation in a family with Leber hereditary optic neuroretinopathy
    • Lamminen T., Majander A., Juvonen V., Wikstrom M., Aula P., Nikoskelainen E., and Savontous M.L. A mitochondrial mutation at nt 9101 in the ATP synthase 6 gene associated with deficient oxidative phosphorylation in a family with Leber hereditary optic neuroretinopathy. Am. J. Hum. Genet. 56 (1995) 1238-1240
    • (1995) Am. J. Hum. Genet. , vol.56 , pp. 1238-1240
    • Lamminen, T.1    Majander, A.2    Juvonen, V.3    Wikstrom, M.4    Aula, P.5    Nikoskelainen, E.6    Savontous, M.L.7
  • 107
    • 0026879664 scopus 로고
    • An analysis of the role of coenzyme Q in free radical generation and as an antioxidant
    • Beyer R.E. An analysis of the role of coenzyme Q in free radical generation and as an antioxidant. Biochem. Cell. Biol. 70 (1992) 390-403
    • (1992) Biochem. Cell. Biol. , vol.70 , pp. 390-403
    • Beyer, R.E.1
  • 108
    • 0015363173 scopus 로고
    • The cellular production of hydrogen peroxide
    • Boveris A., Oshino N., and Chance B. The cellular production of hydrogen peroxide. Biochem. J. 128 (1972) 617-630
    • (1972) Biochem. J. , vol.128 , pp. 617-630
    • Boveris, A.1    Oshino, N.2    Chance, B.3
  • 109
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B., Sies H., and Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59 (1979) 527-605
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 110
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • Turrens J.F., and Boveris A. Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem. J. 191 (1980) 421-427
    • (1980) Biochem. J. , vol.191 , pp. 421-427
    • Turrens, J.F.1    Boveris, A.2
  • 111
    • 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., and 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
  • 112
    • 1942453308 scopus 로고    scopus 로고
    • The mtDNA T8993G (NARP) mutation results in an impairment of oxidative phosphorylation that can be improved by antioxidants
    • Mattiazzi M., Vijayvergiya C., Gajewski C.D., DeVivo D.C., Lenaz G., Wiedmann M., and Manfredi G. The mtDNA T8993G (NARP) mutation results in an impairment of oxidative phosphorylation that can be improved by antioxidants. Hum. Mol. Genet. 13 (2004) 869-879
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 869-879
    • Mattiazzi, M.1    Vijayvergiya, C.2    Gajewski, C.D.3    DeVivo, D.C.4    Lenaz, G.5    Wiedmann, M.6    Manfredi, G.7
  • 113
    • 0035872917 scopus 로고    scopus 로고
    • Superoxide-induced massive apoptosis in cultured skin fibroblasts harboring the neurogenic ataxia retinitis pigmentosa (NARP) mutation in the ATPase-6 gene of the mitochondrial DNA
    • Geromel V., Kadhom N., Cebalos-Picot I., Ouari O., Polidori A., Munnich A., Rotig A., and Rustin P. Superoxide-induced massive apoptosis in cultured skin fibroblasts harboring the neurogenic ataxia retinitis pigmentosa (NARP) mutation in the ATPase-6 gene of the mitochondrial DNA. Hum. Mol. Genet. 10 (2001) 1221-1228
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1221-1228
    • Geromel, V.1    Kadhom, N.2    Cebalos-Picot, I.3    Ouari, O.4    Polidori, A.5    Munnich, A.6    Rotig, A.7    Rustin, P.8
  • 114
    • 39949085048 scopus 로고    scopus 로고
    • The mtDNA NARP mutation activates the actin-Nrf2 signaling of antioxidant defenses
    • Dassa E.P., Paupe V., Goncalves S., and Rustin P. The mtDNA NARP mutation activates the actin-Nrf2 signaling of antioxidant defenses. Biochem. Biophys. Res. Commun. 368 (2008) 620-624
    • (2008) Biochem. Biophys. Res. Commun. , vol.368 , pp. 620-624
    • Dassa, E.P.1    Paupe, V.2    Goncalves, S.3    Rustin, P.4
  • 116
    • 33748154507 scopus 로고    scopus 로고
    • Mitochondrial disease activates transcripts of the unfolded protein response and cell cycle and inhibits vesicular secretion and oligodendrocyte-specific transcripts
    • Cortopassi G., Danielson S., Alemi M., Zhan S.S., Tong W., Carelli V., Martinuzzi A., Marzuki S., Majamaa K., and Wong A. Mitochondrial disease activates transcripts of the unfolded protein response and cell cycle and inhibits vesicular secretion and oligodendrocyte-specific transcripts. Mitochondrion 6 (2006) 161-175
    • (2006) Mitochondrion , vol.6 , pp. 161-175
    • Cortopassi, G.1    Danielson, S.2    Alemi, M.3    Zhan, S.S.4    Tong, W.5    Carelli, V.6    Martinuzzi, A.7    Marzuki, S.8    Majamaa, K.9    Wong, A.10
  • 118
    • 33847653346 scopus 로고    scopus 로고
    • CHOP (C/EBP homologous protein) and ASNS (asparagine synthetase) induction in cybrid cells harboring MELAS and NARP mitochondrial DNA mutations
    • Fujita Y., Ito M., Nozawa Y., Yoneda M., Oshida Y., and Tanaka M. CHOP (C/EBP homologous protein) and ASNS (asparagine synthetase) induction in cybrid cells harboring MELAS and NARP mitochondrial DNA mutations. Mitochondrion 7 (2007) 80-88
    • (2007) Mitochondrion , vol.7 , pp. 80-88
    • Fujita, Y.1    Ito, M.2    Nozawa, Y.3    Yoneda, M.4    Oshida, Y.5    Tanaka, M.6
  • 119
    • 33746016268 scopus 로고    scopus 로고
    • Mitochondria: more than just a powerhouse
    • McBride H.M., Neuspiel M., and Wasiak S. Mitochondria: more than just a powerhouse. Curr. Biol. 16 (2006) R551-560
    • (2006) Curr. Biol. , vol.16
    • McBride, H.M.1    Neuspiel, M.2    Wasiak, S.3
  • 120
    • 33745274726 scopus 로고    scopus 로고
    • Mitochondria: dynamic organelles in disease, aging, and development
    • Chan D.C. Mitochondria: dynamic organelles in disease, aging, and development. Cell 125 (2006) 1241-1252
    • (2006) Cell , vol.125 , pp. 1241-1252
    • Chan, D.C.1
  • 127
    • 33646573057 scopus 로고    scopus 로고
    • Ectopic localization of mitochondrial ATP synthase: a target for anti-angiogenesis intervention?
    • Kenan D.J., and Wahl M.L. Ectopic localization of mitochondrial ATP synthase: a target for anti-angiogenesis intervention?. J. Bioenerg. Biomembr. 37 (2005) 461-465
    • (2005) J. Bioenerg. Biomembr. , vol.37 , pp. 461-465
    • Kenan, D.J.1    Wahl, M.L.2
  • 130
    • 12544257800 scopus 로고    scopus 로고
    • An inhibitor of the F1 subunit of ATP synthase (IF1) modulates the activity of angiostatin on the endothelial cell surface
    • Burwick N.R., Wahl M.L., Fang J., Zhong Z., Moser T.L., Li B., Capaldi R.A., Kenan D.J., and Pizzo S.V. An inhibitor of the F1 subunit of ATP synthase (IF1) modulates the activity of angiostatin on the endothelial cell surface. J. Biol. Chem. 280 (2005) 1740-1745
    • (2005) J. Biol. Chem. , vol.280 , pp. 1740-1745
    • Burwick, N.R.1    Wahl, M.L.2    Fang, J.3    Zhong, Z.4    Moser, T.L.5    Li, B.6    Capaldi, R.A.7    Kenan, D.J.8    Pizzo, S.V.9
  • 133
    • 33748089976 scopus 로고    scopus 로고
    • Approaches to the treatment of mitochondrial diseases
    • DiMauro S., Hirano M., and Schon E.A. Approaches to the treatment of mitochondrial diseases. Muscle Nerve 34 (2006) 265-283
    • (2006) Muscle Nerve , vol.34 , pp. 265-283
    • DiMauro, S.1    Hirano, M.2    Schon, E.A.3
  • 134
    • 34250676955 scopus 로고    scopus 로고
    • Mitochondrial diseases: therapeutic approaches
    • DiMauro S., and Mancuso M. Mitochondrial diseases: therapeutic approaches. Biosci. Rep. 27 (2007) 125-137
    • (2007) Biosci. Rep. , vol.27 , pp. 125-137
    • DiMauro, S.1    Mancuso, M.2
  • 135
    • 34547877924 scopus 로고    scopus 로고
    • Mitochondrial medicine: pharmacological targeting of mitochondria in disease
    • Armstrong J.S. Mitochondrial medicine: pharmacological targeting of mitochondria in disease. Br. J. Pharmacol. 151 (2007) 1154-1165
    • (2007) Br. J. Pharmacol. , vol.151 , pp. 1154-1165
    • Armstrong, J.S.1
  • 136
    • 33847071146 scopus 로고    scopus 로고
    • Targeting antioxidants to mitochondria by conjugation to lipophilic cations
    • Murphy M.P., and Smith R.A. Targeting antioxidants to mitochondria by conjugation to lipophilic cations. Annu. Rev. Pharmacol. Toxicol. 47 (2007) 629-656
    • (2007) Annu. Rev. Pharmacol. Toxicol. , vol.47 , pp. 629-656
    • Murphy, M.P.1    Smith, R.A.2
  • 137
    • 29344446328 scopus 로고    scopus 로고
    • Targeting antioxidants to mitochondria: a new therapeutic direction
    • Sheu S.S., Nauduri D., and Anders M.W. Targeting antioxidants to mitochondria: a new therapeutic direction. Biochim. Biophys. Acta. 1762 (2006) 256-265
    • (2006) Biochim. Biophys. Acta. , vol.1762 , pp. 256-265
    • Sheu, S.S.1    Nauduri, D.2    Anders, M.W.3
  • 138
    • 33847618832 scopus 로고    scopus 로고
    • Mitochondrial drug delivery and mitochondrial disease therapy-an approach to liposome-based delivery targeted to mitochondria
    • Yamada Y., Akita H., Kogure K., Kamiya H., and Harashima H. Mitochondrial drug delivery and mitochondrial disease therapy-an approach to liposome-based delivery targeted to mitochondria. Mitochondrion 7 (2007) 63-71
    • (2007) Mitochondrion , vol.7 , pp. 63-71
    • Yamada, Y.1    Akita, H.2    Kogure, K.3    Kamiya, H.4    Harashima, H.5
  • 139
    • 34248175243 scopus 로고    scopus 로고
    • The evidence basis for coenzyme Q therapy in oxidative phosphorylation disease
    • Haas R.H. The evidence basis for coenzyme Q therapy in oxidative phosphorylation disease. Mitochondrion 7 Suppl (2007) S136-145
    • (2007) Mitochondrion , vol.7 SUPPL
    • Haas, R.H.1
  • 140
    • 84865193829 scopus 로고    scopus 로고
    • P. Chinnery, K. Majamaa, D. Turnbull, D. Thorburn, Treatment for mitochondrial disorders, Cochrane Database Syst Rev (2006) CD004426.
    • P. Chinnery, K. Majamaa, D. Turnbull, D. Thorburn, Treatment for mitochondrial disorders, Cochrane Database Syst Rev (2006) CD004426.
  • 141
    • 34250617518 scopus 로고    scopus 로고
    • Experimental strategies towards treating mitochondrial DNA disorders
    • Gardner J.L., Craven L., Turnbull D.M., and Taylor R.W. Experimental strategies towards treating mitochondrial DNA disorders. Biosci Rep. 27 (2007) 139-150
    • (2007) Biosci Rep. , vol.27 , pp. 139-150
    • Gardner, J.L.1    Craven, L.2    Turnbull, D.M.3    Taylor, R.W.4
  • 142
    • 15244354458 scopus 로고    scopus 로고
    • Gene therapy for the treatment of mitochondrial DNA disorders
    • Taylor R.W. Gene therapy for the treatment of mitochondrial DNA disorders. Expert Opin. Biol. Ther. 5 (2005) 183-194
    • (2005) Expert Opin. Biol. Ther. , vol.5 , pp. 183-194
    • Taylor, R.W.1
  • 144
    • 4444334765 scopus 로고    scopus 로고
    • Approaches to mitochondrial gene therapy
    • D'Souza G.G., and Weissig V. Approaches to mitochondrial gene therapy. Curr. Gene Ther. 4 (2004) 317-328
    • (2004) Curr. Gene Ther. , vol.4 , pp. 317-328
    • D'Souza, G.G.1    Weissig, V.2
  • 145
    • 10244252759 scopus 로고    scopus 로고
    • Development of mitochondrial gene replacement therapy
    • Khan S.M., and Bennett Jr. J.P. Development of mitochondrial gene replacement therapy. J. Bioenerg Biomembr 36 (2004) 387-393
    • (2004) J. Bioenerg Biomembr , vol.36 , pp. 387-393
    • Khan, S.M.1    Bennett Jr., J.P.2
  • 146
    • 0022550120 scopus 로고
    • A mitochondrial RNA maturase gene transferred to the yeast nucleus can control mitochondrial mRNA splicing
    • Banroques J., Delahodde A., and Jacq C. A mitochondrial RNA maturase gene transferred to the yeast nucleus can control mitochondrial mRNA splicing. Cell 46 (1986) 837-844
    • (1986) Cell , vol.46 , pp. 837-844
    • Banroques, J.1    Delahodde, A.2    Jacq, C.3
  • 147
    • 0024121557 scopus 로고
    • Assembly of functional proton-translocating ATPase complex in yeast mitochondria with cytoplasmically synthesized subunit 8, a polypeptide normally encoded within the organelle
    • Nagley P., Farrell L.B., Gearing D.P., Nero D., Meltzer S., and Devenish R.J. Assembly of functional proton-translocating ATPase complex in yeast mitochondria with cytoplasmically synthesized subunit 8, a polypeptide normally encoded within the organelle. Proc Natl Acad Sci U S A 85 (1988) 2091-2095
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 2091-2095
    • Nagley, P.1    Farrell, L.B.2    Gearing, D.P.3    Nero, D.4    Meltzer, S.5    Devenish, R.J.6
  • 148
    • 0036544631 scopus 로고    scopus 로고
    • Rescue of a deficiency in ATP synthesis by transfer of MTATP6, a mitochondrial DNA-encoded gene, to the nucleus
    • Manfredi G., Fu J., Ojaimi J., Sadlock J.E., Kwong J.Q., Guy J., and Schon E.A. Rescue of a deficiency in ATP synthesis by transfer of MTATP6, a mitochondrial DNA-encoded gene, to the nucleus. Nat. Genet. 30 (2002) 394-399
    • (2002) Nat. Genet. , vol.30 , pp. 394-399
    • Manfredi, G.1    Fu, J.2    Ojaimi, J.3    Sadlock, J.E.4    Kwong, J.Q.5    Guy, J.6    Schon, E.A.7
  • 150
    • 0036855408 scopus 로고    scopus 로고
    • An algal nucleus-encoded subunit of mitochondrial ATP synthase rescues a defect in the analogous human mitochondrial-encoded subunit
    • Ojaimi J., Pan J., Santra S., Snell W.J., and Schon E.A. An algal nucleus-encoded subunit of mitochondrial ATP synthase rescues a defect in the analogous human mitochondrial-encoded subunit. Mol. Biol. Cell. 13 (2002) 3836-3844
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 3836-3844
    • Ojaimi, J.1    Pan, J.2    Santra, S.3    Snell, W.J.4    Schon, E.A.5
  • 151
    • 16844381561 scopus 로고    scopus 로고
    • Stable transformation of CHO Cells and human NARP cybrids confers oligomycin resistance (oli(r)) following transfer of a mitochondrial DNA-encoded oli(r) ATPase6 gene to the nuclear genome: a model system for mtDNA gene therapy
    • Zullo S.J., Parks W.T., Chloupkova M., Wei B., Weiner H., Fenton W.A., Eisenstadt J.M., and Merril C.R. Stable transformation of CHO Cells and human NARP cybrids confers oligomycin resistance (oli(r)) following transfer of a mitochondrial DNA-encoded oli(r) ATPase6 gene to the nuclear genome: a model system for mtDNA gene therapy. Rejuvenation Res. 8 (2005) 18-28
    • (2005) Rejuvenation Res. , vol.8 , pp. 18-28
    • Zullo, S.J.1    Parks, W.T.2    Chloupkova, M.3    Wei, B.4    Weiner, H.5    Fenton, W.A.6    Eisenstadt, J.M.7    Merril, C.R.8
  • 152
    • 33846226670 scopus 로고    scopus 로고
    • Expression of algal nuclear ATP synthase subunit 6 in human cells results in protein targeting to mitochondria but no assembly into ATP synthase
    • Bokori-Brown M., and Holt I.J. Expression of algal nuclear ATP synthase subunit 6 in human cells results in protein targeting to mitochondria but no assembly into ATP synthase. Rejuvenation Res. 9 (2006) 455-469
    • (2006) Rejuvenation Res. , vol.9 , pp. 455-469
    • Bokori-Brown, M.1    Holt, I.J.2
  • 153
    • 34250676869 scopus 로고    scopus 로고
    • Allotopic mRNA localization to the mitochondrial surface rescues respiratory chain defects in fibroblasts harboring mitochondrial DNA mutations affecting complex I or v subunits
    • Bonnet C., Kaltimbacher V., Ellouze S., Augustin S., Benit P., Forster V., Rustin P., Sahel J.A., and Corral-Debrinski M. Allotopic mRNA localization to the mitochondrial surface rescues respiratory chain defects in fibroblasts harboring mitochondrial DNA mutations affecting complex I or v subunits. Rejuvenation Res. 10 (2007) 127-144
    • (2007) Rejuvenation Res. , vol.10 , pp. 127-144
    • Bonnet, C.1    Kaltimbacher, V.2    Ellouze, S.3    Augustin, S.4    Benit, P.5    Forster, V.6    Rustin, P.7    Sahel, J.A.8    Corral-Debrinski, M.9
  • 154
    • 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
  • 155
    • 20344366079 scopus 로고    scopus 로고
    • Mitochondrial DNA and disease
    • Dimauro S., and Davidzon G. Mitochondrial DNA and disease. Ann. Med. 37 (2005) 222-232
    • (2005) Ann. Med. , vol.37 , pp. 222-232
    • Dimauro, S.1    Davidzon, G.2
  • 157
    • 0031038812 scopus 로고    scopus 로고
    • Selective inhibition of mutant human mitochondrial DNA replication in vitro by peptide nucleic acids
    • Taylor R.W., Chinnery P.F., Turnbull D.M., and Lightowlers R.N. Selective inhibition of mutant human mitochondrial DNA replication in vitro by peptide nucleic acids. Nat Genet 15 (1997) 212-215
    • (1997) Nat Genet , vol.15 , pp. 212-215
    • Taylor, R.W.1    Chinnery, P.F.2    Turnbull, D.M.3    Lightowlers, R.N.4
  • 158
    • 0035339611 scopus 로고    scopus 로고
    • Targeting peptide nucleic acid (PNA) oligomers to mitochondria within cells by conjugation to lipophilic cations: implications for mitochondrial DNA replication, expression and disease
    • Muratovska A., Lightowlers R.N., Taylor R.W., Turnbull D.M., Smith R.A., Wilce J.A., Martin S.W., and Murphy M.P. Targeting peptide nucleic acid (PNA) oligomers to mitochondria within cells by conjugation to lipophilic cations: implications for mitochondrial DNA replication, expression and disease. Nucleic Acids Res 29 (2001) 1852-1863
    • (2001) Nucleic Acids Res , vol.29 , pp. 1852-1863
    • Muratovska, A.1    Lightowlers, R.N.2    Taylor, R.W.3    Turnbull, D.M.4    Smith, R.A.5    Wilce, J.A.6    Martin, S.W.7    Murphy, M.P.8
  • 159
    • 0141792967 scopus 로고    scopus 로고
    • Synthesis of trifunctional PNA-benzophenone derivatives for mitochondrial targeting, selective DNA binding, and photo-cross-linking
    • Ross G.F., Smith P.M., McGregor A., Turnbull D.M., and Lightowlers R.N. Synthesis of trifunctional PNA-benzophenone derivatives for mitochondrial targeting, selective DNA binding, and photo-cross-linking. Bioconjug. Chem. 14 (2003) 962-966
    • (2003) Bioconjug. Chem. , vol.14 , pp. 962-966
    • Ross, G.F.1    Smith, P.M.2    McGregor, A.3    Turnbull, D.M.4    Lightowlers, R.N.5
  • 160
    • 0038722195 scopus 로고    scopus 로고
    • Specific targeting of a DNA-alkylating reagent to mitochondria. Synthesis and characterization of [4-((11aS)-7-methoxy-1,2,3,11a-tetrahydro-5H-pyrrolo[2,1-c][1,4]benzodiaze pin-5-on-8-oxy)butyl]-triphenylphosphonium iodide
    • James A.M., Blaikie F.H., Smith R.A., Lightowlers R.N., Smith P.M., and Murphy M.P. Specific targeting of a DNA-alkylating reagent to mitochondria. Synthesis and characterization of [4-((11aS)-7-methoxy-1,2,3,11a-tetrahydro-5H-pyrrolo[2,1-c][1,4]benzodiaze pin-5-on-8-oxy)butyl]-triphenylphosphonium iodide. Eur. J. Biochem. 270 (2003) 2827-2836
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2827-2836
    • James, A.M.1    Blaikie, F.H.2    Smith, R.A.3    Lightowlers, R.N.4    Smith, P.M.5    Murphy, M.P.6
  • 161
    • 33845916259 scopus 로고    scopus 로고
    • Sequence-specific modification of mitochondrial DNA using a chimeric zinc finger methylase
    • Minczuk M., Papworth M.A., Kolasinska P., Murphy M.P., and Klug A. Sequence-specific modification of mitochondrial DNA using a chimeric zinc finger methylase. Proc. Natl. Acad. Sci. U S A 103 (2006) 19689-19694
    • (2006) Proc. Natl. Acad. Sci. U S A , vol.103 , pp. 19689-19694
    • Minczuk, M.1    Papworth, M.A.2    Kolasinska, P.3    Murphy, M.P.4    Klug, A.5
  • 163
    • 0035894698 scopus 로고    scopus 로고
    • Manipulating mitochondrial DNA heteroplasmy by a mitochondrially targeted restriction endonuclease
    • Srivastava S., and Moraes C.T. Manipulating mitochondrial DNA heteroplasmy by a mitochondrially targeted restriction endonuclease. Hum. Mol. Genet. 10 (2001) 3093-3099
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 3093-3099
    • Srivastava, S.1    Moraes, C.T.2
  • 164
    • 40949145581 scopus 로고    scopus 로고
    • Selective elimination of mutant mitochondrial genomes as therapeutic strategy for the treatment of NARP and MILS syndromes
    • Alexeyev M.F., Venediktova N., Pastukh V., Shokolenko I., Bonilla G., and Wilson G.L. Selective elimination of mutant mitochondrial genomes as therapeutic strategy for the treatment of NARP and MILS syndromes. Gene Ther. 15 (2008) 516-523
    • (2008) Gene Ther. , vol.15 , pp. 516-523
    • Alexeyev, M.F.1    Venediktova, N.2    Pastukh, V.3    Shokolenko, I.4    Bonilla, G.5    Wilson, G.L.6
  • 165
    • 26444545053 scopus 로고    scopus 로고
    • Rapid directional shift of mitochondrial DNA heteroplasmy in animal tissues by a mitochondrially targeted restriction endonuclease
    • Bayona-Bafaluy M.P., Blits B., Battersby B.J., Shoubridge E.A., and Moraes C.T. Rapid directional shift of mitochondrial DNA heteroplasmy in animal tissues by a mitochondrially targeted restriction endonuclease. Proc. Natl. Acad. Sci. U S A 102 (2005) 14392-14397
    • (2005) Proc. Natl. Acad. Sci. U S A , vol.102 , pp. 14392-14397
    • Bayona-Bafaluy, M.P.1    Blits, B.2    Battersby, B.J.3    Shoubridge, E.A.4    Moraes, C.T.5
  • 166
    • 0001464176 scopus 로고
    • Action de l'acriflavine sur le levures. I. La mutation "petite colonie"
    • Ephrussi B., Hottinguer Y., and Chimenes Y. Action de l'acriflavine sur le levures. I. La mutation "petite colonie". Ann Inst. Pasteur. 76 (1949) 351-367
    • (1949) Ann Inst. Pasteur. , vol.76 , pp. 351-367
    • Ephrussi, B.1    Hottinguer, Y.2    Chimenes, Y.3
  • 167
    • 0025145542 scopus 로고
    • PET genes of Saccharomyces cerevisiae
    • Tzagoloff A., and Dieckmann C.L. PET genes of Saccharomyces cerevisiae. Microbiol. Rev. 54 (1990) 211-225
    • (1990) Microbiol. Rev. , vol.54 , pp. 211-225
    • Tzagoloff, A.1    Dieckmann, C.L.2
  • 169
    • 34147169140 scopus 로고    scopus 로고
    • Genetic transformation of Saccharomyces cerevisiae and Chlamydomonas reinhardtii mitochondria
    • Bonnefoy N., Remacle C., and Fox T.D. Genetic transformation of Saccharomyces cerevisiae and Chlamydomonas reinhardtii mitochondria. Methods. Cell. Biol. 80 (2007) 525-548
    • (2007) Methods. Cell. Biol. , vol.80 , pp. 525-548
    • Bonnefoy, N.1    Remacle, C.2    Fox, T.D.3
  • 171
    • 0034122608 scopus 로고    scopus 로고
    • Maintenance and integrity of the mitochondrial genome: a plethora of nuclear genes in the budding yeast
    • Contamine V., and Picard M. Maintenance and integrity of the mitochondrial genome: a plethora of nuclear genes in the budding yeast. Microbiol. Mol. Biol. Rev. 64 (2000) 281-315
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 281-315
    • Contamine, V.1    Picard, M.2
  • 172
    • 34249722612 scopus 로고    scopus 로고
    • Yeast cells lacking the mitochondrial gene encoding the ATP synthase subunit 6 exhibit a selective loss of complex IV and unusual mitochondrial morphology
    • Rak M., Tetaud E., Godard F., Sagot I., Salin B., Duvezin-Caubet S., Slonimski P.P., Rytka J., and di Rago J.P. Yeast cells lacking the mitochondrial gene encoding the ATP synthase subunit 6 exhibit a selective loss of complex IV and unusual mitochondrial morphology. J. Biol. Chem. 282 (2007) 10853-10864
    • (2007) J. Biol. Chem. , vol.282 , pp. 10853-10864
    • Rak, M.1    Tetaud, E.2    Godard, F.3    Sagot, I.4    Salin, B.5    Duvezin-Caubet, S.6    Slonimski, P.P.7    Rytka, J.8    di Rago, J.P.9
  • 173
    • 0027336812 scopus 로고
    • The aleu207->arg mutation in F1F0-ATP synthase from Escherichia coli. A model for human mitochondrial disease
    • Hartzog P.E., and Cain B.D. The aleu207->arg mutation in F1F0-ATP synthase from Escherichia coli. A model for human mitochondrial disease. J. Biol. Chem. 268 (1993) 12250-12252
    • (1993) J. Biol. Chem. , vol.268 , pp. 12250-12252
    • Hartzog, P.E.1    Cain, B.D.2
  • 175
    • 24744444959 scopus 로고    scopus 로고
    • Increasing mitochondrial substrate-level phosphorylation can rescue respiratory growth of an ATP synthase-deficient yeast
    • Schwimmer C., Lefebvre-Legendre L., Rak M., Devin A., Slonimski P.P., di Rago J.P., and Rigoulet M. Increasing mitochondrial substrate-level phosphorylation can rescue respiratory growth of an ATP synthase-deficient yeast. J. Biol. Chem. 280 (2005) 30751-30759
    • (2005) J. Biol. Chem. , vol.280 , pp. 30751-30759
    • Schwimmer, C.1    Lefebvre-Legendre, L.2    Rak, M.3    Devin, A.4    Slonimski, P.P.5    di Rago, J.P.6    Rigoulet, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.