메뉴 건너뛰기




Volumn 52, Issue 3-4, 2010, Pages 120-130

Thyroid hormone and myocardial mitochondrial biogenesis

Author keywords

Biogenesis; Mitochondria; Myocardial hypertrophy; Signaling pathways; Thyroid hormone

Indexed keywords

CYTOCHROME; LIOTHYRONINE; MITOCHONDRIAL DNA; MITOCHONDRIAL PROTEIN; NUCLEAR PROTEIN; PHOSPHOLIPID; REGULATOR PROTEIN; THYROXINE;

EID: 76849089486     PISSN: 15371891     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.vph.2009.10.008     Document Type: Review
Times cited : (47)

References (97)
  • 1
    • 33947186240 scopus 로고    scopus 로고
    • Effect of chronic contractile activity on SS and IMF mitochondrial apoptotic susceptibility in skeletal muscle
    • Adhihetty P.J., Ljubicic V., and Hood D.A. Effect of chronic contractile activity on SS and IMF mitochondrial apoptotic susceptibility in skeletal muscle. Am. J. Physiol.: Endocrinol. Metab. 292 (2007) E748-E755
    • (2007) Am. J. Physiol.: Endocrinol. Metab. , vol.292
    • Adhihetty, P.J.1    Ljubicic, V.2    Hood, D.A.3
  • 2
    • 3242866272 scopus 로고
    • Association of a protein structure of probable membrane derivation with HeLa cell mitochondrial DNA near its origin of replication
    • Albring M., Griffith J., and Attardi G. Association of a protein structure of probable membrane derivation with HeLa cell mitochondrial DNA near its origin of replication. Proc. Natl. Acad. Sci. U. S. A. 74 (1977) 1348-1352
    • (1977) Proc. Natl. Acad. Sci. U. S. A. , vol.74 , pp. 1348-1352
    • Albring, M.1    Griffith, J.2    Attardi, G.3
  • 4
    • 0025175704 scopus 로고
    • Mitochondrial DNA structure and expression in specialized subtypes of mammalian striated muscle
    • Annex B.H., and Williams R.S. Mitochondrial DNA structure and expression in specialized subtypes of mammalian striated muscle. Mol. Cell. Biol. 10 (1990) 5671-5678
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5671-5678
    • Annex, B.H.1    Williams, R.S.2
  • 6
    • 0035234393 scopus 로고    scopus 로고
    • Triiodothyronine-mediated up-regulation of UCP2 and UCP3 mRNA expression in human skeletal muscle without coordinated induction of mitochondrial respiratory chain genes
    • Barbe P., Larrouy D., Boulanger C., Chevillotte E., Viguerie N., Thalamas C., Trastoy M.O., Roques M., Vidal H., and Langin D. Triiodothyronine-mediated up-regulation of UCP2 and UCP3 mRNA expression in human skeletal muscle without coordinated induction of mitochondrial respiratory chain genes. FASEB J. 15 (2001) 13-15
    • (2001) FASEB J. , vol.15 , pp. 13-15
    • Barbe, P.1    Larrouy, D.2    Boulanger, C.3    Chevillotte, E.4    Viguerie, N.5    Thalamas, C.6    Trastoy, M.O.7    Roques, M.8    Vidal, H.9    Langin, D.10
  • 7
    • 0033933236 scopus 로고    scopus 로고
    • Deactivation of peroxisome proliferator-activated receptor-alpha during cardiac hypertrophic growth
    • Barger P.M., Brandt J.M., Leone T.C., Weinheimer C.J., and Kelly D.P. Deactivation of peroxisome proliferator-activated receptor-alpha during cardiac hypertrophic growth. J. Clin. Invest. 105 (2000) 1723-1730
    • (2000) J. Clin. Invest. , vol.105 , pp. 1723-1730
    • Barger, P.M.1    Brandt, J.M.2    Leone, T.C.3    Weinheimer, C.J.4    Kelly, D.P.5
  • 8
    • 76849087509 scopus 로고    scopus 로고
    • Thyroid hormones and muscle phenotype: involvement of new signaling pathways
    • Bigard A.X., Koulmann N., Bahi L., Sanchez H., and Ventura-Clapier R. Thyroid hormones and muscle phenotype: involvement of new signaling pathways. J. Soc. Biol. 202 (2008) 93-100
    • (2008) J. Soc. Biol. , vol.202 , pp. 93-100
    • Bigard, A.X.1    Koulmann, N.2    Bahi, L.3    Sanchez, H.4    Ventura-Clapier, R.5
  • 10
    • 2442558106 scopus 로고    scopus 로고
    • Protein components of mitochondrial DNA nucleoids in higher eukaryotes
    • Bogenhagen D.F., Wang Y., Shen E.L., and Kobayashi R. Protein components of mitochondrial DNA nucleoids in higher eukaryotes. Mol. Cell Proteomics 2 (2003) 1205-1216
    • (2003) Mol. Cell Proteomics , vol.2 , pp. 1205-1216
    • Bogenhagen, D.F.1    Wang, Y.2    Shen, E.L.3    Kobayashi, R.4
  • 11
    • 0033769441 scopus 로고    scopus 로고
    • Mammalian mitochondrial ribosomal proteins: N-terminal amino acid sequencing, characterization, and identification of corresponding gene sequences
    • Cahill A., and Cunningham C.C. Mammalian mitochondrial ribosomal proteins: N-terminal amino acid sequencing, characterization, and identification of corresponding gene sequences. Electrophoresis 21 (2000) 3420-3426
    • (2000) Electrophoresis , vol.21 , pp. 3420-3426
    • Cahill, A.1    Cunningham, C.C.2
  • 12
    • 0030048586 scopus 로고    scopus 로고
    • Thyromimetic action of the peroxisome proliferators clofibrate, perfluorooctanoic acid, and acetylsalicylic acid includes changes in mRNA levels for certain genes involved in mitochondrial biogenesis
    • Cai Y., Nelson B.D., Li R., Luciakova K., and Depierre J.W. Thyromimetic action of the peroxisome proliferators clofibrate, perfluorooctanoic acid, and acetylsalicylic acid includes changes in mRNA levels for certain genes involved in mitochondrial biogenesis. Arch. Biochem. Biophys. 325 (1996) 107-112
    • (1996) Arch. Biochem. Biophys. , vol.325 , pp. 107-112
    • Cai, Y.1    Nelson, B.D.2    Li, R.3    Luciakova, K.4    Depierre, J.W.5
  • 14
    • 0028173793 scopus 로고
    • V-erb A stimulates quail myoblast differentiation in a T3 independent cell-specific manner
    • Cassar-Malek I., Marchal S., Altabef M., Wrutniak C., Samarut J., and Cabello G. V-erb A stimulates quail myoblast differentiation in a T3 independent cell-specific manner. Oncogene 9 (1994) 2197-2206
    • (1994) Oncogene , vol.9 , pp. 2197-2206
    • Cassar-Malek, I.1    Marchal, S.2    Altabef, M.3    Wrutniak, C.4    Samarut, J.5    Cabello, G.6
  • 15
    • 0022387546 scopus 로고
    • The presence of two mitochondrial DNA topoisomerases in human acute leukemia cells
    • Castora F.J., Lazarus G.M., and Kunes D. The presence of two mitochondrial DNA topoisomerases in human acute leukemia cells. Biochem. Biophys. Res. Commun. 130 (1985) 854-866
    • (1985) Biochem. Biophys. Res. Commun. , vol.130 , pp. 854-866
    • Castora, F.J.1    Lazarus, G.M.2    Kunes, D.3
  • 16
    • 33847766208 scopus 로고    scopus 로고
    • Impact of endurance training on murine spontaneous activity, muscle mitochondrial DNA abundance, gene transcripts, and function
    • Chow L.S., Greenlund L.J., Asmann Y.W., Short K.R., McCrady S.K., Levine J.A., and Nair K.S. Impact of endurance training on murine spontaneous activity, muscle mitochondrial DNA abundance, gene transcripts, and function. J. Appl. Physiol. 102 (2007) 1078-1089
    • (2007) J. Appl. Physiol. , vol.102 , pp. 1078-1089
    • Chow, L.S.1    Greenlund, L.J.2    Asmann, Y.W.3    Short, K.R.4    McCrady, S.K.5    Levine, J.A.6    Nair, K.S.7
  • 18
    • 0027058592 scopus 로고
    • Transcription and replication of animal mitochondrial DNAs
    • Clayton D.A. Transcription and replication of animal mitochondrial DNAs. Int. Rev. Cytol. 141 (1992) 217-232
    • (1992) Int. Rev. Cytol. , vol.141 , pp. 217-232
    • Clayton, D.A.1
  • 19
    • 0032444931 scopus 로고    scopus 로고
    • Thyroid hormone modifies mitochondrial phenotype by increasing protein import without altering degradation
    • Craig E.E., Chesley A., and Hood D.A. Thyroid hormone modifies mitochondrial phenotype by increasing protein import without altering degradation. Am. J. Physiol. 275 (1998) C1508-C1515
    • (1998) Am. J. Physiol. , vol.275
    • Craig, E.E.1    Chesley, A.2    Hood, D.A.3
  • 20
    • 0027412724 scopus 로고
    • Molecular characterization of the transcription termination factor from human mitochondria
    • Daga A., Micol V., Hess D., Aebersold R., and Attardi G. Molecular characterization of the transcription termination factor from human mitochondria. J. Biol. Chem. 268 (1993) 8123-8130
    • (1993) J. Biol. Chem. , vol.268 , pp. 8123-8130
    • Daga, A.1    Micol, V.2    Hess, D.3    Aebersold, R.4    Attardi, G.5
  • 21
    • 0028841899 scopus 로고
    • The mitochondrion as a primary site of action of glucocorticoids: The interaction of the glucocorticoid receptor with mitochondrial DNA sequences showing partial similarity to the nuclear glucocorticoid responsive elements
    • Demonacos C., Djordjevic-Markovic R., Tsawdaroglou N., and Sekeris C.E. The mitochondrion as a primary site of action of glucocorticoids: The interaction of the glucocorticoid receptor with mitochondrial DNA sequences showing partial similarity to the nuclear glucocorticoid responsive elements. J. Steroid Biochem. Mol. Biol. 55 (1995) 43-55
    • (1995) J. Steroid Biochem. Mol. Biol. , vol.55 , pp. 43-55
    • Demonacos, C.1    Djordjevic-Markovic, R.2    Tsawdaroglou, N.3    Sekeris, C.E.4
  • 22
    • 0029974275 scopus 로고    scopus 로고
    • The synthesis of mRNA in isolated mitochondria can be maintained for several hours and is inhibited by high levels of ATP
    • Enriquez J.A., Fernandez-Silva P., Perez-Martos A., Lopez-Perez M.J., and Montoya J. The synthesis of mRNA in isolated mitochondria can be maintained for several hours and is inhibited by high levels of ATP. Eur. J. Biochem. 237 (1996) 601-610
    • (1996) Eur. J. Biochem. , vol.237 , pp. 601-610
    • Enriquez, J.A.1    Fernandez-Silva, P.2    Perez-Martos, A.3    Lopez-Perez, M.J.4    Montoya, J.5
  • 23
    • 0345493790 scopus 로고    scopus 로고
    • Autonomous regulation in mammalian mitochondrial DNA transcription
    • Enriquez J.A., Fernandez-Silva P., and Montoya J. Autonomous regulation in mammalian mitochondrial DNA transcription. Biol. Chem. 380 (1999) 737-747
    • (1999) Biol. Chem. , vol.380 , pp. 737-747
    • Enriquez, J.A.1    Fernandez-Silva, P.2    Montoya, J.3
  • 25
    • 0031048845 scopus 로고    scopus 로고
    • The human mitochondrial transcription termination factor (mTERF) is a multizipper protein but binds to DNA as a monomer, with evidence pointing to intramolecular leucine zipper interactions
    • Fernandez-Silva P., Martinez-Azorin F., Micol V., and Attardi G. The human mitochondrial transcription termination factor (mTERF) is a multizipper protein but binds to DNA as a monomer, with evidence pointing to intramolecular leucine zipper interactions. EMBO J. 16 (1997) 1066-1079
    • (1997) EMBO J. , vol.16 , pp. 1066-1079
    • Fernandez-Silva, P.1    Martinez-Azorin, F.2    Micol, V.3    Attardi, G.4
  • 26
    • 0037252462 scopus 로고    scopus 로고
    • Replication and transcription of mammalian mitochondrial DNA
    • Fernandez-Silva P., Enriquez J.A., and Montoya J. Replication and transcription of mammalian mitochondrial DNA. Exp. Physiol. 88 (2003) 41-56
    • (2003) Exp. Physiol. , vol.88 , pp. 41-56
    • Fernandez-Silva, P.1    Enriquez, J.A.2    Montoya, J.3
  • 27
    • 0026640728 scopus 로고
    • DNA wrapping and bending by a mitochondrial high mobility group-like transcriptional activator protein
    • Fisher R.P., Lisowsky T., Parisi M.A., and Clayton D.A. DNA wrapping and bending by a mitochondrial high mobility group-like transcriptional activator protein. J. Biol. Chem. 267 (1992) 3358-3367
    • (1992) J. Biol. Chem. , vol.267 , pp. 3358-3367
    • Fisher, R.P.1    Lisowsky, T.2    Parisi, M.A.3    Clayton, D.A.4
  • 28
    • 0023259258 scopus 로고
    • Markedly different ATP re-quirements for rRNA synthesis and mtDNA light strand transcription versus mRNA synthesis in isolated human mitochondria
    • Gaines G., Rossi C., and Attardi G. Markedly different ATP re-quirements for rRNA synthesis and mtDNA light strand transcription versus mRNA synthesis in isolated human mitochondria. J. Biol. Chem. 262 (1987) 1907-1915
    • (1987) J. Biol. Chem. , vol.262 , pp. 1907-1915
    • Gaines, G.1    Rossi, C.2    Attardi, G.3
  • 29
    • 0035872767 scopus 로고    scopus 로고
    • Cloning and characterization of human and mouse mitochon-drial elongation factor G, GFM and Gfm, and mapping of GFM to human chromosome 3q25.1-q26.2
    • Gao J., Yu L., Zhang P., Jiang J., Chen J., Peng J., Wei Y., and Zhao S. Cloning and characterization of human and mouse mitochon-drial elongation factor G, GFM and Gfm, and mapping of GFM to human chromosome 3q25.1-q26.2. Genomics 74 (2001) 109-114
    • (2001) Genomics , vol.74 , pp. 109-114
    • Gao, J.1    Yu, L.2    Zhang, P.3    Jiang, J.4    Chen, J.5    Peng, J.6    Wei, Y.7    Zhao, S.8
  • 30
    • 0019495572 scopus 로고
    • Synthesis and turnover of mitochondrial ribonucleic acid in HeLa cells: the mature ribosomal and messenger ribonucleic acid species are metabolically unstable
    • Gelfand R., and Attardi G. Synthesis and turnover of mitochondrial ribonucleic acid in HeLa cells: the mature ribosomal and messenger ribonucleic acid species are metabolically unstable. Mol. Cell. Biol. 1 (1981) 497-511
    • (1981) Mol. Cell. Biol. , vol.1 , pp. 497-511
    • Gelfand, R.1    Attardi, G.2
  • 31
    • 0037459358 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor (PPAR) alpha and PPARbeta/delta, but not PPARgamma, modulate the expression of genes involved in cardiac lipid metabolism
    • Gilde A.J., Van Der Lee K.A., Willemsen P.H., Chinetti G., Van Der Leij F.R., Van Der Vusse G.J., Staels B., and Van Bilsen M. Peroxisome proliferator-activated receptor (PPAR) alpha and PPARbeta/delta, but not PPARgamma, modulate the expression of genes involved in cardiac lipid metabolism. Circ. Res. 92 (2003) 518-524
    • (2003) Circ. Res. , vol.92 , pp. 518-524
    • Gilde, A.J.1    Van Der Lee, K.A.2    Willemsen, P.H.3    Chinetti, G.4    Van Der Leij, F.R.5    Van Der Vusse, G.J.6    Staels, B.7    Van Bilsen, M.8
  • 32
    • 16644371640 scopus 로고    scopus 로고
    • Bioenergetic remodeling of heart mitochondria by thyroid hormone
    • Goldenthal M.J., Weiss H., and Marín-García J. Bioenergetic remodeling of heart mitochondria by thyroid hormone. Mol. Cell. Biochem. 265 (2004) 97-106
    • (2004) Mol. Cell. Biochem. , vol.265 , pp. 97-106
    • Goldenthal, M.J.1    Weiss, H.2    Marín-García, J.3
  • 33
    • 0028936154 scopus 로고
    • Four structurally distinct, non-DNA-binding subunits of human nuclear respiratory factor 2 share a conserved transcriptional activation domain
    • Gugneja S., Virbasius J.V., and Scarpulla R.C. Four structurally distinct, non-DNA-binding subunits of human nuclear respiratory factor 2 share a conserved transcriptional activation domain. Mol. Cell. Biol. 15 (1995) 102-111
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 102-111
    • Gugneja, S.1    Virbasius, J.V.2    Scarpulla, R.C.3
  • 34
    • 0033551701 scopus 로고    scopus 로고
    • Coordinate induction of energy gene expression in tissue of mitochondrial disease patients
    • Heddi A., Stepien G., Benke P.J., and Wallace D.C. Coordinate induction of energy gene expression in tissue of mitochondrial disease patients. J. Biol. Chem. 274 (1999) 22968-22976
    • (1999) J. Biol. Chem. , vol.274 , pp. 22968-22976
    • Heddi, A.1    Stepien, G.2    Benke, P.J.3    Wallace, D.C.4
  • 35
    • 19244383139 scopus 로고    scopus 로고
    • Gene struc-ture of the human mitochondrial outer membrane receptor Tom20 and evolutionary study of its family of processed pseudogenes
    • Hernandez J.M., Giner P., and Hernandez-Yago J. Gene struc-ture of the human mitochondrial outer membrane receptor Tom20 and evolutionary study of its family of processed pseudogenes. Gene 239 (1999) 283-291
    • (1999) Gene , vol.239 , pp. 283-291
    • Hernandez, J.M.1    Giner, P.2    Hernandez-Yago, J.3
  • 36
    • 0029839416 scopus 로고    scopus 로고
    • Thyromimetic mode of action of peroxisome proliferators: activation of 'malic' enzyme gene transcription
    • Hertz R., Nikodem V., Ben-Ishai A., Berman I., and Bar-Tana J. Thyromimetic mode of action of peroxisome proliferators: activation of 'malic' enzyme gene transcription. Biochem. J. 319 (1996) 241-248
    • (1996) Biochem. J. , vol.319 , pp. 241-248
    • Hertz, R.1    Nikodem, V.2    Ben-Ishai, A.3    Berman, I.4    Bar-Tana, J.5
  • 38
    • 67651159365 scopus 로고    scopus 로고
    • Transcriptional control of mitochondrial biogenesis and function
    • Hock M.B., and Kralli A. Transcriptional control of mitochondrial biogenesis and function. Annu. Rev. Physiol. 71 (2009) 177-203
    • (2009) Annu. Rev. Physiol. , vol.71 , pp. 177-203
    • Hock, M.B.1    Kralli, A.2
  • 39
    • 2342429459 scopus 로고    scopus 로고
    • DNA polymerase gamma, the mitochondrial replicase
    • Kaguni L.S. DNA polymerase gamma, the mitochondrial replicase. Annu. Rev. Biochem. 73 (2004) 293-320
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 293-320
    • Kaguni, L.S.1
  • 41
    • 0035416644 scopus 로고    scopus 로고
    • The human mitochondrial ribosomal protein genes: mapping of 54 genes to the chromosomes and implications for human disorders
    • Kenmochi N., Suzuki T., Uechi T., Magoori M., Kuniba M., Higa S., Watanabe K., and Tanaka T. The human mitochondrial ribosomal protein genes: mapping of 54 genes to the chromosomes and implications for human disorders. Genomics 77 (2001) 65-70
    • (2001) Genomics , vol.77 , pp. 65-70
    • Kenmochi, N.1    Suzuki, T.2    Uechi, T.3    Magoori, M.4    Kuniba, M.5    Higa, S.6    Watanabe, K.7    Tanaka, T.8
  • 42
    • 0027300490 scopus 로고
    • Post-transcriptional regulation of the steady-state levels of mitochondrial tRNAs in HeLa cells
    • King M.P., and Attardi G. Post-transcriptional regulation of the steady-state levels of mitochondrial tRNAs in HeLa cells. J. Biol. Chem. 268 (1993) 10228-10237
    • (1993) J. Biol. Chem. , vol.268 , pp. 10228-10237
    • King, M.P.1    Attardi, G.2
  • 43
    • 0037251008 scopus 로고    scopus 로고
    • Cold-induced recruitment of brown adipose tissue thermogenesis
    • Klingenspor M. Cold-induced recruitment of brown adipose tissue thermogenesis. Exp. Physiol. 88 (2003) 141-148
    • (2003) Exp. Physiol. , vol.88 , pp. 141-148
    • Klingenspor, M.1
  • 44
    • 0037144517 scopus 로고    scopus 로고
    • Identification of mammalian mitochondrial translational initiation factor 3 and examination of its role in initiation complex formation with natural mRNAs
    • Koc E.C., and Spremulli L.L. Identification of mammalian mitochondrial translational initiation factor 3 and examination of its role in initiation complex formation with natural mRNAs. J. Biol. Chem. 277 (2002) 35541-35549
    • (2002) J. Biol. Chem. , vol.277 , pp. 35541-35549
    • Koc, E.C.1    Spremulli, L.L.2
  • 45
    • 1542677230 scopus 로고    scopus 로고
    • Twinkle has 5' -> 3' DNA helicase activity and is specifically stimulated by mitochondrial single-stranded DNA-binding protein
    • Korhonen J.A., Gaspari M., and Falkenberg M. Twinkle has 5' -> 3' DNA helicase activity and is specifically stimulated by mitochondrial single-stranded DNA-binding protein. J. Biol. Chem. 278 (2003) 48627-48632
    • (2003) J. Biol. Chem. , vol.278 , pp. 48627-48632
    • Korhonen, J.A.1    Gaspari, M.2    Falkenberg, M.3
  • 46
    • 3242739284 scopus 로고    scopus 로고
    • Reconstitution of a minimal mtDNA replisome in vitro
    • Korhonen J.A., Pham X.H., Pellegrini M., and Falkenberg M. Reconstitution of a minimal mtDNA replisome in vitro. EMBO J. 23 (2004) 2423-2429
    • (2004) EMBO J. , vol.23 , pp. 2423-2429
    • Korhonen, J.A.1    Pham, X.H.2    Pellegrini, M.3    Falkenberg, M.4
  • 49
    • 3242884720 scopus 로고    scopus 로고
    • Organization and dynamics of human mitochondrial DNA
    • Legros F., Malka F., Frachon P., Lombes A., and Rojo M. Organization and dynamics of human mitochondrial DNA. J. Cell Sci. 117 (2004) 2653-2662
    • (2004) J. Cell Sci. , vol.117 , pp. 2653-2662
    • Legros, F.1    Malka, F.2    Frachon, P.3    Lombes, A.4    Rojo, M.5
  • 50
    • 0033580852 scopus 로고    scopus 로고
    • Respiratory uncoupling induces delta-aminolevulinate synthase expression through a nuclear respiratory factor-1-dependent mechanism in HeLa cells
    • Li B., Holloszy J.O., and Semenkovich C.F. Respiratory uncoupling induces delta-aminolevulinate synthase expression through a nuclear respiratory factor-1-dependent mechanism in HeLa cells. J. Biol. Chem. 274 (1999) 17534-17540
    • (1999) J. Biol. Chem. , vol.274 , pp. 17534-17540
    • Li, B.1    Holloszy, J.O.2    Semenkovich, C.F.3
  • 51
    • 0028924425 scopus 로고
    • Cloning and sequence analysis of the cDNA for bovine mitochondrial translational initiation factor 2
    • Ma J., Farwell M.A., Burkhart W.A., and Spremulli L.L. Cloning and sequence analysis of the cDNA for bovine mitochondrial translational initiation factor 2. Biochim. Biophys. Acta 1261 (1995) 321-324
    • (1995) Biochim. Biophys. Acta , vol.1261 , pp. 321-324
    • Ma, J.1    Farwell, M.A.2    Burkhart, W.A.3    Spremulli, L.L.4
  • 52
    • 0027513658 scopus 로고
    • Protein binding to a single termination-associated sequence in the mitochondrial DNA D-loop region
    • Madsen C.S., Ghivizzani S.C., and Hauswirth W.W. Protein binding to a single termination-associated sequence in the mitochondrial DNA D-loop region. Mol. Cell. Biol. 13 (1993) 2162-2171
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2162-2171
    • Madsen, C.S.1    Ghivizzani, S.C.2    Hauswirth, W.W.3
  • 53
    • 0036774412 scopus 로고    scopus 로고
    • Understanding the impact of mitochondrial defects in cardiovascular disease: a review
    • Marín-García J., and Goldenthal M.J. Understanding the impact of mitochondrial defects in cardiovascular disease: a review. J. Card. Fail. 8 (2002) 347-361
    • (2002) J. Card. Fail. , vol.8 , pp. 347-361
    • Marín-García, J.1    Goldenthal, M.J.2
  • 54
    • 0042474390 scopus 로고    scopus 로고
    • Alteration of nucleotide metabolism: a new mechanism for mitochondrial disorders
    • Marti R., Nishigaki Y., Vila M.R., and Hirano M. Alteration of nucleotide metabolism: a new mechanism for mitochondrial disorders. Clin. Chem. Lab. Med. 41 (2003) 845-851
    • (2003) Clin. Chem. Lab. Med. , vol.41 , pp. 845-851
    • Marti, R.1    Nishigaki, Y.2    Vila, M.R.3    Hirano, M.4
  • 56
    • 0032741464 scopus 로고    scopus 로고
    • The preprotein translocase of the outer mitochondrial membrane: receptors and a general import pore
    • Meisinger C., Brix J., Model K., Pfanner N., and Ryan M.T. The preprotein translocase of the outer mitochondrial membrane: receptors and a general import pore. Cell. Mol. Life Sci. 56 (1999) 817-824
    • (1999) Cell. Mol. Life Sci. , vol.56 , pp. 817-824
    • Meisinger, C.1    Brix, J.2    Model, K.3    Pfanner, N.4    Ryan, M.T.5
  • 57
    • 0035313402 scopus 로고    scopus 로고
    • What regulates mitochondrial DNA copy number in animal cells?
    • Moraes C.T. What regulates mitochondrial DNA copy number in animal cells?. Trends Genet. 17 (2001) 199-205
    • (2001) Trends Genet. , vol.17 , pp. 199-205
    • Moraes, C.T.1
  • 58
    • 0023449963 scopus 로고
    • cDNA sequence of a human skeletal muscle ADP/ATP translocator: lack of a leader peptide, divergence from a fibroblast translocator cDNA, and coevolution with mitochondrial DNA genes
    • Neckelmann N., Li K., Wade R.P., Shuster R., and Wallace D.C. cDNA sequence of a human skeletal muscle ADP/ATP translocator: lack of a leader peptide, divergence from a fibroblast translocator cDNA, and coevolution with mitochondrial DNA genes. Proc. Natl. Acad. Sci. U.S.A. 84 (1987) 7580-7584
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 7580-7584
    • Neckelmann, N.1    Li, K.2    Wade, R.P.3    Shuster, R.4    Wallace, D.C.5
  • 59
    • 0029060046 scopus 로고
    • The role of thy-roid hormone and promoter diversity in the regulation of nuclear encoded mitochondrial proteins
    • Nelson B.D., Luciakova K., Li R., and Betina S. The role of thy-roid hormone and promoter diversity in the regulation of nuclear encoded mitochondrial proteins. Biochim. Biophys. Acta 1271 (1995) 85-91
    • (1995) Biochim. Biophys. Acta , vol.1271 , pp. 85-91
    • Nelson, B.D.1    Luciakova, K.2    Li, R.3    Betina, S.4
  • 60
    • 0037029122 scopus 로고    scopus 로고
    • Evolution of a protein-rich mitochondrial ribosome: Implications for human genetic disease
    • O'Brien T.W. Evolution of a protein-rich mitochondrial ribosome: Implications for human genetic disease. Gene 286 (2002) 73-79
    • (2002) Gene , vol.286 , pp. 73-79
    • O'Brien, T.W.1
  • 63
    • 0027979906 scopus 로고
    • Enhanced cytochrome oxidase activity and modification of lipids in heart mitochondria from hyperthyroid rats
    • Paradies G., Ruggiero F.M., Petrosillo G., and Quagliariello E. Enhanced cytochrome oxidase activity and modification of lipids in heart mitochondria from hyperthyroid rats. Biochim. Biophys. Acta 1225 (1994) 165-170
    • (1994) Biochim. Biophys. Acta , vol.1225 , pp. 165-170
    • Paradies, G.1    Ruggiero, F.M.2    Petrosillo, G.3    Quagliariello, E.4
  • 64
    • 0036123951 scopus 로고    scopus 로고
    • The adenine nucleotide translocator: regulation and function during myocardial development and hypertrophy
    • Portman M.A. The adenine nucleotide translocator: regulation and function during myocardial development and hypertrophy. Clin. Exp. Pharmacol. Physiol. 29 (2002) 334-338
    • (2002) Clin. Exp. Pharmacol. Physiol. , vol.29 , pp. 334-338
    • Portman, M.A.1
  • 65
    • 2342481724 scopus 로고    scopus 로고
    • Phospho-rylation of rat mitochondrial transcription termination factor (mTERF) is required for transcription termination but not for binding to DNA
    • Prieto-Martin A., Montoya J., and Martinez-Azorin F. Phospho-rylation of rat mitochondrial transcription termination factor (mTERF) is required for transcription termination but not for binding to DNA. Nucleic Acids Res. 32 (2004) 2059-2068
    • (2004) Nucleic Acids Res. , vol.32 , pp. 2059-2068
    • Prieto-Martin, A.1    Montoya, J.2    Martinez-Azorin, F.3
  • 66
    • 0030587492 scopus 로고    scopus 로고
    • Cloning and characterization of the human mitochondrial DNA polymerase, DNA polymerase gamma
    • Ropp P.A., and Copeland W.C. Cloning and characterization of the human mitochondrial DNA polymerase, DNA polymerase gamma. Genomics 36 (1996) 449-458
    • (1996) Genomics , vol.36 , pp. 449-458
    • Ropp, P.A.1    Copeland, W.C.2
  • 67
    • 0030835513 scopus 로고    scopus 로고
    • Nuclear control of respiratory chain expression in mammalian cells
    • Scarpulla R.C. Nuclear control of respiratory chain expression in mammalian cells. J. Bioenerg. Biomembranes 29 (1997) 109-119
    • (1997) J. Bioenerg. Biomembranes , vol.29 , pp. 109-119
    • Scarpulla, R.C.1
  • 68
    • 0037036115 scopus 로고    scopus 로고
    • Nuclear activators and coactivators in mammalian mitochondrial biogenesis
    • Scarpulla R.C. Nuclear activators and coactivators in mammalian mitochondrial biogenesis. Biochim. Biophys. Acta 1576 (2002) 1-14
    • (2002) Biochim. Biophys. Acta , vol.1576 , pp. 1-14
    • Scarpulla, R.C.1
  • 70
    • 0021874522 scopus 로고
    • Site of synthesis of the pro-teins of mammalian mitochondrial ribosomes. Evidence from cultured bovine cells
    • Schieber G.L., and O'Brien T.W. Site of synthesis of the pro-teins of mammalian mitochondrial ribosomes. Evidence from cultured bovine cells. J. Biol. Chem. 260 (1985) 6367-6372
    • (1985) J. Biol. Chem. , vol.260 , pp. 6367-6372
    • Schieber, G.L.1    O'Brien, T.W.2
  • 71
    • 0033167094 scopus 로고    scopus 로고
    • Expression, purification, and in vitro characterization of the human outer mitochondrial membrane receptor human translocase of the outer mitochondrial membrane 20
    • Schleiff E., Khanna R., Orlicky S., and Vrielink A. Expression, purification, and in vitro characterization of the human outer mitochondrial membrane receptor human translocase of the outer mitochondrial membrane 20. Arch. Biochem. Biophys. 67 (1999) 95-103
    • (1999) Arch. Biochem. Biophys. , vol.67 , pp. 95-103
    • Schleiff, E.1    Khanna, R.2    Orlicky, S.3    Vrielink, A.4
  • 72
    • 0343569843 scopus 로고    scopus 로고
    • Long-chain fatty acid-promoted swelling of mitochondria: further evidence for the protonophoric effect of fatty acids in the inner mitochondrial membrane
    • Schonfeld P., Wieckowski M.R., and Wojtczak L. Long-chain fatty acid-promoted swelling of mitochondria: further evidence for the protonophoric effect of fatty acids in the inner mitochondrial membrane. FEBS Lett. 471 (2000) 108-112
    • (2000) FEBS Lett. , vol.471 , pp. 108-112
    • Schonfeld, P.1    Wieckowski, M.R.2    Wojtczak, L.3
  • 74
    • 0024212359 scopus 로고
    • Oxygen diffusion distance in thyroxine-induced hypertrophic rabbit myocardium
    • Seiden D., Navidad P., and Weiss H.R. Oxygen diffusion distance in thyroxine-induced hypertrophic rabbit myocardium. J. Mol. Cell. Cardiol. 20 (1988) 917-930
    • (1988) J. Mol. Cell. Cardiol. , vol.20 , pp. 917-930
    • Seiden, D.1    Navidad, P.2    Weiss, H.R.3
  • 75
    • 0030920779 scopus 로고    scopus 로고
    • Mitochondrial DNA maintenance in vertebrates
    • Shadel G.S., and Clayton D.A. Mitochondrial DNA maintenance in vertebrates. Ann. Rev. Biochem. 66 (1997) 409-435
    • (1997) Ann. Rev. Biochem. , vol.66 , pp. 409-435
    • Shadel, G.S.1    Clayton, D.A.2
  • 78
    • 0029151579 scopus 로고
    • Human nuclear and mitochondrial Mt element-binding proteins to regulatory regions of the nuclear respiratory genes and to the mitochondrial promoter region
    • Suzuki H., Suzuki S., Kumar S., and Ozawa T. Human nuclear and mitochondrial Mt element-binding proteins to regulatory regions of the nuclear respiratory genes and to the mitochondrial promoter region. Biochem. Biophys. Res. Commun. 213 (1995) 204-210
    • (1995) Biochem. Biophys. Res. Commun. , vol.213 , pp. 204-210
    • Suzuki, H.1    Suzuki, S.2    Kumar, S.3    Ozawa, T.4
  • 79
    • 1942540784 scopus 로고    scopus 로고
    • Mitochondrial ribosomal proteins: candidate genes for mitochondrial disease
    • Sylvester J.E., Fischel-Ghodsian N., Mougey E.B., and O'Brien T.W. Mitochondrial ribosomal proteins: candidate genes for mitochondrial disease. Genet. Med. 6 (2004) 73-80
    • (2004) Genet. Med. , vol.6 , pp. 73-80
    • Sylvester, J.E.1    Fischel-Ghodsian, N.2    Mougey, E.B.3    O'Brien, T.W.4
  • 80
    • 0021983057 scopus 로고
    • Biochemical and morphological study of cardiac hypertrophy. Effect of thyroxin on enzyme activities in the rat myocardium
    • Tanaka T., Morita H., Koide H., Kawamura K., and Takatsu T. Biochemical and morphological study of cardiac hypertrophy. Effect of thyroxin on enzyme activities in the rat myocardium. Basic Res. Cardiol. 80 (1985) 165-174
    • (1985) Basic Res. Cardiol. , vol.80 , pp. 165-174
    • Tanaka, T.1    Morita, H.2    Koide, H.3    Kawamura, K.4    Takatsu, T.5
  • 81
    • 33646124709 scopus 로고    scopus 로고
    • Complementary action of the PGC-1 coactivators in mitochondrial biogenesis and brown fat differentiation
    • Uldry M., Yang W., St-Pierre J., Lin J., Seale P., and Spiegelman B.M. Complementary action of the PGC-1 coactivators in mitochondrial biogenesis and brown fat differentiation. Cell Metab. 3 (2006) 333-341
    • (2006) Cell Metab. , vol.3 , pp. 333-341
    • Uldry, M.1    Yang, W.2    St-Pierre, J.3    Lin, J.4    Seale, P.5    Spiegelman, B.M.6
  • 82
    • 0028011017 scopus 로고
    • Activation of thehuman mitochondrial transcription factor A gene by nuclear respiratory factors: a potential regulatory link between nuclear and mitochondrial gene expression in organelle biogenesis
    • Virbasius J.V., and Scarpulla R.C. Activation of thehuman mitochondrial transcription factor A gene by nuclear respiratory factors: a potential regulatory link between nuclear and mitochondrial gene expression in organelle biogenesis. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 1309-1313
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 1309-1313
    • Virbasius, J.V.1    Scarpulla, R.C.2
  • 84
    • 0037126059 scopus 로고    scopus 로고
    • Dual localization of human DNA topoisomerase III alpha to mitochondria and nucleus
    • Wang Y., Lyu Y.L., and Wang J.C. Dual localization of human DNA topoisomerase III alpha to mitochondria and nucleus. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 12114-12119
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12114-12119
    • Wang, Y.1    Lyu, Y.L.2    Wang, J.C.3
  • 85
    • 0026784329 scopus 로고
    • Regulation by thyroid hormone of nuclear and mitochondrial genes encoding subunits of cytochrome-c oxidase in rat liver and skeletal muscle
    • Wiesner R.J., Kurowski T.T., and Zak R. Regulation by thyroid hormone of nuclear and mitochondrial genes encoding subunits of cytochrome-c oxidase in rat liver and skeletal muscle. Mol. Endocrinol. 6 (1992) 1458-1467
    • (1992) Mol. Endocrinol. , vol.6 , pp. 1458-1467
    • Wiesner, R.J.1    Kurowski, T.T.2    Zak, R.3
  • 86
    • 0028031520 scopus 로고
    • Coordination of nuclear and mitochondrial gene expression during the development of cardiac hypertrophy in rats
    • Wiesner R.J., Aschenbrenner V., Ruegg J.C., and Zak R. Coordination of nuclear and mitochondrial gene expression during the development of cardiac hypertrophy in rats. Am. J. Physiol. 267 (1994) C229-C235
    • (1994) Am. J. Physiol. , vol.267
    • Wiesner, R.J.1    Aschenbrenner, V.2    Ruegg, J.C.3    Zak, R.4
  • 87
    • 0022202524 scopus 로고
    • Isolation and characterization of a DNA primase from human mitochondria
    • Wong T.W., and Clayton D.A. Isolation and characterization of a DNA primase from human mitochondria. J. Biol. Chem. 260 (1985) 11530-11535
    • (1985) J. Biol. Chem. , vol.260 , pp. 11530-11535
    • Wong, T.W.1    Clayton, D.A.2
  • 88
    • 0029562397 scopus 로고
    • Cloning and sequence analysis and expression of mammalian mitochondrial protein synthesis elongation factor Tu
    • Woriax V.L., Burkhart W., and Spremulli L.L. Cloning and sequence analysis and expression of mammalian mitochondrial protein synthesis elongation factor Tu. Biochim. Biophys. Acta 1264 (1995) 347-356
    • (1995) Biochim. Biophys. Acta , vol.1264 , pp. 347-356
    • Woriax, V.L.1    Burkhart, W.2    Spremulli, L.L.3
  • 91
    • 76849115449 scopus 로고    scopus 로고
    • Triiodothyronine mitochondrial receptors: import and molecular mechanisms
    • Wrutniak-Cabello C., Carazo A., Casas F., and Cabello G. Triiodothyronine mitochondrial receptors: import and molecular mechanisms. J. Soc. Biol. 202 (2008) 83-92
    • (2008) J. Soc. Biol. , vol.202 , pp. 83-92
    • Wrutniak-Cabello, C.1    Carazo, A.2    Casas, F.3    Cabello, G.4
  • 93
    • 0029088252 scopus 로고
    • Cloning and expression of mitochondrial translational elongation factor Ts from bovine and human liver
    • Xin H., Woriax V., Burkhart W., and Spremulli L.L. Cloning and expression of mitochondrial translational elongation factor Ts from bovine and human liver. J. Biol. Chem. 270 (1995) 17243-17249
    • (1995) J. Biol. Chem. , vol.270 , pp. 17243-17249
    • Xin, H.1    Woriax, V.2    Burkhart, W.3    Spremulli, L.L.4
  • 94
    • 0029938513 scopus 로고    scopus 로고
    • RNA-DNA hybrid formation at the human mitochondrial heavy-strand origin ceases at replication start sites: an implication for RNA-DNA hybrids serving as primers
    • Xu B., and Clayton D.A. RNA-DNA hybrid formation at the human mitochondrial heavy-strand origin ceases at replication start sites: an implication for RNA-DNA hybrids serving as primers. EMBO J. 15 (1996) 3135-3143
    • (1996) EMBO J. , vol.15 , pp. 3135-3143
    • Xu, B.1    Clayton, D.A.2
  • 95
    • 0035085845 scopus 로고    scopus 로고
    • Uncoupling protein 3 transcription is regulated by peroxisome proliferator-activated receptor (alpha) in the adult rodent heart
    • Young M.E., Patil S., Ying J., Depre C., Ahuja H.S., Shipley G.L., Stepkowski S.M., Davies P.J., and Taegtmeyer H. Uncoupling protein 3 transcription is regulated by peroxisome proliferator-activated receptor (alpha) in the adult rodent heart. FASEB J. 15 (2001) 833-845
    • (2001) FASEB J. , vol.15 , pp. 833-845
    • Young, M.E.1    Patil, S.2    Ying, J.3    Depre, C.4    Ahuja, H.S.5    Shipley, G.L.6    Stepkowski, S.M.7    Davies, P.J.8    Taegtmeyer, H.9
  • 97
    • 0034078708 scopus 로고    scopus 로고
    • Depolarizing stimulation upregulates GA-binding protein in neurons: a transcription factor involved in the bigenomic expression of cytochrome oxidase subunits
    • Zhang C., and Wong-Riley M.T. Depolarizing stimulation upregulates GA-binding protein in neurons: a transcription factor involved in the bigenomic expression of cytochrome oxidase subunits. Eur. J. Neurosci. 12 (2000) 1013-1023
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 1013-1023
    • Zhang, C.1    Wong-Riley, M.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.