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Volumn 35, Issue 1, 2003, Pages 86-94

Mitochondrial biogenesis and the role of the protein import pathway

Author keywords

Exercise; Gene transcription; Heat shock proteins; Mitochondrial disease; Mitochondrial DNA; Skeletal muscle

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 60; MESSENGER RNA; MITOCHONDRIAL DNA;

EID: 0037232726     PISSN: 01959131     EISSN: None     Source Type: Journal    
DOI: 10.1097/00005768-200301000-00015     Document Type: Article
Times cited : (49)

References (75)
  • 1
    • 0027246118 scopus 로고
    • A fatal, systemic mitochondrial disease with decreased mitochondrial enzyme activities, abnormal ultrastructure of the mitochondria and deficiency of heat shock protein 60
    • AGSTERIBBE, E., A. HUCKRIEDE, M. VEENHUIS, et al. A fatal, systemic mitochondrial disease with decreased mitochondrial enzyme activities, abnormal ultrastructure of the mitochondria and deficiency of heat shock protein 60. Biochem. Biophys. Res. Commun. 193:146-154, 1993.
    • (1993) Biochem. Biophys. Res. Commun. , vol.193 , pp. 146-154
    • Agsteribbe, E.1    Huckriede, A.2    Veenhuis, M.3
  • 2
    • 0035665594 scopus 로고    scopus 로고
    • Chronic activation of AMP kinase results in NRF-I activation and mitochondrial biogenesis
    • BERGERON. R., J. M. REN, K. S. CADMAN, et al. Chronic activation of AMP kinase results in NRF-I activation and mitochondrial biogenesis. Am. J. Physiol. 281:E1340-1346, 2001.
    • (2001) Am. J. Physiol. , vol.281
    • Bergeron, R.1    Ren, J.M.2    Cadman, K.S.3
  • 3
    • 0040610676 scopus 로고    scopus 로고
    • Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 i, and Tom70 in a presequence-carrying preprotein and a non-cleavable preprotein
    • BRIX, J., S. RUDIGER, B. BUKAU, J. SCHNEIDER-MERGENER, and N. PFANNER. Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 i, and Tom70 in a presequence-carrying preprotein and a non-cleavable preprotein. J. Biol. Chem. 274:16522-16530, 1999.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16522-16530
    • Brix, J.1    Rudiger, S.2    Bukau, B.3    Schneider-Mergener, J.4    Pfanner, N.5
  • 4
    • 0033965891 scopus 로고    scopus 로고
    • Immunolabelling of mitochondrial superoxide dismutase and of Hsp 60 in muscles harbouring a respiratory chain deficiency
    • CARRIER, H., F. FLOCARD, V. TAGLIATI, A. P. ARRIGO, and C. GODINOT. Immunolabelling of mitochondrial superoxide dismutase and of Hsp60 in muscles harbouring a respiratory chain deficiency. Neuromuscul. Disord. 10:144-149, 2000.
    • (2000) Neuromuscul. Disord. , vol.10 , pp. 144-149
    • Carrier, H.1    Flocard, F.2    Tagliati, V.3    Arrigo, A.P.4    Godinot, C.5
  • 5
    • 0033506827 scopus 로고    scopus 로고
    • A variant of the nuclear triiodothyronine receptor c-Erb Α 1 plays a direct role in regulation of mitochondrial RNA synthesis
    • CASAS, F., P. ROCHARD, A. RODIER, et al. A variant of the nuclear triiodothyronine receptor c-Erb Α 1 plays a direct role in regulation of mitochondrial RNA synthesis. Mol. Cell. Biol. 19:7913-7924, 1999.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7913-7924
    • Casas, F.1    Rochard, P.2    Rodier, A.3
  • 6
    • 0035844172 scopus 로고    scopus 로고
    • Contractile activity-induced transcriptional activation of cytochrome C involves Spl and is proportional to mitochondrial ATP synthesis in C 2C12 muscle cells
    • CONNOR, M. K., I. IRRCHER, and D. A. HOOD. Contractile activity-induced transcriptional activation of cytochrome C involves Spl and is proportional to mitochondrial ATP synthesis in C2C12 muscle cells. J. Biol. Chem. 276:15898-15904, 2001.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15898-15904
    • Connor, M.K.1    Irrcher, I.2    Hood, D.A.3
  • 7
    • 0032444931 scopus 로고    scopus 로고
    • Thyroid hormone modifies mitochondrial phenotype by increasing protein import without altering degradation
    • CRAIG, E. E., A. CHESLEY, and D. A. HOOD. Thyroid hormone modifies mitochondrial phenotype by increasing protein import without altering degradation. Am. J. Physiol. 275:C1508-C1515, 1998.
    • (1998) Am. J. Physiol. , vol.275
    • Craig, E.E.1    Chesley, A.2    Hood, D.A.3
  • 8
    • 0031741738 scopus 로고    scopus 로고
    • Preprotein translocase of the outer mitochondrial membrane: Molecular dissection and assembly of the general import pore
    • DEKKER, P. J. T., M. T. RYAN, J. BRIX, MÜLLER, A. HÖNLINGER, and N. PFANNER. Preprotein translocase of the outer mitochondrial membrane: molecular dissection and assembly of the general import pore. Mol. Cell. Biol. 18:6515-6524, 1998.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6515-6524
    • Dekker, P.J.T.1    Ryan, M.T.2    Brix, J.3    Müller, H.4    Hönlinger, A.5    Pfanner, N.6
  • 10
    • 1842329159 scopus 로고    scopus 로고
    • Tom 5 functionally links mitochondrial preprotein receptors to the general import pore
    • DIETMEIER, K., A. HÖNLINGER, U. BOMER, et al. Tom5 functionally links mitochondrial preprotein receptors to the general import pore. Nature 388:195-200, 1997.
    • (1997) Nature , vol.388 , pp. 195-200
    • Dietmeier, K.1    Hönlinger, A.2    Bomer, U.3
  • 11
    • 0024546684 scopus 로고
    • Adriamycin a drug interacting with acidic phospholipids blocks import of precursor proteins by isolated yeast mitochondria
    • EILERS, M., T. ENDO, and G. SCHATZ. Adriamycin, a drug interacting with acidic phospholipids blocks import of precursor proteins by isolated yeast mitochondria. J. Biol. Chem. 264:2945-2950, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2945-2950
    • Eilers, M.1    Endo, T.2    Schatz, G.3
  • 12
    • 0029689984 scopus 로고    scopus 로고
    • A Contractile activity-induced mitochondrial biogenesis in skeletal muscle
    • ESSIG, D. A Contractile activity-induced mitochondrial biogenesis in skeletal muscle. Exerc. Sport Sci. Rev. 24:289-319, 1996.
    • (1996) Exerc. Sport Sci. Rev. , vol.24 , pp. 289-319
    • Essig, D.1
  • 13
    • 0024358781 scopus 로고
    • Interaction of nuclear factors with multiple sites in the somatic cytochrome c promoter
    • EVANS, M. J., and R. C. SCARPULLA. Interaction of nuclear factors with multiple sites in the somatic cytochrome c promoter. J. Biol. Chem. 264:14361-14368, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14361-14368
    • Evans, M.J.1    Scarpulla, R.C.2
  • 14
    • 0023684801 scopus 로고
    • Purification and characterization of human mitochondrial transcription factor 1
    • FISHER, R. P, and D. A. CLAYTON. Purification and characterization of human mitochondrial transcription factor 1. Mol. Cell. Biol. 8:3496-3509, 1988.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3496-3509
    • Fisher, R.P.1    Clayton, D.A.2
  • 15
    • 0024811763 scopus 로고
    • Flexible recognition of rapidly evolving promoter sequences by mitochondrial transcription factor 1
    • FISHER, R. P., M. A. PARISI, and D. A. CLAYTON. Flexible recognition of rapidly evolving promoter sequences by mitochondrial transcription factor 1. Genes Dev. 3:2202-2217, 1989.
    • (1989) Genes Dev. , vol.3 , pp. 2202-2217
    • Fisher, R.P.1    Parisi, M.A.2    Clayton, D.A.3
  • 16
    • 0032791761 scopus 로고    scopus 로고
    • Cytochrome c transcriptional activation and mRNA stability during contractile activity in skeletal muscle
    • FREYSSENET, D., M. K. CONNOR, M. TAKAHASHI, and D. A. HOOD. Cytochrome c transcriptional activation and mRNA stability during contractile activity in skeletal muscle. Am. J. Physiol. 277: E26-E32, 1999.
    • (1999) Am. J. Physiol. , vol.277
    • Freyssenet, D.1    Connor, M.K.2    Takahashi, M.3    Hood, D.A.4
  • 17
    • 0033515628 scopus 로고    scopus 로고
    • Calcium-dependent regulation of cytochrome c gene expression in skeletal muscle cells: Identification of a protein kinase c-dependent pathway
    • FREYSSENET, D., M. DI CARLO, and D. A. HOOD. Calcium-dependent regulation of cytochrome c gene expression in skeletal muscle cells: identification of a protein kinase c-dependent pathway. J. Biol. Chem. 274:9305-9311, 1999.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9305-9311
    • Freyssenet, D.1    Di Carlo, M.2    Hood, D.A.3
  • 18
    • 0035168996 scopus 로고    scopus 로고
    • Effects of contractile activity on mitochondrial transcription factor A expression in skeletal muscle
    • GORDON, J. W., A. A. RUNGI, H. INAGAKI, and D. A. HOOD. Effects of contractile activity on mitochondrial transcription factor A expression in skeletal muscle. J. Appl. Physiol. 90:389-396, 2001.
    • (2001) J. Appl. Physiol. , vol.90 , pp. 389-396
    • Gordon, J.W.1    Rungi, A.A.2    Inagaki, H.3    Hood, D.A.4
  • 19
    • 0025666322 scopus 로고
    • eu(URR) gene associated with the MELAS subgroup of mitochondrial encephalomyopathies
    • eu(URR) gene associated with the MELAS subgroup of mitochondrial encephalomyopathies. Nature 348:651-653, 1990.
    • (1990) Nature , vol.348 , pp. 651-653
    • Goto, Y.1    Nonaka, I.2    Horai, S.3
  • 20
    • 0033725135 scopus 로고    scopus 로고
    • Tom20-mediated mitochondrial protein import in intact muscle cells during differentiation
    • GREY, J. Y., M. K. CONNOR, J. W. GORDON, and D. A. HOOD. Tom20-mediated mitochondrial protein import in intact muscle cells during differentiation. Am. J. Physiol. 279:C1393-1400, 2000.
    • (2000) Am. J. Physiol. , vol.279
    • Grey, J.Y.1    Connor, M.K.2    Gordon, J.W.3    Hood, D.A.4
  • 21
    • 0033551701 scopus 로고    scopus 로고
    • Coordinate induction of energy gene expression in tissues of mitochondrial disease patients
    • HEDDI, A., G. STEPIEN, P.J. BENKE, and D. C. WALLACE. Coordinate induction of energy gene expression in tissues of mitochondrial disease patients. J. Biol. Chem. 274:22968-22976, 1999.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22968-22976
    • Heddi, A.1    Stepien, G.2    Benke, P.J.3    Wallace, D.C.4
  • 22
    • 0037189583 scopus 로고    scopus 로고
    • The C66W mutation in the deafness dystonia peptide 1 (DDP1) affects the formation of functional DDP1-Tim 13 complexes in the mitochondrial intermembrane space
    • HOFFMAN, S., U. ROTHBAUER, N. MUHLENBEIN, et al. The C66W mutation in the deafness dystonia peptide 1 (DDP1) affects the formation of functional DDP1-Tim13 complexes in the mitochondrial intermembrane space. J. Biol. Chem. 277:23287-23293, 2002.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23287-23293
    • Hoffman, S.1    Rothbauer, U.2    Muhlenbein, N.3
  • 23
    • 0014198263 scopus 로고
    • Biochemical adaptations in muscle
    • HOLLOSZY, J. O. Biochemical adaptations in muscle. J. Biol. Chem. 242:2278-2282, 1967.
    • (1967) J. Biol. Chem. , vol.242 , pp. 2278-2282
    • Holloszy, J.O.1
  • 24
    • 0025267548 scopus 로고
    • A new mitochondrial disease associated with mitochondrial DNA heteroplasmy
    • HOLT, I. J., A. E. HARDING, R. K. H. PETTY, and J. A. MORGAN-HUGHES. A new mitochondrial disease associated with mitochondrial DNA heteroplasmy. Am. J. Hum. Genet. 46:428-433, 1990.
    • (1990) Am. J. Hum. Genet. , vol.46 , pp. 428-433
    • Holt, I.J.1    Harding, A.E.2    Petty, R.K.H.3    Morgan-Hughes, J.A.4
  • 25
    • 0029927409 scopus 로고    scopus 로고
    • Tom7 modulates the dynamics of the mitochondrial outer membrane translocase and plays a pathway-related role in protein import
    • HÖNLINGER, A., U. BÖMER, A. ALCONADA, et al. Tom7 modulates the dynamics of the mitochondrial outer membrane translocase and plays a pathway-related role in protein import. EMBO J. 15:2125-2137, 1996.
    • (1996) EMBO J. , vol.15 , pp. 2125-2137
    • Hönlinger, A.1    Bömer, U.2    Alconada, A.3
  • 26
    • 0035112481 scopus 로고    scopus 로고
    • Invited review: Contractile activity-induced mitochondrial biogenesis in skeletal muscle
    • HOOD, D. A., Invited review: contractile activity-induced mitochondrial biogenesis in skeletal muscle. J. Appl. Physiol. 90:1137-1157, 2001.
    • (2001) J. Appl. Physiol. , vol.90 , pp. 1137-1157
    • Hood, D.A.1
  • 28
    • 0025765069 scopus 로고
    • Metabolic and contractile responses of rat fast-twitch muscle to 10-Hz stimulation
    • HOOD, D. A., and G. PARENT. Metabolic and contractile responses of rat fast-twitch muscle to 10-Hz stimulation. Am. J. Physiol. 260:C832-C840, 1991.
    • (1991) Am. J. Physiol. , vol.260
    • Hood, D.A.1    Parent, G.2
  • 29
    • 0028131509 scopus 로고
    • Decreased synthesis and inefficient mitochondrial import of hsp 60 in a patient with a mitochondrial encephalomyopathy
    • HUCKRIEDE, A., and E. AGSTERIBBE. Decreased synthesis and inefficient mitochondrial import of hsp60 in a patient with a mitochondrial encephalomyopathy. Biochim. Biophys. Acta 1227:200-206, 1994.
    • (1994) Biochim. Biophys. Acta , vol.1227 , pp. 200-206
    • Huckriede, A.1    Agsteribbe, E.2
  • 30
    • 0030845305 scopus 로고    scopus 로고
    • Mutations in genes encoding the mitochondrial outer membrane proteins Tom 70 and Mdm10 of Podospora anserina modify the spectrum of mitochondrial DNA rearrangements associated with cellular death
    • JAMET-VIERNY, C., V. CONTAMINE, J. BOULAY, D. ZICKLER, and M. PICARD. Mutations in genes encoding the mitochondrial outer membrane proteins Tom70 and Mdm10 of Podospora anserina modify the spectrum of mitochondrial DNA rearrangements associated with cellular death. Mol. Cell. Biol. 17:6359-6366, 1997.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6359-6366
    • Jamet-Vierny, C.1    Contamine, V.2    Boulay, J.3    Zickler, D.4    Picard, M.5
  • 31
    • 0031581107 scopus 로고    scopus 로고
    • Visualization of mitochondria with green fluorescent protein in cultured fibroblasts from patients with mitochondrial diseases
    • KANAZAWA, M., M. YANO, C. NAMCHAI, et al. Visualization of mitochondria with green fluorescent protein in cultured fibroblasts from patients with mitochondrial diseases. Biochem. Biophys. Res. Commun. 239:580-584, 1997.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 580-584
    • Kanazawa, M.1    Yano, M.2    Namchai, C.3
  • 33
    • 0027946119 scopus 로고
    • Recognition of mitochondrial-targeting signals by a cytosolic import stimulating factor, MSF
    • KOMIYA, T., N. HACHIYA, M. SAKAGUCHI, T. OMURA, and K. MIHARA. Recognition of mitochondrial- targeting signals by a cytosolic import stimulating factor, MSF. J. Biol. Chem. 269:30893-30897, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30893-30897
    • Komiya, T.1    Hachiya, N.2    Sakaguchi, M.3    Omura, T.4    Mihara, K.5
  • 34
    • 0030045427 scopus 로고    scopus 로고
    • Cytoplasmic chaperones determine the targeting pathway of precursor proteins to mitochondria
    • KOMIYA, T., M. SAKAGUCHI, and K. MIHARA. Cytoplasmic chaperones determine the targeting pathway of precursor proteins to mitochondria. EMBO J. 15:399-407, 1996.
    • (1996) EMBO J. , vol.15 , pp. 399-407
    • Komiya, T.1    Sakaguchi, M.2    Mihara, K.3
  • 35
    • 0032527780 scopus 로고    scopus 로고
    • Interaction of mitochondrial targeting signals with acidic receptor domains along the protein import pathway: Evidence for the "acid chain" hypothesis
    • KOMIYA, T., S. ROSPERT, C. KOEHLER, R. LOOSER, G. SCHATZ, and K. MIHARA. Interaction of mitochondrial targeting signals with acidic receptor domains along the protein import pathway: evidence for the "acid chain" hypothesis. EMBO J. 17:3886-3898, 1998.
    • (1998) EMBO J. , vol.17 , pp. 3886-3898
    • Komiya, T.1    Rospert, S.2    Koehler, C.3    Looser, R.4    Schatz, G.5    Mihara, K.6
  • 36
    • 0033864758 scopus 로고    scopus 로고
    • Mitochondrial protein import motor: The ATPase domain of matrix Hsp70 is crucial for binding to Tim44, while the peptide binding domain and the carboxy-terminal segment play a stimulatory role
    • KRIMMER, T., J. RASSOW, W. H. KUNAU, W. VOOS, and N. PFANNER. Mitochondrial protein import motor: the ATPase domain of matrix Hsp70 is crucial for binding to Tim44, while the peptide binding domain and the carboxy-terminal segment play a stimulatory role. Mol. Cell. Biol. 20:5879-5887, 2000.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5879-5887
    • Krimmer, T.1    Rassow, J.2    Kunau, W.H.3    Voos, W.4    Pfanner, N.5
  • 37
    • 0029941297 scopus 로고    scopus 로고
    • The N-terminal half of a mitochondrial presequence peptide inserts into cardiolipin-containing membranes
    • LEENHOUTS, J. M., Z. TOROK, V. MANDIEAU, E. GOORMAGHTIGH, and B. DE KRUUFF. The N-terminal half of a mitochondrial presequence peptide inserts into cardiolipin-containing membranes. FEBS Lett. 388:34-38, 1996.
    • (1996) FEBS Lett. , vol.388 , pp. 34-38
    • Leenhouts, J.M.1    Torok, Z.2    Mandieau, V.3    Goormaghtigh, E.4    De Kruuff, B.5
  • 38
    • 0031604554 scopus 로고    scopus 로고
    • Structural organization and transcriptional regulation of nuclear genes encoding the mammalian cytochrome c oxidase complex
    • LENKA, N. C., J. VIJAYASARATHY, J. MULLNICK, and N. G. AVADHANI. Structural organization and transcriptional regulation of nuclear genes encoding the mammalian cytochrome c oxidase complex. Prog. Nucl. Acid Res. Mol. Biol. 61:309-344, 1998.
    • (1998) Prog. Nucl. Acid Res. Mol. Biol. , vol.61 , pp. 309-344
    • Lenka, N.C.1    Vijayasarathy, J.2    Mullnick, J.3    Avadhani, N.G.4
  • 39
    • 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., J. O. HOLLOSZY, and C. F. SEMENKOVICH. Respiratory uncoupling induces delta- aminolevulinate synthase expression through a nuclear respiratory factor-1 dependent mechanism in HeLa cells. J. Biol. Chem. 274:17534-17540, 1999.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17534-17540
    • Li, B.1    Holloszy, J.O.2    Semenkovich, C.F.3
  • 40
    • 0025953614 scopus 로고
    • Role of an energized inner membrane in mitochondrial protein import. Delta psi drives the movement of presequences
    • MARTIN, J., K. MAHLKE, and N. PFANNER. Role of an energized inner membrane in mitochondrial protein import. Delta psi drives the movement of presequences. J. Biol. Chem. 266:18051-18057, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18051-18057
    • Martin, J.1    Mahlke, K.2    Pfanner, N.3
  • 41
    • 0034328890 scopus 로고    scopus 로고
    • Protein unfolding by mitochondria. The Hsp 70 import motor
    • MATOUSCHEK, A., N. PFANNER, and W. Voos. Protein unfolding by mitochondria. The Hsp70 import motor. EMBO Rep. 1:404-410, 2000.
    • (2000) EMBO Rep. , vol.1 , pp. 404-410
    • Matouschek, A.1    Pfanner, N.2    Voos, W.3
  • 42
    • 0036148610 scopus 로고    scopus 로고
    • A human mitochondrial transcription factor is related to RNA adenine methyltransferases and binds s-adenosylmethionine
    • MCCULLOCH, V., B. L SEIDEL-ROGOL, and G. S. SHADEL. A human mitochondrial transcription factor is related to RNA adenine methyltransferases and binds s-adenosylmethionine. Mol. Cell Biol. 22:1116-1125, 2002.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 1116-1125
    • Mcculloch, V.1    Seidel-Rogol, B.L.2    Shadel, G.S.3
  • 43
    • 0025968682 scopus 로고
    • Pearson syndrome and mitochondrial encephalomyopathy in a patient with a deletion of mtDNA
    • MCSHANE, M. A., S. R. HAMMANS, M. G. SWEENY, et al. Pearson syndrome and mitochondrial encephalomyopathy in a patient with a deletion of mtDNA. Am. J. Hum. Genet. 48:39-42, 1991.
    • (1991) Am. J. Hum. Genet. , vol.48 , pp. 39-42
    • Mcshane, M.A.1    Hammans, S.R.2    Sweeny, M.G.3
  • 44
    • 0030021114 scopus 로고    scopus 로고
    • Cytoplasmic chaperones in precursor targeting to mitochondria: The role of MSF and hsp 70
    • MIHARA, K., and T. OMURA. Cytoplasmic chaperones in precursor targeting to mitochondria: the role of MSF and hsp70. Trends Cell Biol. 6:104-108, 1996.
    • (1996) Trends Cell Biol. , vol.6 , pp. 104-108
    • Mihara, K.1    Omura, T.2
  • 45
    • 0024328462 scopus 로고
    • Mitochondrial DNA deletions in progressive external ophthalmoplegia and KearnsSayre syndrome
    • MORAES, C. T., S. DIMAURO, M. ZEVIANI, et al. Mitochondrial DNA deletions in progressive external ophthalmoplegia and KearnsSayre syndrome. N. Engl. J. Med. 320:1293-1299, 1989.
    • (1989) N. Engl. J. Med. , vol.320 , pp. 1293-1299
    • Moraes, C.T.1    Dimauro, S.2    Zeviani, M.3
  • 46
    • 0029157324 scopus 로고
    • Expression of stress proteins and mitochondrial chaperonins in chronically stimulated skeletal muscle
    • ORNATSKY, O. I., M. K. CONNOR, and D. A. HOOD. Expression of stress proteins and mitochondrial chaperonins in chronically stimulated skeletal muscle. Biochem. J. 311:119-123, 1995.
    • (1995) Biochem. J. , vol.311 , pp. 119-123
    • Ornatsky, O.I.1    Connor, M.K.2    Hood, D.A.3
  • 47
    • 0030910776 scopus 로고    scopus 로고
    • Mitochondrial biogenesis: The Tom and Tim machine
    • PFANNER, N., and M. MEIJER. Mitochondrial biogenesis: the Tom and Tim machine. Curr. Biol. 7:R100-R103, 1997.
    • (1997) Curr. Biol. , vol.7
    • Pfanner, N.1    Meijer, M.2
  • 48
    • 0029894544 scopus 로고    scopus 로고
    • Crosstalk between nuclear and mitochondrial genomes
    • POYTON, R. O., and J. E. MCEWEN. Crosstalk between nuclear and mitochondrial genomes. Annu. Rev. Biochem. 65:563-607, 1996.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 563-607
    • Poyton, R.O.1    Mcewen, J.E.2
  • 49
    • 0034756937 scopus 로고    scopus 로고
    • Structural requirements of Tom 40 for assembly into preexisting TOM complexes of mitochondria
    • RAPAPORT, D., R. D. TAYLOR, M. KÄSER, L. THOMAS, W. NEUPERT, and F. E. NARGANG. Structural requirements of Tom40 for assembly into preexisting TOM complexes of mitochondria. Mol. Biol. Cell 12:1189-1198, 2001.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1189-1198
    • Rapaport, D.1    Taylor, R.D.2    Käser, M.3    Thomas, L.4    Neupert, W.5    Nargang, F.E.6
  • 50
    • 0024999562 scopus 로고
    • Polypeptides traverse the mitochondrial envelope in an extended state
    • RASSOW, J., F. U. HARTL, B. GUIARD, N. PFANNER, and W. NEUPERT. Polypeptides traverse the mitochondrial envelope in an extended state. FEBS Lett. 275:190-194, 1990.
    • (1990) FEBS Lett. , vol.275 , pp. 190-194
    • Rassow, J.1    Hartl, F.U.2    Guiard, B.3    Pfanner, N.4    Neupert, W.5
  • 51
    • 0033548261 scopus 로고    scopus 로고
    • The preprotein translocase of the mitochondrial inner membrane: Function and evolution
    • RASSOW, J., P. J. DEKKER, S. VAN WILPE, M. MEIJER, and J. SOLL. The preprotein translocase of the mitochondrial inner membrane: function and evolution. J. Mol. Biol. 286:105-120, 1999.
    • (1999) J. Mol. Biol. , vol.286 , pp. 105-120
    • Rassow, J.1    Dekker, P.J.2    Van Wilpe, S.3    Meijer, M.4    Soll, J.5
  • 52
    • 18244386043 scopus 로고    scopus 로고
    • Expression of the uncoupling protein 1 from the aP2 gene promoter stimulates mitochondrial biogenesis in unilocular adipocytes in vivo
    • ROSSMEISL, M., G. BARBATELLI, P. FLACHS, et al. Expression of the uncoupling protein 1 from the aP2 gene promoter stimulates mitochondrial biogenesis in unilocular adipocytes in vivo. Eur. J. Biochem. 269:19-28, 2002.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 19-28
    • Rossmeisl, M.1    Barbatelli, G.2    Flachs, P.3
  • 53
    • 0037117307 scopus 로고    scopus 로고
    • Events upstream of mitochondrial protein import limit the oxidative capacity of fibroblasts in multiple mitochondrial disease
    • RUNGI, A. A., A. PRIMEAU, L. N. CHRISTIE, J. W. GORDON, B. H. ROBINSON, and D. A. HOOD. Events upstream of mitochondrial protein import limit the oxidative capacity of fibroblasts in multiple mitochondrial disease. Biochim. Biophys. Acta 1586:146-154, 2002.
    • (2002) Biochim. Biophys. Acta , vol.1586 , pp. 146-154
    • Rungi, A.A.1    Primeau, A.2    Christie, L.N.3    Gordon, J.W.4    Robinson, B.H.5    Hood, D.A.6
  • 54
    • 0035229003 scopus 로고    scopus 로고
    • Assaying protein import into mitochondria
    • RYAN, M. T., W. Voos, and N. PFANNER. Assaying protein import into mitochondria. Methods Cell Biol. 65:189-215, 2001.
    • (2001) Methods Cell Biol. , vol.65 , pp. 189-215
    • Ryan, M.T.1    Voos, W.2    Pfanner, N.3
  • 55
    • 0034644647 scopus 로고    scopus 로고
    • Identification of mammalian TOM 22 as a subunit of the preprotein translocase of the mitochondrial outer membrane
    • SAEKI, K., H. SUZUKI, M. TSUNEOKA, et al. Identification of mammalian TOM22 as a subunit of the preprotein translocase of the mitochondrial outer membrane. J. Biol. Chem. 275:31996-2002, 2000.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31996-32002
    • Saeki, K.1    Suzuki, H.2    Tsuneoka, M.3
  • 56
    • 0035986085 scopus 로고    scopus 로고
    • Exercise effects on muscle insulin signaling and action
    • SAKAMOTO, K., and L. J. GOODYEAR. Exercise effects on muscle insulin signaling and action. J. Appl. Physiol. 93:369-383, 2002.
    • (2002) J. Appl. Physiol. , vol.93 , pp. 369-383
    • Sakamoto, K.1    Goodyear, L.J.2
  • 57
    • 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 1576:1-14, 2002.
    • (2002) Biochim. Biophys. Acta , vol.1576 , pp. 1-14
    • Scarpulla, R.C.1
  • 58
    • 0025328563 scopus 로고
    • Mitochondrial myopathy with a defect of mitochondrial-protein transport
    • SHAPIRA, A. H. V., J. M. COOPER, D. N. LANDON, and J. B. CLARK. Mitochondrial myopathy with a defect of mitochondrial-protein transport. N. Engl. J. Med. 323:37-41, 1990.
    • (1990) N. Engl. J. Med. , vol.323 , pp. 37-41
    • Shapira, A.H.V.1    Cooper, J.M.2    Landon, D.N.3    Clark, J.B.4
  • 59
    • 0034128065 scopus 로고    scopus 로고
    • Effect of thyroid hormone on mthsp70 expression, mitochondrial import and processing in cardiac muscle
    • SCHNEIDER, J. J., and D. A. HOOD. Effect of thyroid hormone on mthsp70 expression, mitochondrial import and processing in cardiac muscle. J. Endocrinol. 165:9-17, 2000.
    • (2000) J. Endocrinol. , vol.165 , pp. 9-17
    • Schneider, J.J.1    Hood, D.A.2
  • 60
    • 0023373784 scopus 로고
    • Characterization of translocation contact sites involved in the import of mitochondrial proteins
    • SCHWAIGER, M., V. HERZOG, and W. NEUPERT. Characterization of translocation contact sites involved in the import of mitochondrial proteins. J. Cell Biol. 105:235-246, 1987.
    • (1987) J. Cell Biol. , vol.105 , pp. 235-246
    • Schwaiger, M.1    Herzog, V.2    Neupert, W.3
  • 61
    • 0027478067 scopus 로고
    • Chronic stimulation-induced changes in mitochondria and performance in rat skeletal muscle
    • TAKAHASHI, M., and D. A. HOOD. Chronic stimulation-induced changes in mitochondria and performance in rat skeletal muscle. J. Appl. Physiol. 74:934-941, 1993.
    • (1993) J. Appl. Physiol. , vol.74 , pp. 934-941
    • Takahashi, M.1    Hood, D.A.2
  • 62
    • 0031831491 scopus 로고    scopus 로고
    • Contractile activity-induced adaptations in the mitochondrial protein import system
    • TAKAHASHI, M., A. CHESLEY, D. FREYSSENET, and D. A. HOOD. Contractile activity-induced adaptations in the mitochondrial protein import system. Am. J. Physiol. 274:C1380-C1387, 1998.
    • (1998) Am. J. Physiol. , vol.274
    • Takahashi, M.1    Chesley, A.2    Freyssenet, D.3    Hood, D.A.4
  • 63
    • 0022481113 scopus 로고
    • The presequences of two imported mitochondrial proteins contain information for intracellular and intramitochondrial sorting
    • VAN LOON, A. P., A. W. BRANDLI, and G. SCHATZ. The presequences of two imported mitochondrial proteins contain information for intracellular and intramitochondrial sorting. Cell 44:801-812, 1986.
    • (1986) Cell , vol.44 , pp. 801-812
    • Van Loon, A.P.1    Brandli, A.W.2    Schatz, G.3
  • 64
    • 0033981680 scopus 로고    scopus 로고
    • Mitochondrial defects in cardiomyopathy and neuromuscular disease
    • WALLACE, D. C. Mitochondrial defects in cardiomyopathy and neuromuscular disease. Am. Heart J. 139:S70-S85, 2000.
    • (2000) Am. Heart J. , vol.139
    • Wallace, D.C.1
  • 66
    • 0025765070 scopus 로고
    • Mitochondrial adaptations in denervated muscle: Relationship to muscle performance
    • WICKS, K. L., and D. A. HOOD. Mitochondrial adaptations in denervated muscle: relationship to muscle performance. Am. J. Physiol. 260:C841-C850, 1991.
    • (1991) Am. J. Physiol. , vol.260
    • Wicks, K.L.1    Hood, D.A.2
  • 67
    • 0022974362 scopus 로고
    • Mitochondrial gene expression in mammalian striated muscle: Evidence that variation in gene dosage is the major regulatory event
    • WILLIAMS, R. S. Mitochondrial gene expression in mammalian striated muscle: evidence that variation in gene dosage is the major regulatory event. J. Biol. Chem. 261:12390-12394, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12390-12394
    • Williams, R.S.1
  • 68
    • 0022650598 scopus 로고
    • Regulation of nuclear and mitochondrial gene expression by contractile activity in skeletal muscle
    • WILLIAMS, R. S., S. SALMONS, E. A. NEWSHOLME, R. E. KAUFMAN, and J. MELLOR. Regulation of nuclear and mitochondrial gene expression by contractile activity in skeletal muscle. J. Biol. Chem. 261:376-380, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 376-380
    • Williams, R.S.1    Salmons, S.2    Newsholme, E.A.3    Kaufman, R.E.4    Mellor, J.5
  • 69
    • 0032792665 scopus 로고    scopus 로고
    • AMP-activated protein kinase, a metabolic master switch: Possible roles in Type 2 diabetes
    • WINDER, W. W., and D. G. HARDIE, AMP-activated protein kinase, a metabolic master switch: possible roles in Type 2 diabetes. Am. J. Physiol. 277:E1-E10, 1999.
    • (1999) Am. J. Physiol. , vol.277
    • Winder, W.W.1    Hardie, D.G.2
  • 70
    • 0033949848 scopus 로고    scopus 로고
    • Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle
    • WINDER, W. W., B. F. HOLMES, D. S. RUBINK, E. B. JENSEN, M. CHEN, and J. O. HOLLOSZY. Activation of AMP- activated protein kinase increases mitochondrial enzymes in skeletal muscle. J. Appl. Physiol. 88:2219-2226, 2000.
    • (2000) J. Appl. Physiol. , vol.88 , pp. 2219-2226
    • Winder, W.W.1    Holmes, B.F.2    Rubink, D.S.3    Jensen, E.B.4    Chen, M.5    Holloszy, J.O.6
  • 71
    • 0037066459 scopus 로고    scopus 로고
    • Regulation of mitochondrial biogenesis in skeletal muscle by CaMK
    • Wu, H., S. B. KANATOUS, F. A. THURMOND, et al. Regulation of mitochondrial biogenesis in skeletal muscle by CaMK. Science 296:349-352, 2002.
    • (2002) Science , vol.296 , pp. 349-352
    • Wu, H.1    Kanatous, S.B.2    Thurmond, F.A.3
  • 72
    • 0033538473 scopus 로고    scopus 로고
    • Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1
    • WU, Z., P. PUIGSERVER, U. ANDERSSON, et al. Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1. Cell 98:115-124, 1999.
    • (1999) Cell , vol.98 , pp. 115-124
    • Wu, Z.1    Puigserver, P.2    Andersson, U.3
  • 73
    • 0030881873 scopus 로고    scopus 로고
    • Electrical stimulation of neonatal cardiomyocytes results in the sequential activation of nuclear genes governing mitochondrial proliferation and differentiation
    • XIA, Y., L. M. BUJA, R. C. SCARPULLA, and J. B. MCMILLIN. Electrical stimulation of neonatal cardiomyocytes results in the sequential activation of nuclear genes governing mitochondrial proliferation and differentiation. Proc. Natl. Acad. Sci. USA 94: 11399-11404, 1997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11399-11404
    • Xia, Y.1    Buja, L.M.2    Scarpulla, R.C.3    Mcmillin, J.B.4
  • 74
    • 0029862518 scopus 로고    scopus 로고
    • Increased contractile activity decreases RNA-protein interaction in the 3′-UTR of cytochrome c mRNA
    • YAN, Z., S. SALMONS, Y. LI DANG, M. T. HAMILTON, and F. W. BOOTH. Increased contractile activity decreases RNA-protein interaction in the 3′-UTR of cytochrome c mRNA. Am. J. Physiol. 271:C1157-C1166, 1996.
    • (1996) Am. J. Physiol. , vol.271
    • Yan, Z.1    Salmons, S.2    Li Dang, Y.3    Hamilton, M.T.4    Booth, F.W.5
  • 75
    • 0032780688 scopus 로고    scopus 로고
    • On the role of the general transcription factor Spl in the activation and repression of diverse mammalian oxidative phosphorylation genes
    • ZAID, A., R. LI, K. LUCIAKOVA, P. BARATH, S. NERY, and B. D. NELSON. On the role of the general transcription factor Spl in the activation and repression of diverse mammalian oxidative phosphorylation genes. J. Bioenerg. Biomembr. 31:129-135, 1999.
    • (1999) J. Bioenerg. Biomembr. , vol.31 , pp. 129-135
    • Zaid, A.1    Li, R.2    Luciakova, K.3    Barath, P.4    Nery, S.5    Nelson, B.D.6


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