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Volumn 119, Issue 14, 2006, Pages 2855-2862

Nitric oxide and mitochondrial biogenesis

Author keywords

Aging; Mitochondrial biogenesis; Nitric oxide; Peroxisome proliferator activated receptor coactivator 1

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIUM ION; CD28 ANTIGEN; CD3 ANTIGEN; CELL PROTEIN; CYTOCHROME C OXIDASE; ENDOTHELIAL NITRIC OXIDE SYNTHASE; LIPID; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; NUCLEAR PROTEIN; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR;

EID: 33746841367     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.03062     Document Type: Article
Times cited : (248)

References (110)
  • 1
    • 0035425503 scopus 로고    scopus 로고
    • Nitric oxide synthases: Structure, function and inhibition
    • Alderton, W. K., Cooper, C. E. and Knowles, R. G. (2001). Nitric oxide synthases: structure, function and inhibition. Biochem. J. 357, 593-615.
    • (2001) Biochem. J. , vol.357 , pp. 593-615
    • Alderton, W.K.1    Cooper, C.E.2    Knowles, R.G.3
  • 2
    • 33746811205 scopus 로고
    • Die elementarorganismen und ihre beziehungen zu den zellen
    • Leipzig: Viet & Comp. In (1994) (ed. J. Sapp), New York: Oxford University Press
    • Altmann, R. (1890). Die elementarorganismen und ihre beziehungen zu den zellen. Leipzig: Viet & Comp. In (1994) Evolution by Association. A History of Symbiosis (ed. J. Sapp), pp. 100-101. New York: Oxford University Press.
    • (1890) Evolution By Association. A History of Symbiosis , pp. 100-101
    • Altmann, R.1
  • 3
    • 0038329323 scopus 로고    scopus 로고
    • Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae
    • Anderson, R. M., Bitterman, K. J., Wood, J. G., Medvedik, O. and Sinclair, D. A. (2003). Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae. Nature 423, 181-185.
    • (2003) Nature , vol.423 , pp. 181-185
    • Anderson, R.M.1    Bitterman, K.J.2    Wood, J.G.3    Medvedik, O.4    Sinclair, D.A.5
  • 5
    • 0037593949 scopus 로고    scopus 로고
    • Mitofusin-2 determines mitochondrial network architecture and mitochondrial metabolism. A novel regulatory mechanism altered in obesity
    • Bach, D., Pich, S., Soriano, F. X., Vega, N., Baumgartner, B., Oriola, J., Daugaard, J. R., Lloberas, J., Camps, M., Zierath, J. R. et al. (2003). Mitofusin-2 determines mitochondrial network architecture and mitochondrial metabolism. A novel regulatory mechanism altered in obesity. J. Biol. Chem. 278, 17190-17197.
    • (2003) J. Biol. Chem. , vol.278 , pp. 17190-17197
    • Bach, D.1    Pich, S.2    Soriano, F.X.3    Vega, N.4    Baumgartner, B.5    Oriola, J.6    Daugaard, J.R.7    Lloberas, J.8    Camps, M.9    Zierath, J.R.10
  • 7
    • 0025036216 scopus 로고
    • Behavior of mitochondria in the living cell
    • Bereiter-Hahn, J. (1990). Behavior of mitochondria in the living cell. Int. Rev. Cytol. 122, 1-63.
    • (1990) Int. Rev. Cytol. , vol.122 , pp. 1-63
    • Bereiter-Hahn, J.1
  • 8
    • 0028047262 scopus 로고
    • Dynamics of mitochondria in living cells: Shape changes, dislocations, fusion, and fission of mitochondria
    • Bereiter-Hahn, J. and Voth, M. (1994). Dynamics of mitochondria in living cells: shape changes, dislocations, fusion, and fission of mitochondria. Microsc. Res. Tech. 27, 198-219.
    • (1994) Microsc. Res. Tech. , vol.27 , pp. 198-219
    • Bereiter-Hahn, J.1    Voth, M.2
  • 9
    • 0037942739 scopus 로고    scopus 로고
    • Extended longevity in mice lacking the insulin receptor in adipose tissue
    • Bluher, M., Kahn, B. B. and Kahn, C. R. (2003). Extended longevity in mice lacking the insulin receptor in adipose tissue. Science 299, 572-574.
    • (2003) Science , vol.299 , pp. 572-574
    • Bluher, M.1    Kahn, B.B.2    Kahn, C.R.3
  • 10
    • 17144429302 scopus 로고    scopus 로고
    • Calorie restriction, SIRT1 and metabolism: Understanding longevity
    • Bordone, L. and Guarente, L. (2005). Calorie restriction, SIRT1 and metabolism: understanding longevity. Nat. Rev. Mol. Cell Biol. 6, 298-305.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 298-305
    • Bordone, L.1    Guarente, L.2
  • 12
    • 0037105335 scopus 로고    scopus 로고
    • Mitochondria: Regulators of signal transduction by reactive oxygen and nitrogen species
    • Brookes, P. S., Levonen, A. L., Shiva, S., Sarti, P. and Darley-Usmar, V. M. (2002). Mitochondria: regulators of signal transduction by reactive oxygen and nitrogen species. Free Radic. Biol. Med. 33, 755-764.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 755-764
    • Brookes, P.S.1    Levonen, A.L.2    Shiva, S.3    Sarti, P.4    Darley-Usmar, V.M.5
  • 13
    • 0028134892 scopus 로고
    • Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase
    • Brown, G. C. and Cooper, C. E. (1994). Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase. FEBS Lett. 356, 295-298.
    • (1994) FEBS Lett. , vol.356 , pp. 295-298
    • Brown, G.C.1    Cooper, C.E.2
  • 14
    • 0019768234 scopus 로고
    • Mitochondrial proliferation during myogenesis
    • Brunk, C. F. (1981). Mitochondrial proliferation during myogenesis. Exp. Cell Res. 136, 305-309.
    • (1981) Exp. Cell Res. , vol.136 , pp. 305-309
    • Brunk, C.F.1
  • 16
    • 1842665662 scopus 로고    scopus 로고
    • Mitochondrial signaling: The retrograde response
    • Butow, R. A. and Avadhani, N. G. (2004). Mitochondrial signaling: the retrograde response. Mol. Cell 14, 1-15.
    • (2004) Mol. Cell , vol.14 , pp. 1-15
    • Butow, R.A.1    Avadhani, N.G.2
  • 17
    • 11144314179 scopus 로고    scopus 로고
    • Increased mitochondrial biogenesis in primary leukemia cells: The role of endogenous nitric oxide and impact on sensitivity to fludarabine
    • Carew, J. S., Nawrocki, S. T., Xu, R. H., Dunner, K., McConkey, D. J., Wierda, W. G., Keating, M. J. and Huang, P. (2004). Increased mitochondrial biogenesis in primary leukemia cells: the role of endogenous nitric oxide and impact on sensitivity to fludarabine. Leukemia 18, 1934-1940.
    • (2004) Leukemia , vol.18 , pp. 1934-1940
    • Carew, J.S.1    Nawrocki, S.T.2    Xu, R.H.3    Dunner, K.4    McConkey, D.J.5    Wierda, W.G.6    Keating, M.J.7    Huang, P.8
  • 18
    • 28844466919 scopus 로고    scopus 로고
    • How is mitochondrial biogenesis affected in mitochondrial disease?
    • Chabi, B., Adhihetty, P. J., Ljubicic, V. and Hood, D. A. (2005). How is mitochondrial biogenesis affected in mitochondrial disease? Med. Sci. Sports Exerc. 37, 2102-2110.
    • (2005) Med. Sci. Sports Exerc. , vol.37 , pp. 2102-2110
    • Chabi, B.1    Adhihetty, P.J.2    Ljubicic, V.3    Hood, D.A.4
  • 19
    • 0024148694 scopus 로고
    • Mitochondrial membrane potential in living cells
    • Chen, L. B. (1988). Mitochondrial membrane potential in living cells. Annu. Rev. Cell Biol. 4, 155-181.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 155-181
    • Chen, L.B.1
  • 20
    • 4043164343 scopus 로고    scopus 로고
    • Effect of a C/EBP gene replacement on mitochondrial biogenesis in fat cells
    • Chiu, C. H., Lin, W. D., Huang, S. Y. and Lee, Y. H. (2004). Effect of a C/EBP gene replacement on mitochondrial biogenesis in fat cells. Genes Dev. 18, 1970-1975.
    • (2004) Genes Dev. , vol.18 , pp. 1970-1975
    • Chiu, C.H.1    Lin, W.D.2    Huang, S.Y.3    Lee, Y.H.4
  • 21
    • 28044464985 scopus 로고
    • Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide. Implications for neurodegenerative diseases
    • Cleeter, M. W., Cooper, J. M., Darley-Usmar, V. M., Moncada, S. and Schapira, A. H. (1994). Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide. Implications for neurodegenerative diseases. FEBS Lett. 345, 50-54.
    • (1994) FEBS Lett. , vol.345 , pp. 50-54
    • Cleeter, M.W.1    Cooper, J.M.2    Darley-Usmar, V.M.3    Moncada, S.4    Schapira, A.H.5
  • 22
    • 0032560572 scopus 로고    scopus 로고
    • Persistent inhibition of cell respiration by nitric oxide: Crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione
    • Clementi, E., Brown, G. C., Feelisch, M. and Moncada, S. (1998). Persistent inhibition of cell respiration by nitric oxide: crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione. Proc. Natl. Acad. Sci. USA 95, 7631-7636.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7631-7636
    • Clementi, E.1    Brown, G.C.2    Feelisch, M.3    Moncada, S.4
  • 23
    • 0033573981 scopus 로고    scopus 로고
    • On the mechanism by which vascular endothelial cells regulate their oxygen consumption
    • Clementi, E., Brown, G. C., Foxwell, N. and Moncada, S. (1999). On the mechanism by which vascular endothelial cells regulate their oxygen consumption. Proc. Natl. Acad. Sci. USA 96, 1559-1562.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1559-1562
    • Clementi, E.1    Brown, G.C.2    Foxwell, N.3    Moncada, S.4
  • 25
    • 11144356896 scopus 로고    scopus 로고
    • Docking of endothelial nitric oxide synthase (eNOS) to the mitochondrial outer membrane: A pentabasic amino acid sequence in the autoinhibitory domain of eNOS targets a proteinase K-cleavable peptide on the cytoplasmic face of mitochondria
    • Gao, S., Chen, J., Brodsky, S. V., Huang, H., Adler, S., Lee, J. H., Dhadwal, N., Cohen-Gould, L., Gross, S. S. and Goligorsky, M. S. (2004). Docking of endothelial nitric oxide synthase (eNOS) to the mitochondrial outer membrane: a pentabasic amino acid sequence in the autoinhibitory domain of eNOS targets a proteinase K-cleavable peptide on the cytoplasmic face of mitochondria. J. Biol. Chem. 279, 15968-15974.
    • (2004) J. Biol. Chem. , vol.279 , pp. 15968-15974
    • Gao, S.1    Chen, J.2    Brodsky, S.V.3    Huang, H.4    Adler, S.5    Lee, J.H.6    Dhadwal, N.7    Cohen-Gould, L.8    Gross, S.S.9    Goligorsky, M.S.10
  • 26
    • 0038532257 scopus 로고    scopus 로고
    • Regulation of the nitric oxide reduction operon (norRVW) in Escherichia coli. Role of NorR and sigma54 in the nitric oxide stress response
    • Gardner, A. M., Gessner, C. R. and Gardner, P. R. (2003). Regulation of the nitric oxide reduction operon (norRVW) in Escherichia coli. Role of NorR and sigma54 in the nitric oxide stress response. J. Biol. Chem. 278, 10081-10086.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10081-10086
    • Gardner, A.M.1    Gessner, C.R.2    Gardner, P.R.3
  • 29
    • 0032079478 scopus 로고    scopus 로고
    • Production of nitric oxide by mitochondria
    • Giulivi, C., Poderoso, J. J. and Boveris, A. (1998). Production of nitric oxide by mitochondria. J. Biol. Chem. 273, 11038-11043.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11038-11043
    • Giulivi, C.1    Poderoso, J.J.2    Boveris, A.3
  • 30
    • 0033040623 scopus 로고    scopus 로고
    • Action of thyroid hormones at the cellular level: The mitochondrial target
    • Goglia, F., Moreno, M. and Lanni, A. (1999). Action of thyroid hormones at the cellular level: the mitochondrial target. FEBS Lett. 452, 115-120.
    • (1999) FEBS Lett. , vol.452 , pp. 115-120
    • Goglia, F.1    Moreno, M.2    Lanni, A.3
  • 31
    • 0033525788 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • Gray, M. G., Burger, G. and Lang, B. F. (1999). Mitochondrial evolution. Science 283, 1476-1481.
    • (1999) Science , vol.283 , pp. 1476-1481
    • Gray, M.G.1    Burger, G.2    Lang, B.F.3
  • 32
    • 0034913239 scopus 로고    scopus 로고
    • The origin and early evolution of mitochondria
    • Gray, M. G., Burger, G. and Lang, B. F. (2001). The origin and early evolution of mitochondria. Genome Biol. 2, 1018.1-1018.5.
    • (2001) Genome Biol. , vol.2
    • Gray, M.G.1    Burger, G.2    Lang, B.F.3
  • 33
    • 0027073347 scopus 로고
    • The endosymbiont hypothesis revisited
    • Gray, M. W. (1992). The endosymbiont hypothesis revisited. Int. Rev. Cytol. 141, 233-357.
    • (1992) Int. Rev. Cytol. , vol.141 , pp. 233-357
    • Gray, M.W.1
  • 34
    • 0000527581 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • In (ed. D. M. Roberts, P. Sharp, G. Alderson and M. Collins), Cambridge: Cambridge University Press
    • Gray, M. W. and Spencer, D. F. (1996). Mitochondrial evolution. In Evolution of Microbial Life (ed. D. M. Roberts, P. Sharp, G. Alderson and M. Collins), pp. 107-126. Cambridge: Cambridge University Press.
    • (1996) Evolution of Microbial Life , pp. 107-126
    • Gray, M.W.1    Spencer, D.F.2
  • 35
    • 0348134741 scopus 로고    scopus 로고
    • Redistribution of intracellular oxygen in hypoxia by nitric oxide: Effect on HIF1α
    • Hagen, T., Taylor, C. T., Lam, F. and Moncada, S. (2003). Redistribution of intracellular oxygen in hypoxia by nitric oxide: effect on HIF1α. Science 302, 1975-1978.
    • (2003) Science , vol.302 , pp. 1975-1978
    • Hagen, T.1    Taylor, C.T.2    Lam, F.3    Moncada, S.4
  • 36
  • 37
    • 0015319592 scopus 로고
    • The biological clock: The mitochondria?
    • Harman, D. (1972). The biological clock: the mitochondria? J. Am. Geriatr. Soc. 20, 145-147.
    • (1972) J. Am. Geriatr. Soc. , vol.20 , pp. 145-147
    • Harman, D.1
  • 38
    • 0037470539 scopus 로고    scopus 로고
    • Genetics and the specificity of the aging process
    • Hekimi, S. and Guarente, L. (2003). Genetics and the specificity of the aging process. Science 299, 1351-1354.
    • (2003) Science , vol.299 , pp. 1351-1354
    • Hekimi, S.1    Guarente, L.2
  • 40
    • 33645086130 scopus 로고    scopus 로고
    • Reactive oxygen species in cardiac signaling: From mitochondria to plasma membrane ion channels
    • Hool, L. C. (2006). Reactive oxygen species in cardiac signaling: from mitochondria to plasma membrane ion channels. Clin. Exp. Pharmacol. Physiol. 33, 146-151.
    • (2006) Clin. Exp. Pharmacol. Physiol. , vol.33 , pp. 146-151
    • Hool, L.C.1
  • 41
    • 0036840502 scopus 로고    scopus 로고
    • High osmolarity extends life span in Saccharomyces cerevisiae by a mechanism related to calorie restriction
    • Kaeberlein, M., Andalis, A. A., Fink, G. R. and Guarente, L. (2002). High osmolarity extends life span in Saccharomyces cerevisiae by a mechanism related to calorie restriction. Mol. Cell. Biol. 22, 8056-8066.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8056-8066
    • Kaeberlein, M.1    Andalis, A.A.2    Fink, G.R.3    Guarente, L.4
  • 43
    • 0026197038 scopus 로고
    • Scanning electron microscopic observations on muscle cells of experimental mitochondrial myopathy produced by 2,4-dinitrophenol
    • Kawahara, H., Houdou, S. and Inoue, T. (1991). Scanning electron microscopic observations on muscle cells of experimental mitochondrial myopathy produced by 2,4-dinitrophenol. J. Submicrosc. Cytol. Pathol. 23, 397-403.
    • (1991) J. Submicrosc. Cytol. Pathol. , vol.23 , pp. 397-403
    • Kawahara, H.1    Houdou, S.2    Inoue, T.3
  • 44
    • 1542373685 scopus 로고    scopus 로고
    • Transcriptional regulatory circuits controlling mitochondrial biogenesis and function
    • Kelly, D. P. and Scarpulla, R. C. (2004). Transcriptional regulatory circuits controlling mitochondrial biogenesis and function. Genes Dev. 15, 357-368.
    • (2004) Genes Dev. , vol.15 , pp. 357-368
    • Kelly, D.P.1    Scarpulla, R.C.2
  • 45
    • 0031031148 scopus 로고    scopus 로고
    • Nitric oxide protects cultured rat hepatocytes from tumor necrosis factor-α-induced apoptosis by inducing heat shock protein 70 expression
    • Kim, Y. M., de Vera, M. E., Watkins, S. C. and Billiar, T. R. (1997). Nitric oxide protects cultured rat hepatocytes from tumor necrosis factor-α-induced apoptosis by inducing heat shock protein 70 expression. J. Biol. Chem. 272, 1402-1411.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1402-1411
    • Kim, Y.M.1    de Vera, M.E.2    Watkins, S.C.3    Billiar, T.R.4
  • 46
    • 0025861442 scopus 로고
    • The uncoupling protein UCP: A mambraneous mitochondrial ion carrier exclusively expressed in brown adipose tissue
    • Klaus, S., Casteilla, L., Bouillaud, F. and Ricquier, D. (1991). The uncoupling protein UCP: a mambraneous mitochondrial ion carrier exclusively expressed in brown adipose tissue. Int. J. Biochem. 23, 791-801.
    • (1991) Int. J. Biochem. , vol.23 , pp. 791-801
    • Klaus, S.1    Casteilla, L.2    Bouillaud, F.3    Ricquier, D.4
  • 48
    • 0028865142 scopus 로고
    • Expression of the mitochondrial uncoupling protein gene from the aP2 gene promoter prevents genetic obesity
    • Kopecky, J., Clarke, G., Enerback, S., Spiegelman, B. M. and Kozak, L. P. (1995). Expression of the mitochondrial uncoupling protein gene from the aP2 gene promoter prevents genetic obesity. J. Clin. Invest. 96, 2914-2923.
    • (1995) J. Clin. Invest. , vol.96 , pp. 2914-2923
    • Kopecky, J.1    Clarke, G.2    Enerback, S.3    Spiegelman, B.M.4    Kozak, L.P.5
  • 51
    • 0346731072 scopus 로고    scopus 로고
    • Nitric oxide and cell signaling: Modulation of redox tone and protein modification
    • Landar, A. and Darley-Usmar, V. M. (2003). Nitric oxide and cell signaling: modulation of redox tone and protein modification. Amino Acids 25, 313-321.
    • (2003) Amino Acids , vol.25 , pp. 313-321
    • Landar, A.1    Darley-Usmar, V.M.2
  • 54
    • 0033803048 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor γ coactivator-1 promotes cardiac mitochondrial biogenesis
    • Lehman, J. J., Barger, P. M., Kovacs, A., Saffitz, J. E., Medeiros, D. M. and Kelly, D. P. (2000). Peroxisome proliferator-activated receptor γ coactivator-1 promotes cardiac mitochondrial biogenesis. J. Clin. Invest. 106, 847-856.
    • (2000) J. Clin. Invest. , vol.106 , pp. 847-856
    • Lehman, J.J.1    Barger, P.M.2    Kovacs, A.3    Saffitz, J.E.4    Medeiros, D.M.5    Kelly, D.P.6
  • 57
    • 24144463983 scopus 로고    scopus 로고
    • Metabolic control through the PGC-1 family transcription coactivators
    • Lin, J., Handschin, C. and Spiegelman, B. M. (2005). Metabolic control through the PGC-1 family transcription coactivators. Cell Metab. 1, 361-370.
    • (2005) Cell Metab. , vol.1 , pp. 361-370
    • Lin, J.1    Handschin, C.2    Spiegelman, B.M.3
  • 58
    • 0034703217 scopus 로고    scopus 로고
    • Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae
    • Lin, S. J., Defossez, P. A. and Guarente, L. (2000). Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae. Science 289, 2126-2128.
    • (2000) Science , vol.289 , pp. 2126-2128
    • Lin, S.J.1    Defossez, P.A.2    Guarente, L.3
  • 59
    • 0347128279 scopus 로고    scopus 로고
    • Calorie restriction extends yeast life span by lowering the level of NADH
    • Lin, S. J., Ford, E., Haigis, M., Liszt, G. and Guarente, L. (2004). Calorie restriction extends yeast life span by lowering the level of NADH. Genes Dev. 18, 12-16.
    • (2004) Genes Dev. , vol.18 , pp. 12-16
    • Lin, S.J.1    Ford, E.2    Haigis, M.3    Liszt, G.4    Guarente, L.5
  • 61
    • 0034611678 scopus 로고    scopus 로고
    • Towards a molecular understanding of adaptive thermogenesis
    • Lowell, B. B. and Spiegelman, B. M. (2000). Towards a molecular understanding of adaptive thermogenesis. Nature 404, 652-660.
    • (2000) Nature , vol.404 , pp. 652-660
    • Lowell, B.B.1    Spiegelman, B.M.2
  • 62
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2α promotes cell survival under stress
    • Luo, J., Nikolaev, A. Y., Imai, S., Chen, D., Su, F., Shiloh, A., Guarente, L. and Gu, W. (2001). Negative control of p53 by Sir2α promotes cell survival under stress. Cell 107, 137-148.
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3    Chen, D.4    Su, F.5    Shiloh, A.6    Guarente, L.7    Gu, W.8
  • 63
    • 0031081742 scopus 로고    scopus 로고
    • Reconsidering mitochondrial structure: New views of an old organelle
    • Mannella, C. A., Marko, M. and Buttle, K. (1997). Reconsidering mitochondrial structure: new views of an old organelle. Trends Biochem. Sci. 22, 37-38.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 37-38
    • Mannella, C.A.1    Marko, M.2    Buttle, K.3
  • 65
    • 0141611988 scopus 로고    scopus 로고
    • Subfield history: Caloric restriction, slowing aging, and extending life
    • Masoro, E. J. (2003). Subfield history: caloric restriction, slowing aging, and extending life. Sci. Aging Knowledge Environ. 8, RE2.
    • (2003) Sci. Aging Knowledge Environ. , vol.8
    • Masoro, E.J.1
  • 66
    • 0033214039 scopus 로고    scopus 로고
    • The bioenergetics of brown fat mitochondria from UCP1-ablated mice. Ucp1 is not involved in fatty acid-induced de-energization ("uncoupling")
    • Matthias, A., Jacobsson, A., Cannon, B. and Nedergaard, J. (1999). The bioenergetics of brown fat mitochondria from UCP1-ablated mice. Ucp1 is not involved in fatty acid-induced de-energization ("uncoupling"). J. Biol. Chem. 274, 28150-28160.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28150-28160
    • Matthias, A.1    Jacobsson, A.2    Cannon, B.3    Nedergaard, J.4
  • 67
    • 0028033934 scopus 로고
    • An oligomeric protein is imported into peroxisomes in vivo
    • McNew, J. A. and Goodman, J. M. (1994). An oligomeric protein is imported into peroxisomes in vivo. J. Cell Biol. 127, 1245-1257.
    • (1994) J. Cell Biol. , vol.127 , pp. 1245-1257
    • McNew, J.A.1    Goodman, J.M.2
  • 68
    • 4544378532 scopus 로고    scopus 로고
    • Mitochondrial fusion intermediates revealed in vitro
    • Meeusen, S., McCaffery, J. M. and Nunnari, J. (2004). Mitochondrial fusion intermediates revealed in vitro. Science 305, 1747-1752.
    • (2004) Science , vol.305 , pp. 1747-1752
    • Meeusen, S.1    McCaffery, J.M.2    Nunnari, J.3
  • 69
    • 33746819399 scopus 로고
    • David Keilin's respiratory chain concept and its chemiosmotic consequences
    • In (ed. S. Forsén), Singapore: World Scientific Publishing Company
    • Mitchell, P. (1993). David Keilin's respiratory chain concept and its chemiosmotic consequences. In Nobel Lectures in Chemistry 1971-1980 (ed. S. Forsén), pp. 295-332. Singapore: World Scientific Publishing Company.
    • (1993) Nobel Lectures in Chemistry 1971-1980 , pp. 295-332
    • Mitchell, P.1
  • 70
    • 0025883342 scopus 로고
    • Nitric oxide: Physiology, pathophysiology, and pharmacology
    • Moncada, S., Palmer, R. M. and Higgs, E. A. (1991). Nitric oxide: physiology, pathophysiology, and pharmacology. Pharmacol. Rev. 43, 109-142.
    • (1991) Pharmacol. Rev. , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.2    Higgs, E.A.3
  • 73
    • 0022641657 scopus 로고
    • Activation of mitochondrial ATPase as evidence of loosely coupled oxidative phosphorylation in various skeletal muscle disorders. A histochemical fine-structural study
    • Muller-Hocker, J., Pongratz, D. and Hubner, G. (1986). Activation of mitochondrial ATPase as evidence of loosely coupled oxidative phosphorylation in various skeletal muscle disorders. A histochemical fine-structural study. J. Neurol. Sci. 74, 199-213.
    • (1986) J. Neurol. Sci. , vol.74 , pp. 199-213
    • Muller-Hocker, J.1    Pongratz, D.2    Hubner, G.3
  • 74
    • 0242663915 scopus 로고    scopus 로고
    • 2+- and redox-dependent production of nitric oxide
    • 2+- and redox-dependent production of nitric oxide. J. Immunol. 171, 5188-5197.
    • (2003) J. Immunol. , vol.171 , pp. 5188-5197
    • Nagy, G.1    Koncz, A.2    Perl, A.3
  • 78
    • 0035283207 scopus 로고    scopus 로고
    • UCP1: The only protein able to mediate adaptive non-shivering thermogenesis and metabolic inefficiency
    • Nedergaard, J., Golozoubova, V., Matthias, A., Asadi, A., Jacobsson, A. and Cannon, B. (2001). UCP1: the only protein able to mediate adaptive non-shivering thermogenesis and metabolic inefficiency. Biochim. Biophys. Acta 1504, 82-106.
    • (2001) Biochim. Biophys. Acta , vol.1504 , pp. 82-106
    • Nedergaard, J.1    Golozoubova, V.2    Matthias, A.3    Asadi, A.4    Jacobsson, A.5    Cannon, B.6
  • 79
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert, W. (1997). Protein import into mitochondria. Annu. Rev. Biochem. 66, 863-917.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 80
    • 0036343904 scopus 로고    scopus 로고
    • The protein import motor of mitochondria
    • Neupert, W. and Brunner, M. (2002). The protein import motor of mitochondria. Nat. Rev. Mol. Cell Biol. 3, 555-565.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 555-565
    • Neupert, W.1    Brunner, M.2
  • 81
    • 0034769244 scopus 로고    scopus 로고
    • Protective effects of noradrenaline against tumor necrosis factor-α-induced apoptosis in cultured rat brown adipocytes: Role of nitric oxide-induced heat shock protein 70 expression
    • Nisoli, E., Regianini, L., Bulbarelli, A., Briscini, L., Bracale, R. and Carruba, M. O. (2001). Protective effects of noradrenaline against tumor necrosis factor-α-induced apoptosis in cultured rat brown adipocytes: role of nitric oxide-induced heat shock protein 70 expression. Int. J. Obes. Relat. Metab. Disord. 25, 1421-1430.
    • (2001) Int. J. Obes. Relat. Metab. Disord. , vol.25 , pp. 1421-1430
    • Nisoli, E.1    Regianini, L.2    Bulbarelli, A.3    Briscini, L.4    Bracale, R.5    Carruba, M.O.6
  • 85
    • 0030841103 scopus 로고    scopus 로고
    • Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA
    • Nunnari, J., Marshall, W. F., Straight, A., Murray, A., Sedat, J. W. and Walter, P. (1997). Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA. Mol. Biol. Cell 8, 1233-1242.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1233-1242
    • Nunnari, J.1    Marshall, W.F.2    Straight, A.3    Murray, A.4    Sedat, J.W.5    Walter, P.6
  • 86
    • 27544466847 scopus 로고    scopus 로고
    • Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes
    • Okamoto, K. and Shaw, J. M. (2005). Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes. Annu. Rev. Genet. 39, 503-536.
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 503-536
    • Okamoto, K.1    Shaw, J.M.2
  • 87
    • 28744457235 scopus 로고    scopus 로고
    • Nuclear hormone receptors, metabolism, and aging: What goes around comes around. Transcription factors link lipid metabolism and aging-related processes
    • Pardee, K., Reinking, J. and Krause, H. (2004). Nuclear hormone receptors, metabolism, and aging: what goes around comes around. Transcription factors link lipid metabolism and aging-related processes. Sci. Aging Knowledge Environ. 47, re8.
    • (2004) Sci. Aging Knowledge Environ. , vol.47
    • Pardee, K.1    Reinking, J.2    Krause, H.3
  • 93
    • 0842302344 scopus 로고    scopus 로고
    • Mitochondrial morphology is dynamic and varied
    • Rube, D. A. and van der Bliek, A. M. (2004). Mitochondrial morphology is dynamic and varied. Mol. Cell. Biochem. 256/257, 331-339.
    • (2004) Mol. Cell. Biochem. , vol.256-257 , pp. 331-339
    • Rube, D.A.1    van der Bliek, A.M.2
  • 94
    • 0033529656 scopus 로고    scopus 로고
    • Perspectives on oxygen sensing
    • Semenza, G. L. (1999). Perspectives on oxygen sensing. Cell 98, 281-284.
    • (1999) Cell , vol.98 , pp. 281-284
    • Semenza, G.L.1
  • 95
    • 0031736354 scopus 로고    scopus 로고
    • Ultrastructural study of mitochondria and their cristae in embryonic rats and primate (N. nemistrina)
    • Shepard, T. H., Muffley, L. A. and Smith, L. T. (1998). Ultrastructural study of mitochondria and their cristae in embryonic rats and primate (N. nemistrina). Anat. Rec. 252, 383-392.
    • (1998) Anat. Rec. , vol.252 , pp. 383-392
    • Shepard, T.H.1    Muffley, L.A.2    Smith, L.T.3
  • 96
    • 31944452442 scopus 로고    scopus 로고
    • Mitochondrial transfer between cells can rescue aerobic respiration
    • Spees, J. L., Olson, S. D., Whitney, M. J. and Prockop, D. J. (2006). Mitochondrial transfer between cells can rescue aerobic respiration. Proc. Natl. Acad. Sci. USA 103, 1283-1288.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 1283-1288
    • Spees, J.L.1    Olson, S.D.2    Whitney, M.J.3    Prockop, D.J.4
  • 97
    • 0035139227 scopus 로고    scopus 로고
    • Physiology of nitric oxide in skeletal muscle
    • Stamler, J. S. and Meissner, G. (2001). Physiology of nitric oxide in skeletal muscle. Physiol. Rev. 81, 209-237.
    • (2001) Physiol. Rev. , vol.81 , pp. 209-237
    • Stamler, J.S.1    Meissner, G.2
  • 100
    • 0021071725 scopus 로고
    • Diazepam inhibits cell respiration and induces fragmentation of mitochondrial reticulum
    • Vorobjev, I. A. and Zorov, D. B. (1983). Diazepam inhibits cell respiration and induces fragmentation of mitochondrial reticulum. FEBS Lett. 163, 311-314.
    • (1983) FEBS Lett. , vol.163 , pp. 311-314
    • Vorobjev, I.A.1    Zorov, D.B.2
  • 101
    • 12444279265 scopus 로고
    • On the origin of cancer cells
    • Warburg, O. (1956). On the origin of cancer cells. Science 123, 309-314.
    • (1956) Science , vol.123 , pp. 309-314
    • Warburg, O.1
  • 102
    • 33646508129 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinases by lysophosphatidylcholine-induced mitochondrial reactive oxygen species generation in endothelial cells
    • Watanabe, N., Zmijewski, J. W., Takabe, W., Umezu-Goto, M., Le Goffe, C., Sekine, A., Landar, A., Watanabe, A., Aoki, J., Arai, H. et al. (2006). Activation of mitogen-activated protein kinases by lysophosphatidylcholine-induced mitochondrial reactive oxygen species generation in endothelial cells. Am. J. Pathol. 168, 1737-1748.
    • (2006) Am. J. Pathol. , vol.168 , pp. 1737-1748
    • Watanabe, N.1    Zmijewski, J.W.2    Takabe, W.3    Umezu-Goto, M.4    Le Goffe, C.5    Sekine, A.6    Landar, A.7    Watanabe, A.8    Aoki, J.9    Arai, H.10
  • 103
    • 28544442609 scopus 로고    scopus 로고
    • Protein translocation across biological membranes
    • Wickner, W. and Schekman, R. (2005). Protein translocation across biological membranes. Science 310, 1452-1456.
    • (2005) Science , vol.310 , pp. 1452-1456
    • Wickner, W.1    Schekman, R.2
  • 104
    • 22444433668 scopus 로고    scopus 로고
    • Oxidant and redox signaling in vascular oxygen sensing mechanisms: Basic concepts, current controversies, and potential importance of cytosolic NADPH
    • Wolin, M. S., Ahmad, M. and Gupte, S. A. (2005). Oxidant and redox signaling in vascular oxygen sensing mechanisms: basic concepts, current controversies, and potential importance of cytosolic NADPH. Am. J. Physiol. Lung Cell. Mol. Physiol. 289, L159-L173.
    • (2005) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.289
    • Wolin, M.S.1    Ahmad, M.2    Gupte, S.A.3
  • 105
    • 0032848295 scopus 로고    scopus 로고
    • Biochemical characterization of S-nitrosohemoglobin. Mechanisms underlying synthesis, no release, and biological activity
    • Wolzt, M., MacAllister, R. J., Davis, D., Feelisch, M., Moncada, S., Vallance, P. and Hobbs, A. J. (1999). Biochemical characterization of S-nitrosohemoglobin. Mechanisms underlying synthesis, no release, and biological activity. J. Biol. Chem. 274, 28983-28990.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28983-28990
    • Wolzt, M.1    MacAllister, R.J.2    Davis, D.3    Feelisch, M.4    Moncada, S.5    Vallance, P.6    Hobbs, A.J.7
  • 106
    • 0038481091 scopus 로고    scopus 로고
    • The cutting edge of mitochondrial fusion
    • Yaffe, M. P. (2003). The cutting edge of mitochondrial fusion. Nat. Cell Biol. 5, 497-499.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 497-499
    • Yaffe, M.P.1
  • 108
    • 29444433392 scopus 로고    scopus 로고
    • 2+ signals?
    • 2+ signals? Sci. STKE 280, pe18.
    • (2005) Sci. STKE , vol.280
    • Yoon, Y.1


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