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Volumn 59, Issue 8, 2007, Pages 729-738

Delivery of drugs and macromolecules to mitochondria

Author keywords

Lipophilic cations; Membrane insertion; Mitochondrial disease; Mitochondrial DNA; Protein and RNA import; Translocators

Indexed keywords

APOPTOTIC PATHWAY; ENERGY PRODUCTION; MITOCHONDRIA; MITOCHONDRIAL FUNCTION;

EID: 34548240181     PISSN: 0169409X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.addr.2007.06.004     Document Type: Review
Times cited : (55)

References (90)
  • 2
    • 0343986284 scopus 로고    scopus 로고
    • Drug delivery to mitochondria: the key to mitochondrial medicine
    • Murphy M.P., and Smith R.A. Drug delivery to mitochondria: the key to mitochondrial medicine. Adv. Drug Deliv. Rev. 41 (2000) 235-250
    • (2000) Adv. Drug Deliv. Rev. , vol.41 , pp. 235-250
    • Murphy, M.P.1    Smith, R.A.2
  • 3
    • 33847071146 scopus 로고    scopus 로고
    • Targeting antioxidants to mitochondria by conjugation to lipophilic cations
    • Murphy M.P., and Smith R.A. Targeting antioxidants to mitochondria by conjugation to lipophilic cations. Annu. Rev. Pharmacol. Toxicol. 47 (2007) 629-656
    • (2007) Annu. Rev. Pharmacol. Toxicol. , vol.47 , pp. 629-656
    • Murphy, M.P.1    Smith, R.A.2
  • 4
    • 33847618832 scopus 로고    scopus 로고
    • Mitochondrial drug delivery and mitochondrial disease therapy - an approach to liposome-based delivery targeted to mitochondria
    • Yamada Y., Akita H., Kogure K., Kamiya H., and Harashima H. Mitochondrial drug delivery and mitochondrial disease therapy - an approach to liposome-based delivery targeted to mitochondria. Mitochondrion 7 (2007) 63-71
    • (2007) Mitochondrion , vol.7 , pp. 63-71
    • Yamada, Y.1    Akita, H.2    Kogure, K.3    Kamiya, H.4    Harashima, H.5
  • 5
    • 33748494877 scopus 로고    scopus 로고
    • Liposomes and liposome-like vesicles for drug and DNA delivery to mitochondria
    • Weissig V., Boddapati S.V., Cheng S.M., and D'Souza G.G. Liposomes and liposome-like vesicles for drug and DNA delivery to mitochondria. J. Liposome Res. 16 (2006) 249-264
    • (2006) J. Liposome Res. , vol.16 , pp. 249-264
    • Weissig, V.1    Boddapati, S.V.2    Cheng, S.M.3    D'Souza, G.G.4
  • 6
    • 33748126226 scopus 로고    scopus 로고
    • Recent approaches to intracellular delivery of drugs and DNA and organelle targeting
    • Torchilin V.P. Recent approaches to intracellular delivery of drugs and DNA and organelle targeting. Annu. Rev. Biomed. Eng. 8 (2006) 343-375
    • (2006) Annu. Rev. Biomed. Eng. , vol.8 , pp. 343-375
    • Torchilin, V.P.1
  • 7
    • 33846022731 scopus 로고    scopus 로고
    • Mitochondrial disease- its impact, etiology, and pathology
    • McFarland R., Taylor R.W., and Turnbull D.M. Mitochondrial disease- its impact, etiology, and pathology. Curr. Top. Dev. Biol. 77 (2007) 113-155
    • (2007) Curr. Top. Dev. Biol. , vol.77 , pp. 113-155
    • McFarland, R.1    Taylor, R.W.2    Turnbull, D.M.3
  • 8
    • 17744393686 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations in human disease
    • Taylor R.W., and Turnbull D.M. Mitochondrial DNA mutations in human disease. Nat. Rev., Genet. 6 (2005) 389-402
    • (2005) Nat. Rev., Genet. , vol.6 , pp. 389-402
    • Taylor, R.W.1    Turnbull, D.M.2
  • 9
    • 0027210411 scopus 로고
    • Current issues in the chemistry of cytochrome c oxidase
    • Palmer G. Current issues in the chemistry of cytochrome c oxidase. J. Bioenerg. Biomembranes 25 (1993) 145-151
    • (1993) J. Bioenerg. Biomembranes , vol.25 , pp. 145-151
    • Palmer, G.1
  • 10
    • 0033795824 scopus 로고    scopus 로고
    • In vivo control of respiration by cytochrome c oxidase in human cells
    • Villani G., and Attardi G. In vivo control of respiration by cytochrome c oxidase in human cells. Free Radic. Biol. Med. 29 (2000) 202-210
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 202-210
    • Villani, G.1    Attardi, G.2
  • 11
    • 0025608225 scopus 로고
    • The effect of carbon monoxide on respiration
    • Haab P. The effect of carbon monoxide on respiration. Experientia 46 (1990) 1202-1206
    • (1990) Experientia , vol.46 , pp. 1202-1206
    • Haab, P.1
  • 12
    • 0037424245 scopus 로고    scopus 로고
    • Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production
    • Li N., Ragheb K., Lawler G., Sturgis J., Rajwa B., Melendez J.A., and Robinson J.P. Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production. J. Biol. Chem. 278 (2003) 8516-8525
    • (2003) J. Biol. Chem. , vol.278 , pp. 8516-8525
    • Li, N.1    Ragheb, K.2    Lawler, G.3    Sturgis, J.4    Rajwa, B.5    Melendez, J.A.6    Robinson, J.P.7
  • 13
    • 33846005185 scopus 로고    scopus 로고
    • Influence on mitochondria and cytotoxicity of different antibiotics administered in high concentrations on primary human osteoblasts and cell lines
    • Duewelhenke N., Krut O., and Eysel P. Influence on mitochondria and cytotoxicity of different antibiotics administered in high concentrations on primary human osteoblasts and cell lines. Antimicrob. Agents Chemother. 51 (2007) 54-63
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 54-63
    • Duewelhenke, N.1    Krut, O.2    Eysel, P.3
  • 16
    • 34447558681 scopus 로고    scopus 로고
    • Interaction of the mitochondria-targeted antioxidant mitoq with phospholipid bilayers and ubiquinone oxidoreductases
    • James A.M., Sharpley M.S., Manas A.R., Frerman F.E., Hirst J., Smith R.A., and Murphy M.P. Interaction of the mitochondria-targeted antioxidant mitoq with phospholipid bilayers and ubiquinone oxidoreductases. J. Biol. Chem. 282 (2007) 14708-14718
    • (2007) J. Biol. Chem. , vol.282 , pp. 14708-14718
    • James, A.M.1    Sharpley, M.S.2    Manas, A.R.3    Frerman, F.E.4    Hirst, J.5    Smith, R.A.6    Murphy, M.P.7
  • 17
    • 21244448078 scopus 로고    scopus 로고
    • Synthesis and characterization of a triphenylphosphonium-conjugated peroxidase mimetic. Insights into the interaction of ebselen with mitochondria
    • Filipovska A., Kelso G.F., Brown S.E., Beer S.M., Smith R.A., and Murphy M.P. Synthesis and characterization of a triphenylphosphonium-conjugated peroxidase mimetic. Insights into the interaction of ebselen with mitochondria. J. Biol. Chem. 280 (2005) 24113-24126
    • (2005) J. Biol. Chem. , vol.280 , pp. 24113-24126
    • Filipovska, A.1    Kelso, G.F.2    Brown, S.E.3    Beer, S.M.4    Smith, R.A.5    Murphy, M.P.6
  • 18
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert W., and Herrmann J.M. Translocation of proteins into mitochondria. Annu. Rev. Biochem. 76 (2007) 723-749
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 19
    • 27844535385 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Mokranjac D., and Neupert W. Protein import into mitochondria. Biochem. Soc. Trans. 33 (2005) 1019-1023
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 1019-1023
    • Mokranjac, D.1    Neupert, W.2
  • 20
    • 2442555970 scopus 로고    scopus 로고
    • The protein import machinery of mitochondria
    • Wiedemann N., Frazier A.E., and Pfanner N. The protein import machinery of mitochondria. J. Biol. Chem. 279 (2004) 14473-14476
    • (2004) J. Biol. Chem. , vol.279 , pp. 14473-14476
    • Wiedemann, N.1    Frazier, A.E.2    Pfanner, N.3
  • 21
    • 33746575844 scopus 로고    scopus 로고
    • Evolution of the molecular machines for protein import into mitochondria
    • Dolezal, Likic V., Tachezy J., and Lithgow T. Evolution of the molecular machines for protein import into mitochondria. Science 313 (2006) 314-318
    • (2006) Science , vol.313 , pp. 314-318
    • Dolezal1    Likic, V.2    Tachezy, J.3    Lithgow, T.4
  • 22
    • 7544219638 scopus 로고    scopus 로고
    • New developments in mitochondrial assembly
    • Koehler C.M. New developments in mitochondrial assembly. Annu. Rev. Cell Dev. Biol. 20 (2004) 309-335
    • (2004) Annu. Rev. Cell Dev. Biol. , vol.20 , pp. 309-335
    • Koehler, C.M.1
  • 25
    • 33748084058 scopus 로고    scopus 로고
    • Mitochondrial disease: maintenance of mitochondrial genome and molecular diagnostics
    • Kang D., and Hamasaki N. Mitochondrial disease: maintenance of mitochondrial genome and molecular diagnostics. Adv. Clin. Chem. 42 (2006) 217-254
    • (2006) Adv. Clin. Chem. , vol.42 , pp. 217-254
    • Kang, D.1    Hamasaki, N.2
  • 26
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin M.T., and Beal M.F. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443 (2006) 787-795
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 27
    • 33745410626 scopus 로고    scopus 로고
    • Mitochondrial disease
    • Schapira A.H. Mitochondrial disease. Lancet 368 (2006) 70-82
    • (2006) Lancet , vol.368 , pp. 70-82
    • Schapira, A.H.1
  • 28
    • 33745274726 scopus 로고    scopus 로고
    • Mitochondria: dynamic organelles in disease, aging, and development
    • Chan D.C. Mitochondria: dynamic organelles in disease, aging, and development. Cell 125 (2006) 1241-1252
    • (2006) Cell , vol.125 , pp. 1241-1252
    • Chan, D.C.1
  • 29
    • 34247127747 scopus 로고    scopus 로고
    • Mitochondrial protein import and human health and disease
    • Mackenzi J.A., and Payne R.M. Mitochondrial protein import and human health and disease. Biochim. Biophys. Acta 1772 (2006) 509-523
    • (2006) Biochim. Biophys. Acta , vol.1772 , pp. 509-523
    • Mackenzi, J.A.1    Payne, R.M.2
  • 32
    • 33846008430 scopus 로고    scopus 로고
    • A novel recurrent mitochondrial DNA mutation in ND3 gene is associated with isolated complex I deficiency causing Leigh syndrome and dystonia
    • Sarzi E., Brown M.D., Lebon S., Chretien D., Munnich A., Rotig A., and Procaccio V. A novel recurrent mitochondrial DNA mutation in ND3 gene is associated with isolated complex I deficiency causing Leigh syndrome and dystonia. Am. J. Med. Genet. A 143 (2007) 33-41
    • (2007) Am. J. Med. Genet. A , vol.143 , pp. 33-41
    • Sarzi, E.1    Brown, M.D.2    Lebon, S.3    Chretien, D.4    Munnich, A.5    Rotig, A.6    Procaccio, V.7
  • 33
    • 33845353404 scopus 로고    scopus 로고
    • Mitochondriopathy in Parkinson disease and amyotrophic lateral sclerosis
    • Martin L.J. Mitochondriopathy in Parkinson disease and amyotrophic lateral sclerosis. J. Neuropathol. Exp. Neurol. 65 (2006) 1103-1110
    • (2006) J. Neuropathol. Exp. Neurol. , vol.65 , pp. 1103-1110
    • Martin, L.J.1
  • 34
    • 33750216506 scopus 로고    scopus 로고
    • Mitochondrial myopathies
    • DiMauro S. Mitochondrial myopathies. Curr. Opin. Rheumatol. 18 (2006) 636-641
    • (2006) Curr. Opin. Rheumatol. , vol.18 , pp. 636-641
    • DiMauro, S.1
  • 35
    • 0034523187 scopus 로고    scopus 로고
    • Mitochondria-dependent apoptosis and cellular pH regulation
    • Matsuyama S., and Reed J.C. Mitochondria-dependent apoptosis and cellular pH regulation. Cell Death Differ. 7 (2000) 1155-1165
    • (2000) Cell Death Differ. , vol.7 , pp. 1155-1165
    • Matsuyama, S.1    Reed, J.C.2
  • 36
    • 33746895175 scopus 로고    scopus 로고
    • Mitochondria as therapeutic targets for cancer chemotherapy
    • Galluzzi L., Larochette N., Zamzami N., and Kroemer G. Mitochondria as therapeutic targets for cancer chemotherapy. Oncogene 25 (2006) 4812-4830
    • (2006) Oncogene , vol.25 , pp. 4812-4830
    • Galluzzi, L.1    Larochette, N.2    Zamzami, N.3    Kroemer, G.4
  • 37
    • 33750619845 scopus 로고    scopus 로고
    • How do Bax and Bak lead to permeabilization of the outer mitochondrial membrane?
    • Antignani A., and Youle R.J. How do Bax and Bak lead to permeabilization of the outer mitochondrial membrane?. Curr. Opin. Cell Biol. 18 (2006) 685-689
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 685-689
    • Antignani, A.1    Youle, R.J.2
  • 38
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green D.R., and Kroemer G. The pathophysiology of mitochondrial cell death. Science 305 (2004) 626-629
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 39
    • 0042090307 scopus 로고    scopus 로고
    • BCL-2 selectively interacts with the BID-induced open conformer of BAK, inhibiting BAK auto-oligomerization
    • Ruffolo S.C., and Shore G.C. BCL-2 selectively interacts with the BID-induced open conformer of BAK, inhibiting BAK auto-oligomerization. J. Biol. Chem. 278 (2003) 25039-25045
    • (2003) J. Biol. Chem. , vol.278 , pp. 25039-25045
    • Ruffolo, S.C.1    Shore, G.C.2
  • 49
    • 33947388409 scopus 로고    scopus 로고
    • Mitochondrial ion channels
    • O'Rourke B. Mitochondrial ion channels. Annu. Rev. Physiol. 69 (2007) 19-49
    • (2007) Annu. Rev. Physiol. , vol.69 , pp. 19-49
    • O'Rourke, B.1
  • 50
    • 0036799548 scopus 로고    scopus 로고
    • Biphasic translocation of Bax to mitochondria
    • Capano M., and Crompton M. Biphasic translocation of Bax to mitochondria. Biochem. J. 367 (2002) 169-178
    • (2002) Biochem. J. , vol.367 , pp. 169-178
    • Capano, M.1    Crompton, M.2
  • 51
    • 0034681110 scopus 로고    scopus 로고
    • Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity
    • Shimizu S., and Tsujimoto Y. Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 577-582
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 577-582
    • Shimizu, S.1    Tsujimoto, Y.2
  • 53
    • 0036510541 scopus 로고    scopus 로고
    • Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis
    • Pastorino J.G., Shulga N., and Hoek J.B. Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis. J. Biol. Chem. 277 (2002) 7610-7618
    • (2002) J. Biol. Chem. , vol.277 , pp. 7610-7618
    • Pastorino, J.G.1    Shulga, N.2    Hoek, J.B.3
  • 54
    • 34247158550 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial dysfunction in neurodegenerative diseases
    • Trushina E., and McMurray C.T. Oxidative stress and mitochondrial dysfunction in neurodegenerative diseases. Neuroscience 145 (2007) 1233-1248
    • (2007) Neuroscience , vol.145 , pp. 1233-1248
    • Trushina, E.1    McMurray, C.T.2
  • 56
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge W. Free radicals in the physiological control of cell function. Physiol. Rev. 82 (2002) 47-95
    • (2002) Physiol. Rev. , vol.82 , pp. 47-95
    • Droge, W.1
  • 57
    • 0036570012 scopus 로고    scopus 로고
    • Repair of oxidative DNA damage in nuclear and mitochondrial DNA, and some changes with aging in mammalian cells
    • Bohr V.A. Repair of oxidative DNA damage in nuclear and mitochondrial DNA, and some changes with aging in mammalian cells. Free Radic. Biol. Med. 32 (2002) 804-812
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 804-812
    • Bohr, V.A.1
  • 58
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer H., Schaur R.J., and Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic. Biol. Med. 11 (1991) 81-128
    • (1991) Free Radic. Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 59
    • 0025911829 scopus 로고
    • Metal-catalyzed oxidation of proteins. Physiological consequences
    • Stadtman E.R., and Oliver C.N. Metal-catalyzed oxidation of proteins. Physiological consequences. J. Biol. Chem. 266 (1991) 2005-2008
    • (1991) J. Biol. Chem. , vol.266 , pp. 2005-2008
    • Stadtman, E.R.1    Oliver, C.N.2
  • 60
    • 33745617384 scopus 로고    scopus 로고
    • Mitochondrial DNA and ageing
    • Trifunovic A. Mitochondrial DNA and ageing. Biochim. Biophys. Acta 1757 (2006) 611-617
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 611-617
    • Trifunovic, A.1
  • 61
    • 0348136710 scopus 로고    scopus 로고
    • Mitochondria-targeted antioxidants protect Friedreich Ataxia fibroblasts from endogenous oxidative stress more effectively than untargeted antioxidants
    • Jauslin M.L., Meier T., Smith R.A., and Murphy M.P. Mitochondria-targeted antioxidants protect Friedreich Ataxia fibroblasts from endogenous oxidative stress more effectively than untargeted antioxidants. FASEB J. 17 (2003) 1972-1974
    • (2003) FASEB J. , vol.17 , pp. 1972-1974
    • Jauslin, M.L.1    Meier, T.2    Smith, R.A.3    Murphy, M.P.4
  • 62
    • 0021207554 scopus 로고
    • Membrane potential and surface potential in mitochondria: uptake and binding of lipophilic cations
    • Rottenberg H. Membrane potential and surface potential in mitochondria: uptake and binding of lipophilic cations. J. Membr. Biol. 81 (1984) 127-138
    • (1984) J. Membr. Biol. , vol.81 , pp. 127-138
    • Rottenberg, H.1
  • 64
    • 0024536726 scopus 로고
    • DNA-protein conjugates can enter mitochondria via the protein import pathway
    • Vestweber D., and Schatz G. DNA-protein conjugates can enter mitochondria via the protein import pathway. Nature 338 (1989) 170-172
    • (1989) Nature , vol.338 , pp. 170-172
    • Vestweber, D.1    Schatz, G.2
  • 65
    • 34247589241 scopus 로고    scopus 로고
    • Peptide nucleic acids with a structurally biased backbone: effects of conformational constraints and stereochemistry
    • Corradini R., Sforza S., Tedeschi T., Totsingan F., and Marchelli R. Peptide nucleic acids with a structurally biased backbone: effects of conformational constraints and stereochemistry. Curr. Top. Med. Chem. 7 (2007) 681-694
    • (2007) Curr. Top. Med. Chem. , vol.7 , pp. 681-694
    • Corradini, R.1    Sforza, S.2    Tedeschi, T.3    Totsingan, F.4    Marchelli, R.5
  • 66
    • 33845575774 scopus 로고    scopus 로고
    • Structural requirements for cellular uptake and antisense activity of peptide nucleic acids conjugated with various peptides
    • Wolf Y., Pritz S., Abes S., Bienert M., Lebleu B., and Oehlke J. Structural requirements for cellular uptake and antisense activity of peptide nucleic acids conjugated with various peptides. Biochemistry 45 (2006) 14944-14954
    • (2006) Biochemistry , vol.45 , pp. 14944-14954
    • Wolf, Y.1    Pritz, S.2    Abes, S.3    Bienert, M.4    Lebleu, B.5    Oehlke, J.6
  • 67
    • 0033374355 scopus 로고    scopus 로고
    • Lightowlers RN. Peptide nucleic acid delivery to human mitochondria
    • Chinnery P.F., Taylor R.W., Diekert K., Lill R., and Turnbull D.M. Lightowlers RN. Peptide nucleic acid delivery to human mitochondria. Gene Ther. 6 (1999) 1919-1928
    • (1999) Gene Ther. , vol.6 , pp. 1919-1928
    • Chinnery, P.F.1    Taylor, R.W.2    Diekert, K.3    Lill, R.4    Turnbull, D.M.5
  • 68
    • 0035339611 scopus 로고    scopus 로고
    • Targeting peptide nucleic acid (PNA) oligomers to mitochondria within cells by conjugation to lipophilic cations: implications for mitochondrial DNA replication, expression and disease
    • Muratovska A., Lightowlers R.N., Taylor R.W., Turnbull D.M., Smith R.A., Wilce J.A., Martin S.W., and Murphy M.P. Targeting peptide nucleic acid (PNA) oligomers to mitochondria within cells by conjugation to lipophilic cations: implications for mitochondrial DNA replication, expression and disease. Nucleic Acids Res. 29 (2001) 1852-1863
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1852-1863
    • Muratovska, A.1    Lightowlers, R.N.2    Taylor, R.W.3    Turnbull, D.M.4    Smith, R.A.5    Wilce, J.A.6    Martin, S.W.7    Murphy, M.P.8
  • 69
    • 23944464403 scopus 로고    scopus 로고
    • Bacterial signal peptide recognizes HeLa cell mitochondrial import receptors and functions as a mitochondrial leader sequence
    • Mukhopadhyay A., Ni L., Yang C.S., and Weiner H. Bacterial signal peptide recognizes HeLa cell mitochondrial import receptors and functions as a mitochondrial leader sequence. Cell. Mol. Life Sci. 62 (2005) 1890-1899
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 1890-1899
    • Mukhopadhyay, A.1    Ni, L.2    Yang, C.S.3    Weiner, H.4
  • 70
    • 13244259426 scopus 로고    scopus 로고
    • Targeting of enteropathogenic Escherichia coli EspF to host mitochondria is essential for bacterial pathogenesis: critical role of the 16th leucine residue in EspF
    • Nagai T., Abe A., and Sasakawa C. Targeting of enteropathogenic Escherichia coli EspF to host mitochondria is essential for bacterial pathogenesis: critical role of the 16th leucine residue in EspF. J. Biol. Chem. 280 (2005) 2998-3011
    • (2005) J. Biol. Chem. , vol.280 , pp. 2998-3011
    • Nagai, T.1    Abe, A.2    Sasakawa, C.3
  • 71
    • 0345732691 scopus 로고    scopus 로고
    • Ribosome binding to the Oxa1 complex facilitates co-translational protein insertion in mitochondria
    • Szyrach G., Ott M., Bonnefoy N., Neupert W., and Herrmann J.M. Ribosome binding to the Oxa1 complex facilitates co-translational protein insertion in mitochondria. EMBO J. 22 (2003) 6448-6457
    • (2003) EMBO J. , vol.22 , pp. 6448-6457
    • Szyrach, G.1    Ott, M.2    Bonnefoy, N.3    Neupert, W.4    Herrmann, J.M.5
  • 72
    • 4344581067 scopus 로고    scopus 로고
    • A co-translational model to explain the in vivo import of proteins into HeLa cell mitochondria
    • Mukhopadhyay A., Ni L., and Weiner H. A co-translational model to explain the in vivo import of proteins into HeLa cell mitochondria. Biochem. J. 382 (2004) 385-392
    • (2004) Biochem. J. , vol.382 , pp. 385-392
    • Mukhopadhyay, A.1    Ni, L.2    Weiner, H.3
  • 73
    • 33744986928 scopus 로고    scopus 로고
    • Factors that might affect the allotopic replacement of a damaged mitochondrial DNA-encoded protein
    • Mukhopadhyay A., Zullo S.J., and Weiner H. Factors that might affect the allotopic replacement of a damaged mitochondrial DNA-encoded protein. Rejuvenation Res. 9 (2006) 182-190
    • (2006) Rejuvenation Res. , vol.9 , pp. 182-190
    • Mukhopadhyay, A.1    Zullo, S.J.2    Weiner, H.3
  • 74
    • 0036840342 scopus 로고    scopus 로고
    • Mitochondrial import of the ADP/ATP carrier: the essential TIM complex of the intermembrane space is required for precursor release from the TOM complex
    • Truscot K.N., Wiedemann N., Rehling P., Muller H., Meisinger C., Pfanner N., and Guiard B. Mitochondrial import of the ADP/ATP carrier: the essential TIM complex of the intermembrane space is required for precursor release from the TOM complex. Mol. Cell. Biol. 22 (2002) 7780-7789
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7780-7789
    • Truscot, K.N.1    Wiedemann, N.2    Rehling, P.3    Muller, H.4    Meisinger, C.5    Pfanner, N.6    Guiard, B.7
  • 75
    • 0030908894 scopus 로고    scopus 로고
    • Insertion into the mitochondrial inner membrane of a polytopic protein, the nuclear-encoded Oxa1p
    • Herrmann J.M., Neupert W., and Stuart R.A. Insertion into the mitochondrial inner membrane of a polytopic protein, the nuclear-encoded Oxa1p. EMBO J. 16 (1997) 2217-2226
    • (1997) EMBO J. , vol.16 , pp. 2217-2226
    • Herrmann, J.M.1    Neupert, W.2    Stuart, R.A.3
  • 76
    • 0028981021 scopus 로고
    • Conservative sorting of F0-ATPase subunit 9: export from matrix requires delta pH across inner membrane and matrix ATP
    • Rojo E.E., Stuart R.A., and Neupert W. Conservative sorting of F0-ATPase subunit 9: export from matrix requires delta pH across inner membrane and matrix ATP. EMBO J. 14 (1995) 3445-3451
    • (1995) EMBO J. , vol.14 , pp. 3445-3451
    • Rojo, E.E.1    Stuart, R.A.2    Neupert, W.3
  • 77
    • 0024121557 scopus 로고
    • Assembly of functional proton-translocating ATPase complex in yeast mitochondria with cytoplasmically synthesized subunit 8, a polypeptide normally encoded within the organelle
    • Nagley P., Farrell L.B., Gearing D.P., Nero D., Meltzer S., and Devenish R.J. Assembly of functional proton-translocating ATPase complex in yeast mitochondria with cytoplasmically synthesized subunit 8, a polypeptide normally encoded within the organelle. Proc. Natl. Acad. Sci. 85 (1988) 2091-2095
    • (1988) Proc. Natl. Acad. Sci. , vol.85 , pp. 2091-2095
    • Nagley, P.1    Farrell, L.B.2    Gearing, D.P.3    Nero, D.4    Meltzer, S.5    Devenish, R.J.6
  • 78
    • 0036544631 scopus 로고    scopus 로고
    • Rescue of a deficiency in ATP synthesis by transfer of MTATP6, a mitochondrial DNA-encoded gene, to the nucleus
    • Manfredi G., Fu J., Ojaimi J., Sadlock J.E., Kwong J.Q., Guy J., and Schon E.A. Rescue of a deficiency in ATP synthesis by transfer of MTATP6, a mitochondrial DNA-encoded gene, to the nucleus. Nat. Genet. 30 (2002) 394-399
    • (2002) Nat. Genet. , vol.30 , pp. 394-399
    • Manfredi, G.1    Fu, J.2    Ojaimi, J.3    Sadlock, J.E.4    Kwong, J.Q.5    Guy, J.6    Schon, E.A.7
  • 79
    • 16844381561 scopus 로고    scopus 로고
    • Stable transformation of CHO Cells and human NARP cybrids confers oligomycin resistance (oli(r)) following transfer of a mitochondrial DNA-encoded oli(r) ATPase6 gene to the nuclear genome: a model system for mtDNA gene therapy
    • Zullo S.J., Parks W.T., Chloupkova M., Wei B., Weiner H., Fenton W.A., Eisenstadt J.M., and Merril C.R. Stable transformation of CHO Cells and human NARP cybrids confers oligomycin resistance (oli(r)) following transfer of a mitochondrial DNA-encoded oli(r) ATPase6 gene to the nuclear genome: a model system for mtDNA gene therapy. Rejuvenation Res. 8 (2005) 18-28
    • (2005) Rejuvenation Res. , vol.8 , pp. 18-28
    • Zullo, S.J.1    Parks, W.T.2    Chloupkova, M.3    Wei, B.4    Weiner, H.5    Fenton, W.A.6    Eisenstadt, J.M.7    Merril, C.R.8
  • 80
    • 0035894698 scopus 로고    scopus 로고
    • Manipulating mitochondrial DNA heteroplasmy by a mitochondrially targeted restriction endonuclease
    • Srivastava S., and Moraes C.T. Manipulating mitochondrial DNA heteroplasmy by a mitochondrially targeted restriction endonuclease. Hum. Mol. Genet. 10 (2001) 3039-3093
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 3039-3093
    • Srivastava, S.1    Moraes, C.T.2
  • 82
    • 0026563681 scopus 로고
    • In vivo import of a normal or mutagenized heterologous transfer RNA into the mitochondria of transgenic plants: towards novel ways of influencing mitochondrial gene expression
    • Small I., Marechal-Drouard L., Masson J., Pelletier G., Cosset A., Weil J.H., and Dietrich A. In vivo import of a normal or mutagenized heterologous transfer RNA into the mitochondria of transgenic plants: towards novel ways of influencing mitochondrial gene expression. EMBO J. 11 (1992) 1291-1296
    • (1992) EMBO J. , vol.11 , pp. 1291-1296
    • Small, I.1    Marechal-Drouard, L.2    Masson, J.3    Pelletier, G.4    Cosset, A.5    Weil, J.H.6    Dietrich, A.7
  • 83
    • 0037954522 scopus 로고    scopus 로고
    • In vitro import of a nuclearly encoded tRNA into mitochondria of Solanum tuberosum
    • Delage L., Dietrich A., Cosset A., and Marechal-Drouard L. In vitro import of a nuclearly encoded tRNA into mitochondria of Solanum tuberosum. Mol. Cell. Biol. 23 (2003) 4000-4012
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4000-4012
    • Delage, L.1    Dietrich, A.2    Cosset, A.3    Marechal-Drouard, L.4
  • 84
    • 0038129639 scopus 로고    scopus 로고
    • The anticodon and the D-domain sequences are essential determinants for plant cytosolic tRNAVal import into mitochondria
    • Delage L., Duchene A.M., Zaepfel M., and Marechal-Drouard L. The anticodon and the D-domain sequences are essential determinants for plant cytosolic tRNAVal import into mitochondria. Plant J. 34 (2003) 623-633
    • (2003) Plant J. , vol.34 , pp. 623-633
    • Delage, L.1    Duchene, A.M.2    Zaepfel, M.3    Marechal-Drouard, L.4
  • 85
    • 0029155450 scopus 로고
    • tRNAs are imported into mitochondria of Trypanosoma brucei independently of their genomic context and genetic origin
    • Hauser R., and Schneider A. tRNAs are imported into mitochondria of Trypanosoma brucei independently of their genomic context and genetic origin. EMBO J. 14 (1995) 4212-4220
    • (1995) EMBO J. , vol.14 , pp. 4212-4220
    • Hauser, R.1    Schneider, A.2
  • 86
    • 0141940264 scopus 로고    scopus 로고
    • Allosteric regulation of tRNA import: interactions between tRNA domains at the inner membrane of Leishmania mitochondria
    • Goswami S., Chatterjee S., Bhattacharyya S.N., Basu S., and Adhya S. Allosteric regulation of tRNA import: interactions between tRNA domains at the inner membrane of Leishmania mitochondria. Nucleic Acids Res. 31 (2003) 5552-5559
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5552-5559
    • Goswami, S.1    Chatterjee, S.2    Bhattacharyya, S.N.3    Basu, S.4    Adhya, S.5
  • 88
    • 33750314614 scopus 로고    scopus 로고
    • Functional delivery of a cytosolic tRNA into mutant mitochondria of human cells
    • Mahata B., Mukherjee S., Mishra S., Bandyopadhyay A., and Adhya S. Functional delivery of a cytosolic tRNA into mutant mitochondria of human cells. Science 314 (2006) 471-474
    • (2006) Science , vol.314 , pp. 471-474
    • Mahata, B.1    Mukherjee, S.2    Mishra, S.3    Bandyopadhyay, A.4    Adhya, S.5
  • 89
    • 0037245651 scopus 로고    scopus 로고
    • A new connection: chaperones meet a mitochondrial receptor
    • Voos W. A new connection: chaperones meet a mitochondrial receptor. Mol. Cell 11 (2003) 1-3
    • (2003) Mol. Cell , vol.11 , pp. 1-3
    • Voos, W.1
  • 90
    • 33746924468 scopus 로고    scopus 로고
    • Hexokinase II: cancer's double-edged sword acting as both facilitator and gatekeeper of malignancy when bound to mitochondria
    • Mathupala S.P., Ko Y.H., and Pedersen P.L. Hexokinase II: cancer's double-edged sword acting as both facilitator and gatekeeper of malignancy when bound to mitochondria. Oncogene 25 (2006) 4777-4786
    • (2006) Oncogene , vol.25 , pp. 4777-4786
    • Mathupala, S.P.1    Ko, Y.H.2    Pedersen, P.L.3


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