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Volumn 51, Issue 5, 2010, Pages 451-461

The approaches for manipulating mitochondrial proteome

Author keywords

Mitochondrial manipulation; Mitochondrial proteome; Protein targeting; Protein therapy

Indexed keywords

CARRIER PROTEIN; GENE PRODUCT; MITOCHONDRIAL PROTEIN; NUCLEAR PROTEIN; PROTEOME;

EID: 77953530666     PISSN: 08936692     EISSN: 10982280     Source Type: Journal    
DOI: 10.1002/em.20570     Document Type: Review
Times cited : (10)

References (99)
  • 1
    • 40949145581 scopus 로고    scopus 로고
    • Selective elimination of mutant mitochondrial genomes as therapeutic strategy for the treatment of NARP and MILS syndromes
    • Alexeyev MF, Venediktova N, Pastukh V, Shokolenko I, Bonilla G, Wilson GL. 2008. Selective elimination of mutant mitochondrial genomes as therapeutic strategy for the treatment of NARP and MILS syndromes. Gene Ther 15:516-523.
    • (2008) Gene Ther , vol.15 , pp. 516-523
    • Alexeyev, M.F.1    Venediktova, N.2    Pastukh, V.3    Shokolenko, I.4    Bonilla, G.5    Wilson, G.L.6
  • 2
    • 70349467827 scopus 로고    scopus 로고
    • Mitochondrial tRNA import - The challenge to understand has just begun
    • Alfonzo JD, Soll D. 2009. Mitochondrial tRNA import - The challenge to understand has just begun. Biol Chem 390:717-722.
    • (2009) Biol Chem , vol.390 , pp. 717-722
    • Alfonzo, J.D.1    Soll, D.2
  • 3
    • 34247872941 scopus 로고    scopus 로고
    • Transduction of anti-cell death protein FNK protects isolated rat hearts from myocardial infarction induced by ischemia/reperfusion
    • Arakawa M, Yasutake M, Miyamoto M, Takano T, Asoh S, Ohta S. 2007. Transduction of anti-cell death protein FNK protects isolated rat hearts from myocardial infarction induced by ischemia/reperfusion. Life Sci 80:2076-2084.
    • (2007) Life Sci , vol.80 , pp. 2076-2084
    • Arakawa, M.1    Yasutake, M.2    Miyamoto, M.3    Takano, T.4    Asoh, S.5    Ohta, S.6
  • 6
    • 0035914437 scopus 로고    scopus 로고
    • Lack of complex I activity in human cells carrying a mutation in MtDNA-encoded ND4 subunit is corrected by the Saccharomyces cerevisiae NADH-quinone oxidoreductase (NDI1) gene
    • Bai Y, Hajek P, Chomyn A, Chan E, Seo BB, Matsuno-Yagi A, Yagi T, Attardi G. 2001. Lack of complex I activity in human cells carrying a mutation in MtDNA-encoded ND4 subunit is corrected by the Saccharomyces cerevisiae NADH-quinone oxidoreductase (NDI1) gene. J Biol Chem 276:38808-38813.
    • (2001) J Biol Chem , vol.276 , pp. 38808-38813
    • Bai, Y.1    Hajek, P.2    Chomyn, A.3    Chan, E.4    Seo, B.B.5    Matsuno-Yagi, A.6    Yagi, T.7    Attardi, G.8
  • 7
    • 22044432479 scopus 로고    scopus 로고
    • Restoration of mitochondrial function in cells with complex I deficiency
    • Bai Y, Park JS, Deng JH, Li Y, Hu P. 2005. Restoration of mitochondrial function in cells with complex I deficiency. Ann NY Acad Sci 1042:25-35.
    • (2005) Ann NY Acad Sci , vol.1042 , pp. 25-35
    • Bai, Y.1    Park, J.S.2    Deng, J.H.3    Li, Y.4    Hu, P.5
  • 9
    • 33744795591 scopus 로고    scopus 로고
    • The complexity of mitochondrial tRNA import
    • Bhattacharyya SN, Adhya S. 2004. The complexity of mitochondrial tRNA import. RNA Biol 1:84-88.
    • (2004) RNA Biol , vol.1 , pp. 84-88
    • Bhattacharyya, S.N.1    Adhya, S.2
  • 10
    • 33846226670 scopus 로고    scopus 로고
    • Expression of algal nuclear ATP synthase subunit 6 in human cells results in protein targeting to mitochondria but no assembly into ATP synthase
    • Bokori-Brown M, Holt IJ. Expression of algal nuclear ATP synthase subunit 6 in human cells results in protein targeting to mitochondria but no assembly into ATP synthase. Rejuvenation Res 9:455-469.
    • Rejuvenation Res , vol.9 , pp. 455-469
    • Bokori-Brown, M.1    Holt, I.J.2
  • 11
    • 34250676869 scopus 로고    scopus 로고
    • Allotopic mRNA localization to the mitochondrial surface rescues respiratory chain defects in fibroblasts harboring mitochondrial DNA mutations affecting complex I or v subunits
    • Bonnet C, Kaltimbacher V, Ellouze S, Augustin S, Benit P, Forster V, Rustin P, Sahel JA, Corral-Debrinski M. 2007. Allotopic mRNA localization to the mitochondrial surface rescues respiratory chain defects in fibroblasts harboring mitochondrial DNA mutations affecting complex I or v subunits. Rejuvenation Res 10:127-144.
    • (2007) Rejuvenation Res , vol.10 , pp. 127-144
    • Bonnet, C.1    Kaltimbacher, V.2    Ellouze, S.3    Augustin, S.4    Benit, P.5    Forster, V.6    Rustin, P.7    Sahel, J.A.8    Corral-Debrinski, M.9
  • 12
    • 50849085156 scopus 로고    scopus 로고
    • The optimized allotopic expression of ND1 or ND4 genes restores respiratory chain complex I activity in fibroblasts harboring mutations in these genes
    • Bonnet C, Augustin S, Ellouze S, Benit P, Bouaita A, Rustin P, Sahel JA, Corral-Debrinski M. 2008. The optimized allotopic expression of ND1 or ND4 genes restores respiratory chain complex I activity in fibroblasts harboring mutations in these genes. Biochim Biophys Acta 1783:1707-1717.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 1707-1717
    • Bonnet, C.1    Augustin, S.2    Ellouze, S.3    Benit, P.4    Bouaita, A.5    Rustin, P.6    Sahel, J.A.7    Corral-Debrinski, M.8
  • 14
    • 17144431814 scopus 로고    scopus 로고
    • 6-methylguanine DNA methyltransferase protects against cell killing by chemotherapeutic alkylating agents
    • Cai S, Xu Y, Cooper RJ, Ferkowicz MJ, Hartwell JR, Pollok KE, Kelley MR. 2005. Mitochondrial targeting of human O6-methylguanine DNA methyltransferase protects against cell killing by chemotherapeutic alkylating agents. Cancer Res 65:3319-3327. (Pubitemid 40524616)
    • (2005) Cancer Research , vol.65 , Issue.8 , pp. 3319-3327
    • Cai, S.1    Xu, Y.2    Cooper, R.J.3    Ferkowiez, M.J.4    Hartwell, J.R.5    Pollok, K.E.6    Kelley, M.R.7
  • 16
    • 33846591495 scopus 로고    scopus 로고
    • The taming of the cell penetrating domain of the HIV Tat: Myths and realities
    • Chauhan A, Tikoo A, Kapur AK, Singh M. 2007. The taming of the cell penetrating domain of the HIV Tat: myths and realities. J Control Release 117:148-162.
    • (2007) J Control Release , vol.117 , pp. 148-162
    • Chauhan, A.1    Tikoo, A.2    Kapur, A.K.3    Singh, M.4
  • 18
    • 33846058307 scopus 로고    scopus 로고
    • Gene therapy of the other genome: The challenges of treating mitochondrial DNA defects
    • D'Souza GG, Boddapati SV, Weissig V. 2007. Gene therapy of the other genome: the challenges of treating mitochondrial DNA defects. Pharm Res 24:228-238.
    • (2007) Pharm Res , vol.24 , pp. 228-238
    • D'Souza, G.G.1    Boddapati, S.V.2    Weissig, V.3
  • 19
    • 70450277400 scopus 로고    scopus 로고
    • The alternative oxidase, a tool for compensating cytochrome c oxidase deficiency in human cells
    • Dassa EP, Dufour E, Goncalves S, Jacobs HT, Rustin P. 2009. The alternative oxidase, a tool for compensating cytochrome c oxidase deficiency in human cells. Physiol Plant 137:427-434.
    • (2009) Physiol Plant , vol.137 , pp. 427-434
    • Dassa, E.P.1    Dufour, E.2    Goncalves, S.3    Jacobs, H.T.4    Rustin, P.5
  • 21
    • 0038730828 scopus 로고    scopus 로고
    • A novel TAT-mitochondrial signal sequence fusion protein is processed, stays in mitochondria, and crosses the placenta
    • Del Gaizo V, Payne RM. 2003. A novel TAT-mitochondrial signal sequence fusion protein is processed, stays in mitochondria, and crosses the placenta. Mol Ther 7:720-730.
    • (2003) Mol Ther , vol.7 , pp. 720-730
    • Del Gaizo, V.1    Payne, R.M.2
  • 22
    • 0036367823 scopus 로고    scopus 로고
    • Targeting DNA repair proteins to mitochondria
    • Copeland WC, editors. Totowa, New Jersey: Humana Press
    • Dobson AW, Kelley MR, Wilson GL, LeDoux SP. 2002a. Targeting DNA repair proteins to mitochondria. In: Copeland WC, editors. Mitochondrial DNA: Methods and Protocols, Vol. 197. Totowa, New Jersey: Humana Press. pp 351-362.
    • (2002) Mitochondrial DNA: Methods and Protocols , vol.197 , pp. 351-362
    • Dobson, A.W.1    Kelley, M.R.2    Wilson, G.L.3    Ledoux, S.P.4
  • 24
    • 57749177307 scopus 로고    scopus 로고
    • Mitochondrial gene therapy: An evaluation of strategies for the treatment of mitochondrial DNA disorders
    • Doyle SR, Chan CK. 2008. Mitochondrial gene therapy: An evaluation of strategies for the treatment of mitochondrial DNA disorders. Hum Gene Ther 19:1335-1348.
    • (2008) Hum Gene Ther , vol.19 , pp. 1335-1348
    • Doyle, S.R.1    Chan, C.K.2
  • 25
    • 0038458979 scopus 로고    scopus 로고
    • Targeting human 8-oxoguanine glycosylase to mitochondria of oligodendrocytes protects against menadione-induced oxidative stress
    • Druzhyna NM, Hollensworth SB, Kelley MR, Wilson GL, Ledoux SP. 2003. Targeting human 8-oxoguanine glycosylase to mitochondria of oligodendrocytes protects against menadione-induced oxidative stress. Glia 42:370-378.
    • (2003) Glia , vol.42 , pp. 370-378
    • Druzhyna, N.M.1    Hollensworth, S.B.2    Kelley, M.R.3    Wilson, G.L.4    Ledoux, S.P.5
  • 26
    • 20444430445 scopus 로고    scopus 로고
    • Cytokines induce nitric oxide-mediated mtDNA damage and apoptosis in oligodendrocytes. Protective role of targeting 8-oxoguanine glycosylase to mitochondria
    • Druzhyna NM, Musiyenko SI, Wilson GL, LeDoux SP. 2005. Cytokines induce nitric oxide-mediated mtDNA damage and apoptosis in oligodendrocytes. Protective role of targeting 8-oxoguanine glycosylase to mitochondria. J Biol Chem 280:21673-21679.
    • (2005) J Biol Chem , vol.280 , pp. 21673-21679
    • Druzhyna, N.M.1    Musiyenko, S.I.2    Wilson, G.L.3    Ledoux, S.P.4
  • 28
    • 0037309710 scopus 로고    scopus 로고
    • Imbalancing the DNA base excision repair pathway in the mitochondria; targeting and overexpressing N-methylpurine DNA glycosylase in mitochondria leads to enhanced cell killing
    • Fishel ML, Seo YR, Smith ML, Kelley MR. 2003. Imbalancing the DNA base excision repair pathway in the mitochondria; targeting and overexpressing N-methylpurine DNA glycosylase in mitochondria leads to enhanced cell killing. Cancer Res 63:608-615.
    • (2003) Cancer Res , vol.63 , pp. 608-615
    • Fishel, M.L.1    Seo, Y.R.2    Smith, M.L.3    Kelley, M.R.4
  • 30
    • 0026611680 scopus 로고
    • Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism
    • Glick BS, Brandt A, Cunningham K, Muller S, Hallberg RL, Schatz G. 1992. Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism. Cell 69:809-822.
    • (1992) Cell , vol.69 , pp. 809-822
    • Glick, B.S.1    Brandt, A.2    Cunningham, K.3    Muller, S.4    Hallberg, R.L.5    Schatz, G.6
  • 32
    • 33645769763 scopus 로고    scopus 로고
    • Allotopic expression of a mitochondrial alternative oxidase confers cyanide resistance to human cell respiration
    • Hakkaart GA, Dassa EP, Jacobs HT, Rustin P. 2006. Allotopic expression of a mitochondrial alternative oxidase confers cyanide resistance to human cell respiration. EMBO Rep 7:341-345.
    • (2006) EMBO Rep , vol.7 , pp. 341-345
    • Hakkaart, G.A.1    Dassa, E.P.2    Jacobs, H.T.3    Rustin, P.4
  • 33
    • 6944240044 scopus 로고    scopus 로고
    • The C-terminal alphaO helix of human Ogg1 is essential for 8-oxoguanine DNA glycosylase activity: The mitochondrial beta-Ogg1 lacks this domain and does not have glycosylase activity
    • Hashiguchi, K, Stuart JA, de Souza-Pinto NC, Bohr VA. 2004. The C-terminal alphaO helix of human Ogg1 is essential for 8-oxoguanine DNA glycosylase activity: The mitochondrial beta-Ogg1 lacks this domain and does not have glycosylase activity. Nucleic Acids Res 32:5596-5608.
    • (2004) Nucleic Acids Res , vol.32 , pp. 5596-5608
    • Hashiguchi, K.1    Stuart, J.A.2    De Souza-Pinto, N.C.3    Bohr, V.A.4
  • 34
    • 68549110328 scopus 로고    scopus 로고
    • Twenty years of cell-penetrating peptides: From molecular mechanisms to therapeutics
    • Heitz F, Morris MC, Divita G. 2009. Twenty years of cell-penetrating peptides: From molecular mechanisms to therapeutics. Br J Pharmacol 157:195-206.
    • (2009) Br J Pharmacol , vol.157 , pp. 195-206
    • Heitz, F.1    Morris, M.C.2    Divita, G.3
  • 35
    • 33847365287 scopus 로고    scopus 로고
    • Catch me if you can! Oxidative protein trapping in the intermembrane space of mitochondria
    • Herrmann JM, Kohl R. 2007. Catch me if you can! Oxidative protein trapping in the intermembrane space of mitochondria. J Cell Biol 176:559-563.
    • (2007) J Cell Biol , vol.176 , pp. 559-563
    • Herrmann, J.M.1    Kohl, R.2
  • 36
    • 34250163244 scopus 로고    scopus 로고
    • Yeast apurinic/apyrimidinic endonuclease Apn1 protects mammalian neuronal cell line from oxidative stress
    • Ho R, Rachek LI, Xu Y, Kelley MR, LeDoux SP, Wilson GL. 2007. Yeast apurinic/apyrimidinic endonuclease Apn1 protects mammalian neuronal cell line from oxidative stress. J Neurochem 102:13-24.
    • (2007) J Neurochem , vol.102 , pp. 13-24
    • Ho, R.1    Rachek, L.I.2    Xu, Y.3    Kelley, M.R.4    Ledoux, S.P.5    Wilson, G.L.6
  • 37
    • 0021676056 scopus 로고
    • The cleavable prepiece of an imported mitochondrial protein is sufficient to direct cytosolic dihydrofolate reductase into the mitochondrial matrix
    • Hurt EC, Pesold-Hurt B, Schatz, G. 1984a. The cleavable prepiece of an imported mitochondrial protein is sufficient to direct cytosolic dihydrofolate reductase into the mitochondrial matrix. FEBS Lett 178:306-310.
    • (1984) FEBS Lett , vol.178 , pp. 306-310
    • Hurt, E.C.1    Pesold-Hurt, B.2    Schatz, G.3
  • 38
    • 0021767867 scopus 로고
    • The amino-terminal region of an imported mitochondrial precursor polypeptide can direct cytoplasmic dihydrofolate reductase into the mitochondrial matrix
    • Hurt EC, Pesold-Hurt B, Schatz G. 1984b. The amino-terminal region of an imported mitochondrial precursor polypeptide can direct cytoplasmic dihydrofolate reductase into the mitochondrial matrix. Embo J 3:3149-3156.
    • (1984) Embo J , vol.3 , pp. 3149-3156
    • Hurt, E.C.1    Pesold-Hurt, B.2    Schatz, G.3
  • 39
    • 64549106494 scopus 로고    scopus 로고
    • Recombinant mitochondrial transcription factor a with N-terminal mitochondrial transduction domain increases respiration and mitochondrial gene expression
    • Iyer S, Thomas RR, Portell FR, Dunham LD, Quigley CK, Bennett JP Jr. 2009. Recombinant mitochondrial transcription factor A with N-terminal mitochondrial transduction domain increases respiration and mitochondrial gene expression. Mitochondrion 9:196-203.
    • (2009) Mitochondrion , vol.9 , pp. 196-203
    • Iyer, S.1    Thomas, R.R.2    Portell, F.R.3    Dunham, L.D.4    Quigley, C.K.5    Bennett Jr., J.P.6
  • 40
    • 0033804253 scopus 로고    scopus 로고
    • Som1, a third component of the yeast mitochondrial inner membrane peptidase complex that contains Imp1 and Imp2
    • Jan PS, Esser K, Pratje E, Michaelis G. 2000. Som1, a third component of the yeast mitochondrial inner membrane peptidase complex that contains Imp1 and Imp2. Mol Gen Genet 263:483-491.
    • (2000) Mol Gen Genet , vol.263 , pp. 483-491
    • Jan, P.S.1    Esser, K.2    Pratje, E.3    Michaelis, G.4
  • 41
    • 0028216609 scopus 로고
    • Targeting of passenger protein domains to multiple intracellular membranes
    • Janiak F, Glover JR, Leber B, Rachubinski RA, Andrews DW. 1994. Targeting of passenger protein domains to multiple intracellular membranes. Biochem J 300(Part 1):191-199.
    • (1994) Biochem J , vol.300 , Issue.PART 1 , pp. 191-199
    • Janiak, F.1    Glover, J.R.2    Leber, B.3    Rachubinski, R.A.4    Andrews, D.W.5
  • 42
    • 33745592512 scopus 로고    scopus 로고
    • MRNA localization to the mitochondrial surface allows the efficient translocation inside the organelle of a nuclear recoded ATP6 protein
    • Kaltimbacher V, Bonnet C, Lecoeuvre G, Forster V, Sahel JA, Corral-Debrinski M. 2006. mRNA localization to the mitochondrial surface allows the efficient translocation inside the organelle of a nuclear recoded ATP6 protein. Rna 12:1408-1417.
    • (2006) Rna , vol.12 , pp. 1408-1417
    • Kaltimbacher, V.1    Bonnet, C.2    Lecoeuvre, G.3    Forster, V.4    Sahel, J.A.5    Corral-Debrinski, M.6
  • 48
    • 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, Adhya S. 2006. Functional delivery of a cytosolic tRNA into mutant mitochondria of human cells. Science 314:471-474.
    • (2006) Science , vol.314 , pp. 471-474
    • Mahata, B.1    Mukherjee, S.2    Mishra, S.3    Bandyopadhyay, A.4    Adhya, S.5
  • 49
    • 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 JE, Kwong JQ, Guy J, Schon EA. 2002. Rescue of a deficiency in ATP synthesis by transfer of MTATP6, a mitochondrial DNA-encoded gene, to the nucleus. Nat Genet 30:394-399.
    • (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
  • 52
    • 21244445718 scopus 로고    scopus 로고
    • A disulfide relay system in the intermembrane space of mitochondria that mediates protein import
    • Mesecke N, Terziyska N, Kozany C, Baumann F, Neupert W, Hell K, Herrmann JM. 2005. A disulfide relay system in the intermembrane space of mitochondria that mediates protein import. Cell 121:1059-1069.
    • (2005) Cell , vol.121 , pp. 1059-1069
    • Mesecke, N.1    Terziyska, N.2    Kozany, C.3    Baumann, F.4    Neupert, W.5    Hell, K.6    Herrmann, J.M.7
  • 53
    • 47249099910 scopus 로고    scopus 로고
    • Development of a single-chain, quasi-dimeric zinc-finger nuclease for the selective degradation of mutated human mitochondrial DNA
    • Minczuk M, Papworth MA, Miller JC, Murphy MP, Klug A. 2008. Development of a single-chain, quasi-dimeric zinc-finger nuclease for the selective degradation of mutated human mitochondrial DNA. Nucleic Acids Res 36:3926-3938.
    • (2008) Nucleic Acids Res , vol.36 , pp. 3926-3938
    • Minczuk, M.1    Papworth, M.A.2    Miller, J.C.3    Murphy, M.P.4    Klug, A.5
  • 54
    • 56349144637 scopus 로고    scopus 로고
    • Thirty years of protein translocation into mitochondria: Unexpectedly complex and still puzzling
    • Mokranjac D, Neupert W. 2009. Thirty years of protein translocation into mitochondria: Unexpectedly complex and still puzzling. Biochim Biophys Acta 1793:33-41.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 33-41
    • Mokranjac, D.1    Neupert, W.2
  • 57
    • 33947113002 scopus 로고    scopus 로고
    • Protection of hepatic cells from apoptosis induced by ischemia/reperfusion injury by protein therapeutics
    • Nagai S, Asoh S, Kobayashi Y, Shidara Y, Mori T, Suzuki M, Moriyama Y, Ohta S. 2007. Protection of hepatic cells from apoptosis induced by ischemia/reperfusion injury by protein therapeutics. Hepatol Res 37:133-142.
    • (2007) Hepatol Res , vol.37 , pp. 133-142
    • Nagai, S.1    Asoh, S.2    Kobayashi, Y.3    Shidara, Y.4    Mori, T.5    Suzuki, M.6    Moriyama, Y.7    Ohta, S.8
  • 58
    • 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 LB, Gearing DP, Nero D, Meltzer S, Devenish RJ. 1988. 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 USA 85:2091-2095.
    • (1988) Proc Natl Acad Sci USA , 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
  • 59
    • 0035896587 scopus 로고    scopus 로고
    • Nuclear localization of yeast Nfs1p is required for cell survival
    • Nakai Y, Nakai M, Hayashi H, Kagamiyama H. 2001. Nuclear localization of yeast Nfs1p is required for cell survival. J Biol Chem 276:8314-8320.
    • (2001) J Biol Chem , vol.276 , pp. 8314-8320
    • Nakai, Y.1    Nakai, M.2    Hayashi, H.3    Kagamiyama, H.4
  • 61
    • 0036855408 scopus 로고    scopus 로고
    • An algal nucleus-encoded subunit of mitochondrial ATP synthase rescues a defect in the analogous human mitochondrial-encoded subunit
    • Ojaimi J, Pan J, Santra S, Snell WJ, Schon EA. 2002. An algal nucleus-encoded subunit of mitochondrial ATP synthase rescues a defect in the analogous human mitochondrial-encoded subunit. Mol Biol Cell 13:3836-3844.
    • (2002) Mol Biol Cell , vol.13 , pp. 3836-3844
    • Ojaimi, J.1    Pan, J.2    Santra, S.3    Snell, W.J.4    Schon, E.A.5
  • 62
    • 32044458625 scopus 로고    scopus 로고
    • Designer zinc-finger proteins and their applications
    • DOI 10.1016/j.gene.2005.09.011, PII S0378111905005731
    • Papworth M, Kolasinska P, Minczuk M. 2006. Designer zinc-finger proteins and their applications. Gene 366:27-38. (Pubitemid 43199591)
    • (2006) Gene , vol.366 , Issue.1 , pp. 27-38
    • Papworth, M.1    Kolasinska, P.2    Minczuk, M.3
  • 63
    • 36749087020 scopus 로고    scopus 로고
    • Human mitochondrial transcription factor a possesses multiple subcellular targeting signals
    • Pastukh V, Shokolenko I, Wang B, Wilson G, Alexeyev M. 2007. Human mitochondrial transcription factor A possesses multiple subcellular targeting signals. FEBS J 274:6488-6499.
    • (2007) FEBS J , vol.274 , pp. 6488-6499
    • Pastukh, V.1    Shokolenko, I.2    Wang, B.3    Wilson, G.4    Alexeyev, M.5
  • 64
    • 44049093473 scopus 로고    scopus 로고
    • Mutations in the passenger polypeptide can affect its partitioning between mitochondria and cytoplasm: Mutations can impair the mitochondrial import of DsRed
    • Pastukh V, Shokolenko IN, Wilson GL, Alexeyev MF. 2008. Mutations in the passenger polypeptide can affect its partitioning between mitochondria and cytoplasm: Mutations can impair the mitochondrial import of DsRed. Mol Biol Rep 35:215-223.
    • (2008) Mol Biol Rep , vol.35 , pp. 215-223
    • Pastukh, V.1    Shokolenko, I.N.2    Wilson, G.L.3    Alexeyev, M.F.4
  • 66
    • 2942676945 scopus 로고    scopus 로고
    • Endonuclease III and endonuclease VIII conditionally targeted into mitochondria enhance mitochondrial DNA repair and cell survival following oxidative stress
    • Rachek LI, Grishko VI, Alexeyev MF, Pastukh VV, LeDoux SP, Wilson GL. 2004. Endonuclease III and endonuclease VIII conditionally targeted into mitochondria enhance mitochondrial DNA repair and cell survival following oxidative stress. Nucleic Acids Res 32:3240-3247.
    • (2004) Nucleic Acids Res , vol.32 , pp. 3240-3247
    • Rachek, L.I.1    Grishko, V.I.2    Alexeyev, M.F.3    Pastukh, V.V.4    Ledoux, S.P.5    Wilson, G.L.6
  • 67
    • 41149128339 scopus 로고    scopus 로고
    • TAT-mediated delivery of LAD restores pyruvate dehydrogenase complex activity in the mitochondria of patients with LAD deficiency
    • Rapoport M, Saada A, Elpeleg O, Lorberboum-Galski H. 2008. TAT-mediated delivery of LAD restores pyruvate dehydrogenase complex activity in the mitochondria of patients with LAD deficiency. Mol Ther 16:691-697.
    • (2008) Mol Ther , vol.16 , pp. 691-697
    • Rapoport, M.1    Saada, A.2    Elpeleg, O.3    Lorberboum-Galski, H.4
  • 68
    • 29544434573 scopus 로고    scopus 로고
    • Targeting of O6-MeG DNA methyltransferase (MGMT) to mitochondria protects against alkylation induced cell death
    • Rasmussen AK, Rasmussen LJ. 2005. Targeting of O6-MeG DNA methyltransferase (MGMT) to mitochondria protects against alkylation induced cell death. Mitochondrion 5:411-417.
    • (2005) Mitochondrion , vol.5 , pp. 411-417
    • Rasmussen, A.K.1    Rasmussen, L.J.2
  • 69
    • 24344441532 scopus 로고    scopus 로고
    • Yeast aconitase in two locations and two metabolic pathways: Seeing small amounts is believing
    • Regev-Rudzki N, Karniely S, Ben-Haim NN, Pines O. 2005. Yeast aconitase in two locations and two metabolic pathways: Seeing small amounts is believing. Mol Biol Cell 16:4163-4171.
    • (2005) Mol Biol Cell , vol.16 , pp. 4163-4171
    • Regev-Rudzki, N.1    Karniely, S.2    Ben-Haim, N.N.3    Pines, O.4
  • 70
    • 20144386176 scopus 로고    scopus 로고
    • N-methylpurine DNA glycosylase overexpression increases alkylation sensitivity by rapidly removing non-toxic 7-methylguanine adducts
    • Rinne ML, He Y, Pachkowski BF, Nakamura J, Kelley MR. 2005. N-methylpurine DNA glycosylase overexpression increases alkylation sensitivity by rapidly removing non-toxic 7-methylguanine adducts. Nucleic Acids Res 33:2859-2867.
    • (2005) Nucleic Acids Res , vol.33 , pp. 2859-2867
    • Rinne, M.L.1    He, Y.2    Pachkowski, B.F.3    Nakamura, J.4    Kelley, M.R.5
  • 73
    • 70450253363 scopus 로고    scopus 로고
    • Respiratory chain alternative enzymes as tools to better understand and counteract respiratory chain deficiencies in human cells and animals
    • Rustin P, Jacobs HT. 2009. Respiratory chain alternative enzymes as tools to better understand and counteract respiratory chain deficiencies in human cells and animals. Physiol Plant 137:362-370.
    • (2009) Physiol Plant , vol.137 , pp. 362-370
    • Rustin, P.1    Jacobs, H.T.2
  • 74
    • 29144439725 scopus 로고    scopus 로고
    • Comparison of the protein-unfolding pathways between mitochondrial protein import and atomic-force microscopy measurements
    • Sato T, Esaki M, Fernandez JM, Endo T. 2005. Comparison of the protein-unfolding pathways between mitochondrial protein import and atomic-force microscopy measurements. Proc Natl Acad Sci USA 102:17999-18004.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17999-18004
    • Sato, T.1    Esaki, M.2    Fernandez, J.M.3    Endo, T.4
  • 75
    • 0018791915 scopus 로고
    • How mitochondria import proteins from the cytoplasm
    • Schatz G. 1979. How mitochondria import proteins from the cytoplasm. FEBS Lett 103:203-211.
    • (1979) FEBS Lett , vol.103 , pp. 203-211
    • Schatz, G.1
  • 76
    • 0020566056 scopus 로고
    • How are proteins imported into mitochondria?
    • Schatz G, Butow RA. 1983. How are proteins imported into mitochondria? Cell 32:316-318.
    • (1983) Cell , vol.32 , pp. 316-318
    • Schatz, G.1    Butow, R.A.2
  • 78
    • 0034531991 scopus 로고    scopus 로고
    • Use of the NADH-quinone oxidoreductase (NDI1) gene of Saccharomyces cerevisiae as a possible cure for complex I defects in human cells
    • Seo BB, Wang J, Flotte TR, Yagi T, Matsuno-Yagi A. 2000. Use of the NADH-quinone oxidoreductase (NDI1) gene of Saccharomyces cerevisiae as a possible cure for complex I defects in human cells. J Biol Chem 275:37774-37778.
    • (2000) J Biol Chem , vol.275 , pp. 37774-37778
    • Seo, B.B.1    Wang, J.2    Flotte, T.R.3    Yagi, T.4    Matsuno-Yagi, A.5
  • 79
    • 33744924255 scopus 로고    scopus 로고
    • In vivo complementation of complex I by the yeast Ndi1 enzyme. Possible application for treatment of Parkinson disease
    • Seo BB, Nakamaru-Ogiso E, Flotte TR, Matsuno-Yagi A, Yagi T. 2006. In vivo complementation of complex I by the yeast Ndi1 enzyme. Possible application for treatment of Parkinson disease. J Biol Chem 281:14250-14255.
    • (2006) J Biol Chem , vol.281 , pp. 14250-14255
    • Seo, B.B.1    Nakamaru-Ogiso, E.2    Flotte, T.R.3    Matsuno-Yagi, A.4    Yagi, T.5
  • 80
    • 0242669946 scopus 로고    scopus 로고
    • The expression of Exonuclease III from E. coli in mitochondria of breast cancer cells diminishes mitochondrial DNA repair capacity and cell survival after oxidative stress
    • Shokolenko IN, Alexeyev MF, Robertson FM, LeDoux SP, Wilson GL. 2003. The expression of Exonuclease III from E. coli in mitochondria of breast cancer cells diminishes mitochondrial DNA repair capacity and cell survival after oxidative stress. DNA Repair (Amst) 2:471-482.
    • (2003) DNA Repair (Amst) , vol.2 , pp. 471-482
    • Shokolenko, I.N.1    Alexeyev, M.F.2    Robertson, F.M.3    Ledoux, S.P.4    Wilson, G.L.5
  • 81
    • 13844317215 scopus 로고    scopus 로고
    • TAT-mediated protein transduction and targeted delivery of fusion proteins into mitochondria of breast cancer cells
    • Shokolenko IN, Alexeyev MF, LeDoux SP, Wilson, GL. 2005. TAT-mediated protein transduction and targeted delivery of fusion proteins into mitochondria of breast cancer cells. DNA Repair (Amst) 4:511-518.
    • (2005) DNA Repair (Amst) , vol.4 , pp. 511-518
    • Shokolenko, I.N.1    Alexeyev, M.F.2    Ledoux, S.P.3    Wilson, G.L.4
  • 82
    • 0034663499 scopus 로고    scopus 로고
    • The mitochondrial cyanide-resistant oxidase: Structural conservation amid regulatory diversity
    • Siedow JN, Umbach AL. 2000. The mitochondrial cyanide-resistant oxidase: structural conservation amid regulatory diversity. Biochim Biophys Acta 1459:432-439.
    • (2000) Biochim Biophys Acta , vol.1459 , pp. 432-439
    • Siedow, J.N.1    Umbach, A.L.2
  • 83
    • 33745208665 scopus 로고    scopus 로고
    • Mitochondrial import of human and yeast fumarase in live mammalian cells: Retrograde translocation of the yeast enzyme is mainly caused by its poor targeting sequence
    • Singh B, Gupta RS. 2006. Mitochondrial import of human and yeast fumarase in live mammalian cells: Retrograde translocation of the yeast enzyme is mainly caused by its poor targeting sequence. Biochem Biophys Res Commun 346:911-918.
    • (2006) Biochem Biophys Res Commun , vol.346 , pp. 911-918
    • Singh, B.1    Gupta, R.S.2
  • 84
    • 0035894698 scopus 로고    scopus 로고
    • Manipulating mitochondrial DNA heteroplasmy by a mitochondrially targeted restriction endonuclease
    • Srivastava S, Moraes CT. 2001. Manipulating mitochondrial DNA heteroplasmy by a mitochondrially targeted restriction endonuclease. Hum Mol Genet 10:3093-3099. (Pubitemid 34083495)
    • (2001) Human Molecular Genetics , vol.10 , Issue.26 , pp. 3093-3099
    • Srivastava, S.1    Moraes, C.T.2
  • 88
    • 0023054140 scopus 로고
    • Targeting efficiency of a mitochondrial pre-sequence is dependent on the passenger protein
    • Van Steeg H, Oudshoorn P, Van Hell B, Polman JE, Grivell LA. 1986. Targeting efficiency of a mitochondrial pre-sequence is dependent on the passenger protein. Embo J 5:3643-3650.
    • (1986) Embo J , vol.5 , pp. 3643-3650
    • Van Steeg, H.1    Oudshoorn, P.2    Van Hell, B.3    Polman, J.E.4    Grivell, L.A.5
  • 89
    • 75649090482 scopus 로고    scopus 로고
    • Novel role of ATPase subunit c targeting peptides beyond mitochondrial protein import
    • Vives-Bauza C, Magrane J, Andreu AL, Manfredi G. 2009. Novel role of ATPase subunit c targeting peptides beyond mitochondrial protein import. Mol Biol Cell 21:131-139.
    • (2009) Mol Biol Cell , vol.21 , pp. 131-139
    • Vives-Bauza, C.1    Magrane, J.2    Andreu, A.L.3    Manfredi, G.4
  • 92
    • 0038048992 scopus 로고    scopus 로고
    • Modulation of cellular function by TAT mediated transduction of full length proteins
    • Wadia JS, Dowdy SF. 2003. Modulation of cellular function by TAT mediated transduction of full length proteins. Curr Protein Pept Sci 4:97-104.
    • (2003) Curr Protein Pept Sci , vol.4 , pp. 97-104
    • Wadia, J.S.1    Dowdy, S.F.2
  • 93
    • 33646525645 scopus 로고    scopus 로고
    • Protein transduction: Cell penetrating peptides and their therapeutic applications
    • Wagstaff KM, Jans DA. 2006. Protein transduction: Cell penetrating peptides and their therapeutic applications. Curr Med Chem 13:1371-1387.
    • (2006) Curr Med Chem , vol.13 , pp. 1371-1387
    • Wagstaff, K.M.1    Jans, D.A.2
  • 94
    • 0029813508 scopus 로고    scopus 로고
    • Influence of the mature portion of a precursor protein on the mitochondrial signal sequence
    • Waltner M, Hammen PK, Weiner H. 1996. Influence of the mature portion of a precursor protein on the mitochondrial signal sequence. J Biol Chem 271:21226-21230.
    • (1996) J Biol Chem , vol.271 , pp. 21226-21230
    • Waltner, M.1    Hammen, P.K.2    Weiner, H.3
  • 97
    • 51249109260 scopus 로고    scopus 로고
    • Mitochondrial drug delivery systems for macromolecule and their therapeutic application to mitochondrial diseases
    • Yamada Y, Harashima H. 2008. Mitochondrial drug delivery systems for macromolecule and their therapeutic application to mitochondrial diseases. Adv Drug Deliv Rev 60:1439-1462.
    • (2008) Adv Drug Deliv Rev , vol.60 , pp. 1439-1462
    • Yamada, Y.1    Harashima, H.2
  • 98
    • 70350263429 scopus 로고    scopus 로고
    • PCR-based cloning of the complete mouse mitochondrial genome and stable engineering in Escherichia coli
    • Yoon YG, Yang YW, Koob MD. 2009. PCR-based cloning of the complete mouse mitochondrial genome and stable engineering in Escherichia coli. Biotechnol Lett 31:1671-1676.
    • (2009) Biotechnol Lett , vol.31 , pp. 1671-1676
    • Yoon, Y.G.1    Yang, Y.W.2    Koob, M.D.3
  • 99
    • 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 SJ, Parks WT, Chloupkova M, Wei B, Weiner H, Fenton WA, Eisenstadt JM, Merril CR. 2005. 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 8:18-28.
    • (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


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