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Volumn 1, Issue NOV, 2014, Pages

Protein folding as a driving force for dual protein targeting in eukaryotes

Author keywords

Chaperones; Echoforms; Membranes; MTS (mitochondrial targeting sequence); Organelles; Retrotranslocation; Reverse translocation; Signal peptide

Indexed keywords


EID: 84974687278     PISSN: None     EISSN: 2296889X     Source Type: Journal    
DOI: 10.3389/fmolb.2014.00023     Document Type: Review
Times cited : (17)

References (87)
  • 1
    • 0030611669 scopus 로고    scopus 로고
    • Targeting of NH2-terminal-processed microsomal protein to mitochondria: a novel pathway for the biogenesis of hepatic mitochondrial P450MT2
    • Addya, S., Anandatheerthavarada, H. K., Biswas, G., Bhagwat, S. V., Mullick, J., and Avadhani, N. G. (1997). Targeting of NH2-terminal-processed microsomal protein to mitochondria: a novel pathway for the biogenesis of hepatic mitochondrial P450MT2. J. Cell Biol. 139, 589-599. doi: 10.1083/jcb.139.3.589
    • (1997) J. Cell Biol , vol.139 , pp. 589-599
    • Addya, S.1    Anandatheerthavarada, H.K.2    Biswas, G.3    Bhagwat, S.V.4    Mullick, J.5    Avadhani, N.G.6
  • 2
    • 77649190277 scopus 로고    scopus 로고
    • Tid1 is a new regulator of p53 mitochondrial translocation and apoptosis in cancer
    • Ahn, B. Y., Trinh, D. L., Zajchowski, L. D., Lee, B., Elwi, A. N., and Kim, S. W. (2010). Tid1 is a new regulator of p53 mitochondrial translocation and apoptosis in cancer. Oncogene 29, 1155-1166. doi: 10.1038/onc.2009.413
    • (2010) Oncogene , vol.29 , pp. 1155-1166
    • Ahn, B.Y.1    Trinh, D.L.2    Zajchowski, L.D.3    Lee, B.4    Elwi, A.N.5    Kim, S.W.6
  • 3
    • 84901837487 scopus 로고    scopus 로고
    • Cellular functions of the dual-targeted catalytic subunit of telomerase, telomerase reverse transcriptase-potential role in senescence and aging
    • Ale-Agha, N., Dyballa-Rukes, N., Jakob, S., Altschmied, J., and Haendeler, J. (2014). Cellular functions of the dual-targeted catalytic subunit of telomerase, telomerase reverse transcriptase-potential role in senescence and aging. Exp. Gerontol. 56, 189-193. doi: 10.1016/j.exger.2014.02.011
    • (2014) Exp. Gerontol , vol.56 , pp. 189-193
    • Ale-Agha, N.1    Dyballa-Rukes, N.2    Jakob, S.3    Altschmied, J.4    Haendeler, J.5
  • 4
    • 67650559448 scopus 로고    scopus 로고
    • Mitochondrial targeting of cytochrome P450 proteins containing NH2-terminal chimeric signals involves an unusual TOM20/TOM22 bypass mechanism
    • Anandatheerthavarada, H. K., Sepuri, N. B., and Avadhani, N. G. (2009). Mitochondrial targeting of cytochrome P450 proteins containing NH2-terminal chimeric signals involves an unusual TOM20/TOM22 bypass mechanism. J. Biol. Chem. 284, 17352-17363. doi: 10.1074/jbc.M109.007492
    • (2009) J. Biol. Chem , vol.284 , pp. 17352-17363
    • Anandatheerthavarada, H.K.1    Sepuri, N.B.2    Avadhani, N.G.3
  • 5
    • 80255137185 scopus 로고    scopus 로고
    • Targeting of the same proteins to multiple subcellular destinations: mechanisms and physiological implications
    • Avadhani, N. G. (2011). Targeting of the same proteins to multiple subcellular destinations: mechanisms and physiological implications. FEBS J. 278, 4217. doi: 10.1111/j.1742-4658.2011.08355.x
    • (2011) FEBS J , vol.278 , pp. 4217
    • Avadhani, N.G.1
  • 6
    • 80255136273 scopus 로고    scopus 로고
    • Bimodal targeting of cytochrome P450s to endoplasmic reticulum and mitochondria: the concept of chimeric signals
    • Avadhani, N. G., Sangar, M. C., Bansal, S., and Bajpai, P. (2011). Bimodal targeting of cytochrome P450s to endoplasmic reticulum and mitochondria: the concept of chimeric signals. FEBS J. 278, 4218-4229. doi: 10.1111/j.1742-4658.2011.08356.x
    • (2011) FEBS J , vol.278 , pp. 4218-4229
    • Avadhani, N.G.1    Sangar, M.C.2    Bansal, S.3    Bajpai, P.4
  • 7
    • 0032518742 scopus 로고    scopus 로고
    • Influence of N-terminal sequence variation on the sorting of major adenylate kinase to the mitochondrial intermembrane space in yeast
    • Bandlow, W., Strobel, G., and Schricker, R. (1998). Influence of N-terminal sequence variation on the sorting of major adenylate kinase to the mitochondrial intermembrane space in yeast. Biochem. J. 329(Pt 2), 359-367
    • (1998) Biochem. J , vol.329 , pp. 359-367
    • Bandlow, W.1    Strobel, G.2    Schricker, R.3
  • 8
    • 79955904604 scopus 로고    scopus 로고
    • The aconitase C-terminal domain is an independent dual targeting element
    • Ben-Menachem, R., Regev-Rudzki, N., and Pines, O. (2011a). The aconitase C-terminal domain is an independent dual targeting element. J. Mol. Biol. 409, 113-123. doi: 10.1016/j.jmb.2011.03.045
    • (2011) J. Mol. Biol , vol.409 , pp. 113-123
    • Ben-Menachem, R.1    Regev-Rudzki, N.2    Pines, O.3
  • 9
    • 81855185408 scopus 로고    scopus 로고
    • A third of the yeast mitochondrial proteome is dual localized: a question of evolution
    • Ben-Menachem, R., Tal, M., Shadur, T., and Pines, O. (2011b). A third of the yeast mitochondrial proteome is dual localized: a question of evolution. Proteomics 11, 4468-4476. doi: 10.1002/pmic.201100199
    • (2011) Proteomics , vol.11 , pp. 4468-4476
    • Ben-Menachem, R.1    Tal, M.2    Shadur, T.3    Pines, O.4
  • 10
    • 84883585280 scopus 로고    scopus 로고
    • Mitochondrial p53 mediates a transcription-independent regulation of cell respiration and interacts with the mitochondrial F(1)F0-ATP synthase
    • Bergeaud, M., Mathieu, L., Guillaume, A., Moll, U. M., Mignotte, B., Le Floch, N., et al. (2013). Mitochondrial p53 mediates a transcription-independent regulation of cell respiration and interacts with the mitochondrial F(1)F0-ATP synthase. Cell Cycle 12, 2781-2793. doi: 10.4161/cc.25870
    • (2013) Cell Cycle , vol.12 , pp. 2781-2793
    • Bergeaud, M.1    Mathieu, L.2    Guillaume, A.3    Moll, U.M.4    Mignotte, B.5    Le Floch, N.6
  • 11
    • 41649116014 scopus 로고    scopus 로고
    • Derlin-1 facilitates the retro-translocation of cholera toxin
    • Bernardi, K. M., Forster, M. L., Lencer, W. I., and Tsai, B. (2008). Derlin-1 facilitates the retro-translocation of cholera toxin. Mol. Biol. Cell 19, 877-884. doi: 10.1091/mbc.E07-08-0755
    • (2008) Mol. Biol. Cell , vol.19 , pp. 877-884
    • Bernardi, K.M.1    Forster, M.L.2    Lencer, W.I.3    Tsai, B.4
  • 12
    • 75649144790 scopus 로고    scopus 로고
    • The E3 ubiquitin ligases Hrd1 and gp78 bind to and promote cholera toxin retro-translocation
    • Bernardi, K. M., Williams, J. M., Kikkert, M., van Voorden, S., Wiertz, E. J., Ye, Y., et al. (2010). The E3 ubiquitin ligases Hrd1 and gp78 bind to and promote cholera toxin retro-translocation. Mol. Biol. Cell 21, 140-151. doi: 10.1091/mbc.E09-07-0586
    • (2010) Mol. Biol. Cell , vol.21 , pp. 140-151
    • Bernardi, K.M.1    Williams, J.M.2    Kikkert, M.3    van Voorden, S.4    Wiertz, E.J.5    Ye, Y.6
  • 13
    • 84856411525 scopus 로고    scopus 로고
    • Prion protein at the crossroads of physiology and disease
    • Biasini, E., Turnbaugh, J. A., Unterberger, U., and Harris, D. A. (2012). Prion protein at the crossroads of physiology and disease. Trends Neurosci. 35, 92-103. doi: 10.1016/j.tins.2011.10.002
    • (2012) Trends Neurosci , vol.35 , pp. 92-103
    • Biasini, E.1    Turnbaugh, J.A.2    Unterberger, U.3    Harris, D.A.4
  • 14
    • 84891762584 scopus 로고    scopus 로고
    • LoQAtE-Localization and Quantitation ATlas of the yeast proteomE A new tool for multiparametric dissection of single-protein behavior in response to biological perturbations in yeast
    • Breker, M., Gymrek, M., Moldavski, O., and Schuldiner, M. (2014). LoQAtE-Localization and Quantitation ATlas of the yeast proteomE. A new tool for multiparametric dissection of single-protein behavior in response to biological perturbations in yeast. Nucleic Acids Res. 42, D726-D730. doi: 10.1093/nar/gkt933
    • (2014) Nucleic Acids Res , vol.42 , pp. D726-D730
    • Breker, M.1    Gymrek, M.2    Moldavski, O.3    Schuldiner, M.4
  • 15
    • 70549107710 scopus 로고    scopus 로고
    • Mitochondrial cell death effectors
    • Brenner, D., and Mak, T. W. (2009). Mitochondrial cell death effectors. Curr. Opin. Cell Biol. 21, 871-877. doi: 10.1016/j.ceb.2009.09.004
    • (2009) Curr. Opin. Cell Biol , vol.21 , pp. 871-877
    • Brenner, D.1    Mak, T.W.2
  • 16
    • 84879406272 scopus 로고    scopus 로고
    • Evolving dual targeting of a prokaryotic protein in yeast
    • Burak, E., Yogev, O., Sheffer, S., Schueler-Furman, O., and Pines, O. (2013). Evolving dual targeting of a prokaryotic protein in yeast. Mol. Biol. Evol. 30, 1563-1573. doi: 10.1093/molbev/mst039
    • (2013) Mol. Biol. Evol , vol.30 , pp. 1563-1573
    • Burak, E.1    Yogev, O.2    Sheffer, S.3    Schueler-Furman, O.4    Pines, O.5
  • 17
    • 84871779194 scopus 로고    scopus 로고
    • A reevaluation of dual-targeting of proteins to mitochondria and chloroplasts
    • Carrie, C., and Small, I. (2013). A reevaluation of dual-targeting of proteins to mitochondria and chloroplasts. Biochim. Biophys. Acta 1833, 253-259. doi: 10.1016/j.bbamcr.2012.05.029
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 253-259
    • Carrie, C.1    Small, I.2
  • 18
    • 84881154724 scopus 로고    scopus 로고
    • Widespread dual targeting of proteins in land plants: when, where, how and why
    • Carrie, C., and Whelan, J. (2013). Widespread dual targeting of proteins in land plants: when, where, how and why. Plant Signal. Behav. 8:e25034. doi: 10.4161/psb.25034
    • (2013) Plant Signal. Behav , vol.8
    • Carrie, C.1    Whelan, J.2
  • 19
    • 68749112707 scopus 로고    scopus 로고
    • Importing mitochondrial proteins: machineries and mechanisms
    • Chacinska, A., Koehler, C. M., Milenkovic, D., Lithgow, T., and Pfanner, N. (2009). Importing mitochondrial proteins: machineries and mechanisms. Cell 138, 628-644. doi: 10.1016/j.cell.2009.08.005
    • (2009) Cell , vol.138 , pp. 628-644
    • Chacinska, A.1    Koehler, C.M.2    Milenkovic, D.3    Lithgow, T.4    Pfanner, N.5
  • 20
    • 35748929414 scopus 로고    scopus 로고
    • Cytosolic accumulation of HSP60 during apoptosis with or without apparent mitochondrial release: evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase-3
    • Chandra, D., Choy, G., and Tang, D. G. (2007). Cytosolic accumulation of HSP60 during apoptosis with or without apparent mitochondrial release: evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase-3. J. Biol. Chem. 282, 31289-31301. doi: 10.1074/jbc.M702777200
    • (2007) J. Biol. Chem , vol.282 , pp. 31289-31301
    • Chandra, D.1    Choy, G.2    Tang, D.G.3
  • 21
    • 84864966476 scopus 로고    scopus 로고
    • Nuclear import of hTERT requires a bipartite nuclear localization signal and Akt-mediated phosphorylation
    • Chung, J., Khadka, P., and Chung, I. K. (2012). Nuclear import of hTERT requires a bipartite nuclear localization signal and Akt-mediated phosphorylation. J. Cell Sci. 125, 2684-2697. doi: 10.1242/jcs.099267
    • (2012) J. Cell Sci , vol.125 , pp. 2684-2697
    • Chung, J.1    Khadka, P.2    Chung, I.K.3
  • 22
    • 0037474269 scopus 로고    scopus 로고
    • NF-kappa B and I kappa B alpha are found in the mitochondria Evidence for regulation of mitochondrial gene expression by NF-kappa B
    • Cogswell, P. C., Kashatus, D. F., Keifer, J. A., Guttridge, D. C., Reuther, J. Y., Bristow, C., et al. (2003). NF-kappa B and I kappa B alpha are found in the mitochondria. Evidence for regulation of mitochondrial gene expression by NF-kappa B. J. Biol. Chem. 278, 2963-2968. doi: 10.1074/jbc.M209995200
    • (2003) J. Biol. Chem , vol.278 , pp. 2963-2968
    • Cogswell, P.C.1    Kashatus, D.F.2    Keifer, J.A.3    Guttridge, D.C.4    Reuther, J.Y.5    Bristow, C.6
  • 23
    • 14744271077 scopus 로고    scopus 로고
    • N-myristoylation determines dual targeting of mammalian NADH-cytochrome b5 reductase to ER and mitochondrial outer membranes by a mechanism of kinetic partitioning
    • Colombo, S., Longhi, R., Alcaro, S., Ortuso, F., Sprocati, T., Flora, A., et al. (2005). N-myristoylation determines dual targeting of mammalian NADH-cytochrome b5 reductase to ER and mitochondrial outer membranes by a mechanism of kinetic partitioning. J. Cell Biol. 168, 735-745. doi: 10.1083/jcb.200407082
    • (2005) J. Cell Biol , vol.168 , pp. 735-745
    • Colombo, S.1    Longhi, R.2    Alcaro, S.3    Ortuso, F.4    Sprocati, T.5    Flora, A.6
  • 24
    • 57649219450 scopus 로고    scopus 로고
    • Targeting of hFis1 to peroxisomes is mediated by Pex19p
    • Delille, H. K., and Schrader, M. (2008). Targeting of hFis1 to peroxisomes is mediated by Pex19p. J. Biol. Chem. 283, 31107-31115. doi: 10.1074/jbc.M803332200
    • (2008) J. Biol. Chem , vol.283 , pp. 31107-31115
    • Delille, H.K.1    Schrader, M.2
  • 25
    • 84864804909 scopus 로고    scopus 로고
    • RECQL4 is essential for the transport of p53 to mitochondria in normal human cells in the absence of exogenous stress
    • De, S., Kumari, J., Mudgal, R., Modi, P., Gupta, S., Futami, K., et al. (2012). RECQL4 is essential for the transport of p53 to mitochondria in normal human cells in the absence of exogenous stress. J. Cell Sci. 125, 2509-2522. doi: 10.1242/jcs.101501
    • (2012) J. Cell Sci , vol.125 , pp. 2509-2522
    • De, S.1    Kumari, J.2    Mudgal, R.3    Modi, P.4    Gupta, S.5    Futami, K.6
  • 26
    • 4444323263 scopus 로고    scopus 로고
    • p53 functions in the incorporation step in DNA base excision repair in mouse liver mitochondria
    • de Souza-Pinto, N. C., Harris, C. C., and Bohr, V. A. (2004). p53 functions in the incorporation step in DNA base excision repair in mouse liver mitochondria. Oncogene 23, 6559-6568. doi: 10.1038/sj.onc.1207874
    • (2004) Oncogene , vol.23 , pp. 6559-6568
    • de Souza-Pinto, N.C.1    Harris, C.C.2    Bohr, V.A.3
  • 27
    • 47749097978 scopus 로고    scopus 로고
    • Dual targeted mitochondrial proteins are characterized by lower MTS parameters and total net charge
    • Dinur-Mills, M., Tal, M., and Pines, O. (2008). Dual targeted mitochondrial proteins are characterized by lower MTS parameters and total net charge. PLoS ONE 3:e2161. doi: 10.1371/journal.pone.0002161
    • (2008) PLoS ONE , vol.3
    • Dinur-Mills, M.1    Tal, M.2    Pines, O.3
  • 28
    • 84877924814 scopus 로고    scopus 로고
    • Dual localized mitochondrial and nuclear proteins as gene expression regulators in plants?
    • Duchene, A. M., and Giege, P. (2012). Dual localized mitochondrial and nuclear proteins as gene expression regulators in plants? Front. Plant Sci. 3:221. doi: 10.3389/fpls.2012.00221
    • (2012) Front. Plant Sci , vol.3 , pp. 221
    • Duchene, A.M.1    Giege, P.2
  • 29
    • 0023644959 scopus 로고
    • Structure of the complex of yeast adenylate kinase with the inhibitor P1, P5-di(adenosine-5'-)pentaphosphate at 2.6 A resolution
    • Egner, U., Tomasselli, A. G., and Schulz, G. E. (1987). Structure of the complex of yeast adenylate kinase with the inhibitor P1, P5-di(adenosine-5'-)pentaphosphate at 2.6 A resolution. J. Mol. Biol. 195, 649-658. doi: 10.1016/0022-2836(87)90188-4
    • (1987) J. Mol. Biol , vol.195 , pp. 649-658
    • Egner, U.1    Tomasselli, A.G.2    Schulz, G.E.3
  • 30
    • 80755153578 scopus 로고    scopus 로고
    • Staying in touch: the molecular era of organelle contact sites
    • Elbaz, Y., and Schuldiner, M. (2011). Staying in touch: the molecular era of organelle contact sites. Trends Biochem. Sci. 36, 616-623. doi: 10.1016/j.tibs.2011.08.004
    • (2011) Trends Biochem. Sci , vol.36 , pp. 616-623
    • Elbaz, Y.1    Schuldiner, M.2
  • 32
    • 3242690522 scopus 로고    scopus 로고
    • In vivo mitochondrial p53 translocation triggers a rapid first wave of cell death in response to DNA damage that can precede p53 target gene activation
    • Erster, S., Mihara, M., Kim, R. H., Petrenko, O., and Moll, U. M. (2004). In vivo mitochondrial p53 translocation triggers a rapid first wave of cell death in response to DNA damage that can precede p53 target gene activation. Mol. Cell Biol. 24, 6728-6741. doi: 10.1128/MCB.24.15.6728-6741.2004
    • (2004) Mol. Cell Biol , vol.24 , pp. 6728-6741
    • Erster, S.1    Mihara, M.2    Kim, R.H.3    Petrenko, O.4    Moll, U.M.5
  • 33
    • 65449172879 scopus 로고    scopus 로고
    • Yeast mitochondrial Gln-tRNA(Gln) is generated by a GatFAB-mediated transamidation pathway involving Arc1p-controlled subcellular sorting of cytosolic GluRS
    • Frechin, M., Senger, B., Braye, M., Kern, D., Martin, R. P., and Becker, H. D. (2009). Yeast mitochondrial Gln-tRNA(Gln) is generated by a GatFAB-mediated transamidation pathway involving Arc1p-controlled subcellular sorting of cytosolic GluRS. Genes Dev. 23, 1119-1130. doi: 10.1101/gad.518109
    • (2009) Genes Dev , vol.23 , pp. 1119-1130
    • Frechin, M.1    Senger, B.2    Braye, M.3    Kern, D.4    Martin, R.P.5    Becker, H.D.6
  • 34
    • 84861430732 scopus 로고    scopus 로고
    • Cryptic peroxisomal targeting via alternative splicing and stop codon read-through in fungi
    • Freitag, J., Ast, J., and Bolker, M. (2012). Cryptic peroxisomal targeting via alternative splicing and stop codon read-through in fungi. Nature 485, 522-525. doi: 10.1038/nature11051
    • (2012) Nature , vol.485 , pp. 522-525
    • Freitag, J.1    Ast, J.2    Bolker, M.3
  • 35
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green, D. R., and Kroemer, G. (2004). The pathophysiology of mitochondrial cell death. Science 305, 626-629. doi: 10.1126/science.1099320
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 36
    • 80054711990 scopus 로고    scopus 로고
    • Mitochondrial Ccs1 contains a structural disulfide bond crucial for the import of this unconventional substrate by the disulfide relay system
    • Gross, D. P., Burgard, C. A., Reddehase, S., Leitch, J. M., Culotta, V. C., and Hell, K. (2011). Mitochondrial Ccs1 contains a structural disulfide bond crucial for the import of this unconventional substrate by the disulfide relay system. Mol. Biol. Cell 22, 3758-3767. doi: 10.1091/mbc.E11-04-0296
    • (2011) Mol. Biol. Cell , vol.22 , pp. 3758-3767
    • Gross, D.P.1    Burgard, C.A.2    Reddehase, S.3    Leitch, J.M.4    Culotta, V.C.5    Hell, K.6
  • 37
    • 66349130192 scopus 로고    scopus 로고
    • Mitochondrial telomerase reverse transcriptase binds to and protects mitochondrial DNA and function from damage
    • Haendeler, J., Drose, S., Buchner, N., Jakob, S., Altschmied, J., Goy, C., et al. (2009). Mitochondrial telomerase reverse transcriptase binds to and protects mitochondrial DNA and function from damage. Arterioscler. Thromb. Vasc. Biol. 29, 929-935. doi: 10.1161/ATVBAHA.109.185546
    • (2009) Arterioscler. Thromb. Vasc. Biol , vol.29 , pp. 929-935
    • Haendeler, J.1    Drose, S.2    Buchner, N.3    Jakob, S.4    Altschmied, J.5    Goy, C.6
  • 38
    • 84896716062 scopus 로고    scopus 로고
    • The protein import machinery of mitochondria-a regulatory hub in metabolism, stress, and disease
    • Harbauer, A. B., Zahedi, R. P., Sickmann, A., Pfanner, N., and Meisinger, C. (2014). The protein import machinery of mitochondria-a regulatory hub in metabolism, stress, and disease. Cell Metab. 19, 357-372. doi: 10.1016/j.cmet.2014.01.010
    • (2014) Cell Metab , vol.19 , pp. 357-372
    • Harbauer, A.B.1    Zahedi, R.P.2    Sickmann, A.3    Pfanner, N.4    Meisinger, C.5
  • 39
    • 84856853161 scopus 로고    scopus 로고
    • Mitochondrial disulfide relay: redox-regulated protein import into the intermembrane space
    • Herrmann, J. M., and Riemer, J. (2012). Mitochondrial disulfide relay: redox-regulated protein import into the intermembrane space. J. Biol. Chem. 287, 4426-4433. doi: 10.1074/jbc.R111.270678
    • (2012) J. Biol. Chem , vol.287 , pp. 4426-4433
    • Herrmann, J.M.1    Riemer, J.2
  • 40
    • 84865097949 scopus 로고    scopus 로고
    • Interaction of OKL38 and p53 in regulating mitochondrial structure and function
    • Hu, J., Yao, H., Gan, F., Tokarski, A., and Wang, Y. (2012). Interaction of OKL38 and p53 in regulating mitochondrial structure and function. PLoS ONE 7:e43362. doi: 10.1371/journal.pone.0043362
    • (2012) PLoS ONE , vol.7
    • Hu, J.1    Yao, H.2    Gan, F.3    Tokarski, A.4    Wang, Y.5
  • 41
    • 77950370585 scopus 로고    scopus 로고
    • Reconstitution of the mitochondrial Hsp70 (mortalin)-p53 interaction using purified proteins-identification of additional interacting regions
    • Iosefson, O., and Azem, A. (2010). Reconstitution of the mitochondrial Hsp70 (mortalin)-p53 interaction using purified proteins-identification of additional interacting regions. FEBS Lett. 584, 1080-1084. doi: 10.1016/j.febslet.2010.02.019
    • (2010) FEBS Lett , vol.584 , pp. 1080-1084
    • Iosefson, O.1    Azem, A.2
  • 42
    • 20044387943 scopus 로고    scopus 로고
    • Single translation-dual destination: mechanisms of dual protein targeting in eukaryotes
    • Karniely, S., and Pines, O. (2005). Single translation-dual destination: mechanisms of dual protein targeting in eukaryotes. EMBO Rep. 6, 420-425. doi: 10.1038/sj.embor.7400394
    • (2005) EMBO Rep , vol.6 , pp. 420-425
    • Karniely, S.1    Pines, O.2
  • 43
    • 33646109080 scopus 로고    scopus 로고
    • The presequence of fumarase is exposed to the cytosol during import into mitochondria
    • Karniely, S., Regev-Rudzki, N., and Pines, O. (2006). The presequence of fumarase is exposed to the cytosol during import into mitochondria. J. Mol. Biol. 358, 396-405. doi: 10.1016/j.jmb.2006.02.023
    • (2006) J. Mol. Biol , vol.358 , pp. 396-405
    • Karniely, S.1    Regev-Rudzki, N.2    Pines, O.3
  • 44
    • 33847651284 scopus 로고    scopus 로고
    • Three faces of mortalin: a housekeeper, guardian and killer
    • Kaul, S. C., Deocaris, C. C., and Wadhwa, R. (2007). Three faces of mortalin: a housekeeper, guardian and killer. Exp. Gerontol. 42, 263-274. doi: 10.1016/j.exger.2006.10.020
    • (2007) Exp. Gerontol , vol.42 , pp. 263-274
    • Kaul, S.C.1    Deocaris, C.C.2    Wadhwa, R.3
  • 45
    • 84930342555 scopus 로고    scopus 로고
    • Dual-targeted proteins tend to be more evolutionarily conserved
    • Kisslov, I., Naamati, A., Shakarchy, N., and Pines, O. (2014). Dual-targeted proteins tend to be more evolutionarily conserved. Mol. Biol. Evol. 31, 2770-2779. doi: 10.1093/molbev/msu221
    • (2014) Mol. Biol. Evol , vol.31 , pp. 2770-2779
    • Kisslov, I.1    Naamati, A.2    Shakarchy, N.3    Pines, O.4
  • 46
    • 78649699760 scopus 로고    scopus 로고
    • In yeast redistribution of Sod1 to the mitochondrial intermembrane space provides protection against respiration derived oxidative stress
    • Kloppel, C., Michels, C., Zimmer, J., Herrmann, J. M., and Riemer, J. (2010). In yeast redistribution of Sod1 to the mitochondrial intermembrane space provides protection against respiration derived oxidative stress. Biochem. Biophys. Res. Commun. 403, 114-119. doi: 10.1016/j.bbrc.2010.10.129
    • (2010) Biochem. Biophys. Res. Commun , vol.403 , pp. 114-119
    • Kloppel, C.1    Michels, C.2    Zimmer, J.3    Herrmann, J.M.4    Riemer, J.5
  • 47
    • 80054690509 scopus 로고    scopus 로고
    • Mia40-dependent oxidation of cysteines in domain I of Ccs1 controls its distribution between mitochondria and the cytosol
    • Kloppel, C., Suzuki, Y., Kojer, K., Petrungaro, C., Longen, S., Fiedler, S., et al. (2011). Mia40-dependent oxidation of cysteines in domain I of Ccs1 controls its distribution between mitochondria and the cytosol. Mol. Biol. Cell 22, 3749-3757. doi: 10.1091/mbc.E11-04-0293
    • (2011) Mol. Biol. Cell , vol.22 , pp. 3749-3757
    • Kloppel, C.1    Suzuki, Y.2    Kojer, K.3    Petrungaro, C.4    Longen, S.5    Fiedler, S.6
  • 48
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis
    • Kluck, R. M., Bossy-Wetzel, E., Green, D. R., and Newmeyer, D. D. (1997). The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 275, 1132-1136. doi: 10.1126/science.275.5303.1132
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 49
    • 67749122635 scopus 로고    scopus 로고
    • An ER-mitochondria tethering complex revealed by a synthetic biology screen
    • Kornmann, B., Currie, E., Collins, S. R., Schuldiner, M., Nunnari, J., Weissman, J. S., et al. (2009). An ER-mitochondria tethering complex revealed by a synthetic biology screen. Science 325, 477-481. doi: 10.1126/science.1175088
    • (2009) Science , vol.325 , pp. 477-481
    • Kornmann, B.1    Currie, E.2    Collins, S.R.3    Schuldiner, M.4    Nunnari, J.5    Weissman, J.S.6
  • 50
    • 84866936356 scopus 로고    scopus 로고
    • Dual targeting and retrograde translocation: regulators of plant nuclear gene expression can be sequestered by plastids
    • Krause, K., Oetke, S., and Krupinska, K. (2012). Dual targeting and retrograde translocation: regulators of plant nuclear gene expression can be sequestered by plastids. Int. J. Mol. Sci. 13, 11085-11101. doi: 10.3390/ijms130911085
    • (2012) Int. J. Mol. Sci , vol.13 , pp. 11085-11101
    • Krause, K.1    Oetke, S.2    Krupinska, K.3
  • 51
    • 84875186757 scopus 로고    scopus 로고
    • COX19 mediates the transduction of a mitochondrial redox signal from SCO1 that regulates ATP7A-mediated cellular copper efflux
    • Leary, S. C., Cobine, P. A., Nishimura, T., Verdijk, R. M., de Krijger, R., de Coo, R., et al. (2013). COX19 mediates the transduction of a mitochondrial redox signal from SCO1 that regulates ATP7A-mediated cellular copper efflux. Mol. Biol. Cell 24, 683-691. doi: 10.1091/mbc.E12-09-0705
    • (2013) Mol. Biol. Cell , vol.24 , pp. 683-691
    • Leary, S.C.1    Cobine, P.A.2    Nishimura, T.3    Verdijk, R.M.4    de Krijger, R.5    de Coo, R.6
  • 52
    • 28844499005 scopus 로고    scopus 로고
    • Mitochondrial cyclic AMP response element-binding protein (CREB) mediates mitochondrial gene expression and neuronal survival
    • Lee, J., Kim, C. H., Simon, D. K., Aminova, L. R., Andreyev, A. Y., Kushnareva, Y. E., et al. (2005). Mitochondrial cyclic AMP response element-binding protein (CREB) mediates mitochondrial gene expression and neuronal survival. J. Biol. Chem. 280, 40398-40401. doi: 10.1074/jbc.C500140200
    • (2005) J. Biol. Chem , vol.280 , pp. 40398-40401
    • Lee, J.1    Kim, C.H.2    Simon, D.K.3    Aminova, L.R.4    Andreyev, A.Y.5    Kushnareva, Y.E.6
  • 53
    • 77955106651 scopus 로고    scopus 로고
    • Folding-competent and folding-defective forms of ricin A chain have different fates after retrotranslocation from the endoplasmic reticulum
    • Li, S., Spooner, R. A., Allen, S. C., Guise, C. P., Ladds, G., Schnoder, T., et al. (2010). Folding-competent and folding-defective forms of ricin A chain have different fates after retrotranslocation from the endoplasmic reticulum. Mol. Biol. Cell 21, 2543-2554. doi: 10.1091/mbc.E09-08-0743
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2543-2554
    • Li, S.1    Spooner, R.A.2    Allen, S.C.3    Guise, C.P.4    Ladds, G.5    Schnoder, T.6
  • 54
    • 0035910069 scopus 로고    scopus 로고
    • Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation
    • Ma, J., and Lindquist, S. (2001). Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation. Proc. Natl. Acad. Sci. U.S.A. 98, 14955-14960. doi: 10.1073/pnas.011578098
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 14955-14960
    • Ma, J.1    Lindquist, S.2
  • 55
    • 0034717014 scopus 로고    scopus 로고
    • Death signal-induced localization of p53 protein to mitochondria A potential role in apoptotic signaling
    • Marchenko, N. D., Zaika, A., and Moll, U. M. (2000). Death signal-induced localization of p53 protein to mitochondria. A potential role in apoptotic signaling. J. Biol. Chem. 275, 16202-16212. doi: 10.1074/jbc.275.21.16202
    • (2000) J. Biol. Chem , vol.275 , pp. 16202-16212
    • Marchenko, N.D.1    Zaika, A.2    Moll, U.M.3
  • 56
    • 84897863239 scopus 로고    scopus 로고
    • Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control
    • McLelland, G. L., Soubannier, V., Chen, C. X., McBride, H. M., and Fon, E. A. (2014). Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control. EMBO J. 33, 282-295. doi: 10.1002/embj.201385902
    • (2014) EMBO J , vol.33 , pp. 282-295
    • McLelland, G.L.1    Soubannier, V.2    Chen, C.X.3    McBride, H.M.4    Fon, E.A.5
  • 57
    • 0037349289 scopus 로고    scopus 로고
    • p53 has a direct apoptogenic role at the mitochondria
    • Mihara, M., Erster, S., Zaika, A., Petrenko, O., Chittenden, T., Pancoska, P., et al. (2003). p53 has a direct apoptogenic role at the mitochondria. Mol. Cell 11, 577-590. doi: 10.1016/S1097-2765(03)00050-9
    • (2003) Mol. Cell , vol.11 , pp. 577-590
    • Mihara, M.1    Erster, S.2    Zaika, A.3    Petrenko, O.4    Chittenden, T.5    Pancoska, P.6
  • 58
    • 59449107366 scopus 로고    scopus 로고
    • By-passing the nonsense mutation in the 4 CV mouse model of muscular dystrophy by induced exon skipping
    • Mitrpant, C., Fletcher, S., Iversen, P. L., and Wilton, S. D. (2009). By-passing the nonsense mutation in the 4 CV mouse model of muscular dystrophy by induced exon skipping. J. Gene Med. 11, 46-56. doi: 10.1002/jgm.1265
    • (2009) J. Gene Med , vol.11 , pp. 46-56
    • Mitrpant, C.1    Fletcher, S.2    Iversen, P.L.3    Wilton, S.D.4
  • 59
    • 71049136017 scopus 로고    scopus 로고
    • Dual targeting of Nfs1 and discovery of its novel processing enzyme, Icp55
    • Naamati, A., Regev-Rudzki, N., Galperin, S., Lill, R., and Pines, O. (2009). Dual targeting of Nfs1 and discovery of its novel processing enzyme, Icp55. J. Biol. Chem. 284, 30200-30208. doi: 10.1074/jbc.M109.034694
    • (2009) J. Biol. Chem , vol.284 , pp. 30200-30208
    • Naamati, A.1    Regev-Rudzki, N.2    Galperin, S.3    Lill, R.4    Pines, O.5
  • 60
    • 84864744900 scopus 로고    scopus 로고
    • Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation
    • Nargund, A. M., Pellegrino, M. W., Fiorese, C. J., Baker, B. M., and Haynes, C. M. (2012). Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation. Science 337, 587-590. doi: 10.1126/science.1223560
    • (2012) Science , vol.337 , pp. 587-590
    • Nargund, A.M.1    Pellegrino, M.W.2    Fiorese, C.J.3    Baker, B.M.4    Haynes, C.M.5
  • 61
    • 0037174842 scopus 로고    scopus 로고
    • Characterization of COX19, a widely distributed gene required for expression of mitochondrial cytochrome oxidase
    • Nobrega, M. P., Bandeira, S. C., Beers, J., and Tzagoloff, A. (2002). Characterization of COX19, a widely distributed gene required for expression of mitochondrial cytochrome oxidase. J. Biol. Chem. 277, 40206-40211. doi: 10.1074/jbc.M207348200
    • (2002) J. Biol. Chem , vol.277 , pp. 40206-40211
    • Nobrega, M.P.1    Bandeira, S.C.2    Beers, J.3    Tzagoloff, A.4
  • 62
    • 84921774753 scopus 로고    scopus 로고
    • Mitochondrial UPR-regulated innate immunity provides resistance to pathogen infection
    • [Epub ahead of print]
    • Pellegrino, M. W., Nargund, A. M., Kirienko, N. V., Gillis, R., Fiorese, C. J., and Haynes, C. M. (2014). Mitochondrial UPR-regulated innate immunity provides resistance to pathogen infection. Nature. doi: 10.1038/nature13818. [Epub ahead of print]
    • (2014) Nature
    • Pellegrino, M.W.1    Nargund, A.M.2    Kirienko, N.V.3    Gillis, R.4    Fiorese, C.J.5    Haynes, C.M.6
  • 63
    • 84875962374 scopus 로고    scopus 로고
    • Structural features within the nascent chain regulate alternative targeting of secretory proteins to mitochondria
    • Pfeiffer, N. V., Dirndorfer, D., Lang, S., Resenberger, U. K., Restelli, L. M., Hemion, C., et al. (2013). Structural features within the nascent chain regulate alternative targeting of secretory proteins to mitochondria. EMBO J. 32, 1036-1051. doi: 10.1038/emboj.2013.46
    • (2013) EMBO J , vol.32 , pp. 1036-1051
    • Pfeiffer, N.V.1    Dirndorfer, D.2    Lang, S.3    Resenberger, U.K.4    Restelli, L.M.5    Hemion, C.6
  • 64
    • 58149102066 scopus 로고    scopus 로고
    • The disulfide relay system of mitochondria is required for the biogenesis of mitochondrial Ccs1 and Sod1
    • Reddehase, S., Grumbt, B., Neupert, W., and Hell, K. (2009). The disulfide relay system of mitochondria is required for the biogenesis of mitochondrial Ccs1 and Sod1. J. Mol. Biol. 385, 331-338. doi: 10.1016/j.jmb.2008.10.088
    • (2009) J. Mol. Biol , vol.385 , pp. 331-338
    • Reddehase, S.1    Grumbt, B.2    Neupert, W.3    Hell, K.4
  • 65
    • 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, N. N., and Pines, O. (2005). Yeast aconitase in two locations and two metabolic pathways: seeing small amounts is believing. Mol. Biol. Cell 16, 4163-4171. doi: 10.1091/mbc.E04-11-1028
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4163-4171
    • Regev-Rudzki, N.1    Karniely, S.2    Ben-Haim, N.N.3    Pines, O.4
  • 66
    • 34547619977 scopus 로고    scopus 로고
    • Eclipsed distribution: a phenomenon of dual targeting of protein and its significance
    • Regev-Rudzki, N., and Pines, O. (2007). Eclipsed distribution: a phenomenon of dual targeting of protein and its significance. Bioessays 29, 772-782. doi: 10.1002/bies.20609
    • (2007) Bioessays , vol.29 , pp. 772-782
    • Regev-Rudzki, N.1    Pines, O.2
  • 67
    • 49649109965 scopus 로고    scopus 로고
    • The mitochondrial targeting sequence tilts the balance between mitochondrial and cytosolic dual localization
    • Regev-Rudzki, N., Yogev, O., and Pines, O. (2008). The mitochondrial targeting sequence tilts the balance between mitochondrial and cytosolic dual localization. J. Cell Sci. 121, 2423-2431. doi: 10.1242/jcs.029207
    • (2008) J. Cell Sci , vol.121 , pp. 2423-2431
    • Regev-Rudzki, N.1    Yogev, O.2    Pines, O.3
  • 68
    • 0037174926 scopus 로고    scopus 로고
    • Bimodal targeting of microsomal CYP2E1 to mitochondria through activation of an N-terminal chimeric signal by cAMP-mediated phosphorylation
    • Robin, M. A., Anandatheerthavarada, H. K., Biswas, G., Sepuri, N. B., Gordon, D. M., Pain, D., et al. (2002). Bimodal targeting of microsomal CYP2E1 to mitochondria through activation of an N-terminal chimeric signal by cAMP-mediated phosphorylation. J. Biol. Chem. 277, 40583-40593. doi: 10.1074/jbc.M203292200
    • (2002) J. Biol. Chem , vol.277 , pp. 40583-40593
    • Robin, M.A.1    Anandatheerthavarada, H.K.2    Biswas, G.3    Sepuri, N.B.4    Gordon, D.M.5    Pain, D.6
  • 69
    • 13844272923 scopus 로고    scopus 로고
    • Mitochondrial hTERT exacerbates free-radical-mediated mtDNA damage
    • Santos, J. H., Meyer, J. N., Skorvaga, M., Annab, L. A., and Van Houten, B. (2004). Mitochondrial hTERT exacerbates free-radical-mediated mtDNA damage. Aging Cell 3, 399-411. doi: 10.1111/j.1474-9728.2004.00124.x
    • (2004) Aging Cell , vol.3 , pp. 399-411
    • Santos, J.H.1    Meyer, J.N.2    Skorvaga, M.3    Annab, L.A.4    Van Houten, B.5
  • 70
    • 0035824654 scopus 로고    scopus 로고
    • Mitochondrial and cytosolic isoforms of yeast fumarase are derivatives of a single translation product and have identical amino termini
    • Sass, E., Blachinsky, E., Karniely, S., and Pines, O. (2001). Mitochondrial and cytosolic isoforms of yeast fumarase are derivatives of a single translation product and have identical amino termini. J. Biol. Chem. 276, 46111-46117. doi: 10.1074/jbc.M106061200
    • (2001) J. Biol. Chem , vol.276 , pp. 46111-46117
    • Sass, E.1    Blachinsky, E.2    Karniely, S.3    Pines, O.4
  • 71
    • 0242413667 scopus 로고    scopus 로고
    • Folding of fumarase during mitochondrial import determines its dual targeting in yeast
    • Sass, E., Karniely, S., and Pines, O. (2003). Folding of fumarase during mitochondrial import determines its dual targeting in yeast. J. Biol. Chem. 278, 45109-45116. doi: 10.1074/jbc.M302344200
    • (2003) J. Biol. Chem , vol.278 , pp. 45109-45116
    • Sass, E.1    Karniely, S.2    Pines, O.3
  • 72
    • 35548992416 scopus 로고    scopus 로고
    • Simian Virus 40 depends on ER protein folding and quality control factors for entry into host cells
    • Schelhaas, M., Malmstrom, J., Pelkmans, L., Haugstetter, J., Ellgaard, L., Grunewald, K., et al. (2007). Simian Virus 40 depends on ER protein folding and quality control factors for entry into host cells. Cell 131, 516-529. doi: 10.1016/j.cell.2007.09.038
    • (2007) Cell , vol.131 , pp. 516-529
    • Schelhaas, M.1    Malmstrom, J.2    Pelkmans, L.3    Haugstetter, J.4    Ellgaard, L.5    Grunewald, K.6
  • 73
    • 78651487830 scopus 로고    scopus 로고
    • Regulation of mitochondrial protein import by cytosolic kinases
    • Schmidt, O., Harbauer, A. B., Rao, S., Eyrich, B., Zahedi, R. P., Stojanovski, D., et al. (2011). Regulation of mitochondrial protein import by cytosolic kinases. Cell 144, 227-239. doi: 10.1016/j.cell.2010.12.015
    • (2011) Cell , vol.144 , pp. 227-239
    • Schmidt, O.1    Harbauer, A.B.2    Rao, S.3    Eyrich, B.4    Zahedi, R.P.5    Stojanovski, D.6
  • 74
    • 84855905939 scopus 로고    scopus 로고
    • Human telomerase acts as a hTR-independent reverse transcriptase in mitochondria
    • Sharma, N. K., Reyes, A., Green, P., Caron, M. J., Bonini, M. G., Gordon, D. M., et al. (2012). Human telomerase acts as a hTR-independent reverse transcriptase in mitochondria. Nucleic Acids Res. 40, 712-725. doi: 10.1093/nar/gkr758
    • (2012) Nucleic Acids Res , vol.40 , pp. 712-725
    • Sharma, N.K.1    Reyes, A.2    Green, P.3    Caron, M.J.4    Bonini, M.G.5    Gordon, D.M.6
  • 75
    • 0030013835 scopus 로고    scopus 로고
    • Identification of endoplasmic reticulum in the primitive eukaryote Giardia lamblia using cryoelectron microscopy and antibody to Bip
    • Soltys, B. J., Falah, M., and Gupta, R. S. (1996). Identification of endoplasmic reticulum in the primitive eukaryote Giardia lamblia using cryoelectron microscopy and antibody to Bip. J. Cell Sci. 109(Pt 7), 1909-1917
    • (1996) J. Cell Sci , vol.109 , pp. 1909-1917
    • Soltys, B.J.1    Falah, M.2    Gupta, R.S.3
  • 76
    • 0035999970 scopus 로고    scopus 로고
    • Competition of spontaneous protein folding and mitochondrial import causes dual subcellular location of major adenylate kinase
    • Strobel, G., Zollner, A., Angermayr, M., and Bandlow, W. (2002). Competition of spontaneous protein folding and mitochondrial import causes dual subcellular location of major adenylate kinase. Mol. Biol. Cell 13, 1439-1448. doi: 10.1091/mbc.01-08-0396
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1439-1448
    • Strobel, G.1    Zollner, A.2    Angermayr, M.3    Bandlow, W.4
  • 77
    • 0035851122 scopus 로고    scopus 로고
    • A fraction of yeast Cu, Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria A physiological role for SOD1 in guarding against mitochondrial oxidative damage
    • Sturtz, L. A., Diekert, K., Jensen, L. T., Lill, R., and Culotta, V. C. (2001). A fraction of yeast Cu, Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage. J. Biol. Chem. 276, 38084-38089. doi: 10.1074/jbc.M105296200
    • (2001) J. Biol. Chem , vol.276 , pp. 38084-38089
    • Sturtz, L.A.1    Diekert, K.2    Jensen, L.T.3    Lill, R.4    Culotta, V.C.5
  • 78
    • 84908085343 scopus 로고    scopus 로고
    • A new pathway for mitochondrial quality control: mitochondrial-derived vesicles
    • Sugiura, A., McLelland, G. L., Fon, E. A., and McBride, H. M. (2014). A new pathway for mitochondrial quality control: mitochondrial-derived vesicles. EMBO J. 33, 2142-2156. doi: 10.15252/embj.201488104
    • (2014) EMBO J , vol.33 , pp. 2142-2156
    • Sugiura, A.1    McLelland, G.L.2    Fon, E.A.3    McBride, H.M.4
  • 79
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • Tsai, B., Rodighiero, C., Lencer, W. I., and Rapoport, T. A. (2001). Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell 104, 937-948. doi: 10.1016/S0092-8674(01)00289-6
    • (2001) Cell , vol.104 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3    Rapoport, T.A.4
  • 80
    • 0035137178 scopus 로고    scopus 로고
    • Pir1p mediates translocation of the yeast Apn1p endonuclease into the mitochondria to maintain genomic stability
    • Vongsamphanh, R., Fortier, P. K., and Ramotar, D. (2001). Pir1p mediates translocation of the yeast Apn1p endonuclease into the mitochondria to maintain genomic stability. Mol. Cell Biol. 21, 1647-1655. doi: 10.1128/MCB.21.5.1647-1655.2001
    • (2001) Mol. Cell Biol , vol.21 , pp. 1647-1655
    • Vongsamphanh, R.1    Fortier, P.K.2    Ramotar, D.3
  • 81
    • 59849101586 scopus 로고    scopus 로고
    • Function of mitochondrial Stat3 in cellular respiration
    • Wegrzyn, J., Potla, R., Chwae, Y. J., Sepuri, N. B., Zhang, Q., Koeck, T., et al. (2009). Function of mitochondrial Stat3 in cellular respiration. Science 323, 793-797. doi: 10.1126/science.1164551
    • (2009) Science , vol.323 , pp. 793-797
    • Wegrzyn, J.1    Potla, R.2    Chwae, Y.J.3    Sepuri, N.B.4    Zhang, Q.5    Koeck, T.6
  • 82
    • 0035476688 scopus 로고    scopus 로고
    • Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
    • Yedidia, Y., Horonchik, L., Tzaban, S., Yanai, A., and Taraboulos, A. (2001). Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein. EMBO J. 20, 5383-5391. doi: 10.1093/emboj/20.19.5383
    • (2001) EMBO J , vol.20 , pp. 5383-5391
    • Yedidia, Y.1    Horonchik, L.2    Tzaban, S.3    Yanai, A.4    Taraboulos, A.5
  • 83
    • 35748984947 scopus 로고    scopus 로고
    • Translation-coupled translocation of yeast fumarase into mitochondria in vivo
    • Yogev, O., Karniely, S., and Pines, O. (2007). Translation-coupled translocation of yeast fumarase into mitochondria in vivo. J. Biol. Chem. 282, 29222-29229. doi: 10.1074/jbc.M704201200
    • (2007) J. Biol. Chem , vol.282 , pp. 29222-29229
    • Yogev, O.1    Karniely, S.2    Pines, O.3
  • 84
    • 80255122737 scopus 로고    scopus 로고
    • Fumarase: a paradigm of dual targeting and dual localized functions
    • Yogev, O., Naamati, A., and Pines, O. (2011). Fumarase: a paradigm of dual targeting and dual localized functions. FEBS J. 278, 4230-4242. doi: 10.1111/j.1742-4658.2011.08359.x
    • (2011) FEBS J , vol.278 , pp. 4230-4242
    • Yogev, O.1    Naamati, A.2    Pines, O.3
  • 85
    • 79851516332 scopus 로고    scopus 로고
    • Dual targeting of mitochondrial proteins: mechanism, regulation and function
    • Yogev, O., and Pines, O. (2011). Dual targeting of mitochondrial proteins: mechanism, regulation and function. Biochim. Biophys. Acta 1808, 1012-1020. doi: 10.1016/j.bbamem.2010.07.004
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 1012-1020
    • Yogev, O.1    Pines, O.2
  • 86
    • 77950553262 scopus 로고    scopus 로고
    • Fumarase: a mitochondrial metabolic enzyme and a cytosolic/nuclear component of the DNA damage response
    • Yogev, O., Singer, E., Shaulian, E., Goldberg, M., Fox, T. D., and Pines, O. (2010). Fumarase: a mitochondrial metabolic enzyme and a cytosolic/nuclear component of the DNA damage response. PLoS Biol. 8:e1000328. doi: 10.1371/journal.pbio.1000328
    • (2010) PLoS Biol , vol.8
    • Yogev, O.1    Singer, E.2    Shaulian, E.3    Goldberg, M.4    Fox, T.D.5    Pines, O.6
  • 87
    • 18144382261 scopus 로고    scopus 로고
    • p53 translocation to mitochondria precedes its nuclear translocation and targets mitochondrial oxidative defense protein-manganese superoxide dismutase
    • Zhao, Y., Chaiswing, L., Velez, J. M., Batinic-Haberle, I., Colburn, N. H., Oberley, T. D., et al. (2005). p53 translocation to mitochondria precedes its nuclear translocation and targets mitochondrial oxidative defense protein-manganese superoxide dismutase. Cancer Res. 65, 3745-3750. doi: 10.1158/0008-5472.CAN-04-3835
    • (2005) Cancer Res , vol.65 , pp. 3745-3750
    • Zhao, Y.1    Chaiswing, L.2    Velez, J.M.3    Batinic-Haberle, I.4    Colburn, N.H.5    Oberley, T.D.6


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