메뉴 건너뛰기




Volumn 1772, Issue 5, 2007, Pages 509-523

Mitochondrial protein import and human health and disease

Author keywords

Human health and disease; Mitochondria; Protein targeting; Protein translocation

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALANINE AMINOTRANSFERASE; CHAPERONE; DNA; HEAT SHOCK PROTEIN 10; HEAT SHOCK PROTEIN 60; LIOTHYRONINE; MANGANESE SUPEROXIDE DISMUTASE; MEMBRANE PROTEIN; MITOCHONDRIAL PROTEIN; PYRUVATE DEHYDROGENASE; THYROID HORMONE;

EID: 34247127747     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2006.12.002     Document Type: Review
Times cited : (91)

References (238)
  • 1
    • 0016753216 scopus 로고
    • Transfer of proteins across membranes: I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma
    • Blobel G., and Dobberstein B. Transfer of proteins across membranes: I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J. Cell Biol. 67 (1975) 835-851
    • (1975) J. Cell Biol. , vol.67 , pp. 835-851
    • Blobel, G.1    Dobberstein, B.2
  • 2
    • 0016752682 scopus 로고
    • Transfer to proteins across membranes: II. Reconstitution of functional rough microsomes from heterologous components
    • Blobel G., and Dobberstein B. Transfer to proteins across membranes: II. Reconstitution of functional rough microsomes from heterologous components. J. Cell Biol. 67 (1975) 852-862
    • (1975) J. Cell Biol. , vol.67 , pp. 852-862
    • Blobel, G.1    Dobberstein, B.2
  • 3
    • 0017681546 scopus 로고
    • Cell-free synthesis of fish preproinsulin, and processing by heterologous mammalian microsomal membranes
    • Shields D., and Blobel G. Cell-free synthesis of fish preproinsulin, and processing by heterologous mammalian microsomal membranes. Proc. Natl. Acad. Sci. U. S. A. 74 (1977) 2059-2063
    • (1977) Proc. Natl. Acad. Sci. U. S. A. , vol.74 , pp. 2059-2063
    • Shields, D.1    Blobel, G.2
  • 4
    • 21644476127 scopus 로고    scopus 로고
    • Beyond the signal sequence: protein routing in health and disease
    • Castro-Fernandez C., Maya-Nunez G., and Conn P.M. Beyond the signal sequence: protein routing in health and disease. Endocr. Rev. 26 (2005) 479-503
    • (2005) Endocr. Rev. , vol.26 , pp. 479-503
    • Castro-Fernandez, C.1    Maya-Nunez, G.2    Conn, P.M.3
  • 5
    • 0037009108 scopus 로고    scopus 로고
    • Import and assembly of proteins into mitochondria of mammalian cells
    • Hoogenraad N., Ward L., and Ryan M. Import and assembly of proteins into mitochondria of mammalian cells. Biochim. Biophys. Acta 1592 (2002) 97-105
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 97-105
    • Hoogenraad, N.1    Ward, L.2    Ryan, M.3
  • 6
    • 33746575844 scopus 로고    scopus 로고
    • Evolution of the molecular machines for protein import into mitochondria
    • Dolezal P., 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
    • Dolezal, P.1    Likic, V.2    Tachezy, J.3    Lithgow, T.4
  • 7
    • 0022731676 scopus 로고
    • Mitochondrial targeting sequences may form amphiphilic helices
    • vonHeijne G. Mitochondrial targeting sequences may form amphiphilic helices. EMBO J. 5 (1986) 1335-1342
    • (1986) EMBO J. , vol.5 , pp. 1335-1342
    • vonHeijne, G.1
  • 8
    • 0022725788 scopus 로고
    • A chemically synthesized pre-sequence of an imported mitochondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers
    • Roise D., Horvath S.J., Tomich J.M., Richards J.H., and Schatz G. A chemically synthesized pre-sequence of an imported mitochondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers. EMBO J. 5 (1986) 1327-1334
    • (1986) EMBO J. , vol.5 , pp. 1327-1334
    • Roise, D.1    Horvath, S.J.2    Tomich, J.M.3    Richards, J.H.4    Schatz, G.5
  • 9
    • 0023920458 scopus 로고
    • Mitochondrial presequences
    • Roise D., and Schatz G. Mitochondrial presequences. J. Biol. Chem. 263 (1988) 4509-4511
    • (1988) J. Biol. Chem. , vol.263 , pp. 4509-4511
    • Roise, D.1    Schatz, G.2
  • 10
    • 0024442722 scopus 로고
    • Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
    • von Heijne G. Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature 341 (1989) 456-458
    • (1989) Nature , vol.341 , pp. 456-458
    • von Heijne, G.1
  • 11
    • 0025077695 scopus 로고
    • 2D NMR and structural model for a mitochondrial signal peptide bound to a micelle
    • Karslake C., Piotto M.E., Pak Y.K., Weiner H., and Gorenstein D.G. 2D NMR and structural model for a mitochondrial signal peptide bound to a micelle. Biochemistry 29 (1990) 9872-9878
    • (1990) Biochemistry , vol.29 , pp. 9872-9878
    • Karslake, C.1    Piotto, M.E.2    Pak, Y.K.3    Weiner, H.4    Gorenstein, D.G.5
  • 12
    • 0032704556 scopus 로고    scopus 로고
    • Positively charged residues, the helical conformation and the structural flexibility of the leader sequence of pALDH are important for recognition by hTom20
    • Schleiff E., Heard T.S., and Weiner H. Positively charged residues, the helical conformation and the structural flexibility of the leader sequence of pALDH are important for recognition by hTom20. FEBS Lett. 461 (1999) 9-12
    • (1999) FEBS Lett. , vol.461 , pp. 9-12
    • Schleiff, E.1    Heard, T.S.2    Weiner, H.3
  • 13
    • 0034598904 scopus 로고    scopus 로고
    • Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20
    • Abe Y., Shodai T., Muto T., Mihara K., Torii H., Nishikawa S., Endo T., and Kohda D. Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20. Cell 100 (2000) 551-560
    • (2000) Cell , vol.100 , pp. 551-560
    • Abe, Y.1    Shodai, T.2    Muto, T.3    Mihara, K.4    Torii, H.5    Nishikawa, S.6    Endo, T.7    Kohda, D.8
  • 14
    • 0037466277 scopus 로고    scopus 로고
    • Peptide library approach with a disulfide tether to refine the tom20 recognition motif in mitochondrial presequences
    • Obita T., Muto T., Endo T., and Kohda D. Peptide library approach with a disulfide tether to refine the tom20 recognition motif in mitochondrial presequences. J. Mol. Biol. 328 (2003) 495-504
    • (2003) J. Mol. Biol. , vol.328 , pp. 495-504
    • Obita, T.1    Muto, T.2    Endo, T.3    Kohda, D.4
  • 15
    • 1842368473 scopus 로고    scopus 로고
    • Just follow the acid chain
    • Schatz G. Just follow the acid chain. Nature 388 (1997) 121-122
    • (1997) Nature , vol.388 , pp. 121-122
    • Schatz, G.1
  • 16
    • 0032527780 scopus 로고    scopus 로고
    • Interaction of mitochondrial targeting signals with acidic receptor domains along the protein import pathway: evidence for the 'acid chain' hypothesis
    • Komiya T., Rospert S., Koehler C., Looser R., Schatz G., and Mihara K. Interaction of mitochondrial targeting signals with acidic receptor domains along the protein import pathway: evidence for the 'acid chain' hypothesis. EMBO J. 17 (1998) 3886-3898
    • (1998) EMBO J. , vol.17 , pp. 3886-3898
    • Komiya, T.1    Rospert, S.2    Koehler, C.3    Looser, R.4    Schatz, G.5    Mihara, K.6
  • 17
    • 0027295559 scopus 로고
    • Import, processing, and two-dimensional NMR structure of a linker-deleted signal peptide of rat liver mitochondrial aldehyde dehydrogenase
    • Thornton K., Wang Y., Weiner H., and Gorenstein D.G. Import, processing, and two-dimensional NMR structure of a linker-deleted signal peptide of rat liver mitochondrial aldehyde dehydrogenase. J. Biol. Chem. 268 (1993) 19906-19914
    • (1993) J. Biol. Chem. , vol.268 , pp. 19906-19914
    • Thornton, K.1    Wang, Y.2    Weiner, H.3    Gorenstein, D.G.4
  • 18
    • 0028068519 scopus 로고
    • Structure of the signal sequences for two mitochondrial matrix proteins that are not proteolytically processed upon import
    • Hammen P.K., Gorenstein D.G., and Weiner H. Structure of the signal sequences for two mitochondrial matrix proteins that are not proteolytically processed upon import. Biochemistry 33 (1994) 8610-8617
    • (1994) Biochemistry , vol.33 , pp. 8610-8617
    • Hammen, P.K.1    Gorenstein, D.G.2    Weiner, H.3
  • 19
    • 0032491415 scopus 로고    scopus 로고
    • A regional net charge and structural compensation model to explain how negatively charged amino acids can be accepted within a mitochondrial leader sequence
    • Heard T.S., and Weiner H. A regional net charge and structural compensation model to explain how negatively charged amino acids can be accepted within a mitochondrial leader sequence. J. Biol. Chem. 273 (1998) 29389-29393
    • (1998) J. Biol. Chem. , vol.273 , pp. 29389-29393
    • Heard, T.S.1    Weiner, H.2
  • 20
    • 0242607644 scopus 로고    scopus 로고
    • Finding the right organelle. Targeting signals in mitochondrial outer-membrane proteins
    • Rapaport D. Finding the right organelle. Targeting signals in mitochondrial outer-membrane proteins. EMBO Rep. 4 (2003) 948-952
    • (2003) EMBO Rep. , vol.4 , pp. 948-952
    • Rapaport, D.1
  • 21
    • 0035283084 scopus 로고    scopus 로고
    • The three modules of ADP/ATP carrier cooperate in receptor recruitment and translocation into mitochondria
    • Wiedemann N., Pfanner N., and Ryan M.T. The three modules of ADP/ATP carrier cooperate in receptor recruitment and translocation into mitochondria. EMBO J. 20 (2001) 951-960
    • (2001) EMBO J. , vol.20 , pp. 951-960
    • Wiedemann, N.1    Pfanner, N.2    Ryan, M.T.3
  • 22
    • 0033564856 scopus 로고    scopus 로고
    • Transport of the ADP/ATP carrier of mitochondria from the TOM complex to the TIM22.54 complex
    • Endres M., Neupert W., and Brunner M. Transport of the ADP/ATP carrier of mitochondria from the TOM complex to the TIM22.54 complex. EMBO J. 18 (1999) 3214-3221
    • (1999) EMBO J. , vol.18 , pp. 3214-3221
    • Endres, M.1    Neupert, W.2    Brunner, M.3
  • 23
    • 0037009090 scopus 로고    scopus 로고
    • Delivery of nascent polypeptides to the mitochondrial surface
    • Beddoe T., and Lithgow T. Delivery of nascent polypeptides to the mitochondrial surface. Biochim. Biophys. Acta 1592 (2002) 35-39
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 35-39
    • Beddoe, T.1    Lithgow, T.2
  • 24
    • 0030769419 scopus 로고    scopus 로고
    • Differential recognition of preproteins by the purified cytosolic domains of the mitochondrial import receptors Tom20, Tom22, and Tom70
    • Brix J., Dietmeier K., and Pfanner N. Differential recognition of preproteins by the purified cytosolic domains of the mitochondrial import receptors Tom20, Tom22, and Tom70. J. Biol. Chem. 272 (1997) 20730-20735
    • (1997) J. Biol. Chem. , vol.272 , pp. 20730-20735
    • Brix, J.1    Dietmeier, K.2    Pfanner, N.3
  • 25
    • 0030752305 scopus 로고    scopus 로고
    • Binding of mitochondrial precursor proteins to the cytoplasmic domains of the import receptors Tom70 and Tom20 is determined by cytoplasmic chaperones
    • Komiya T., Rospert S., Schatz G., and Mihara K. Binding of mitochondrial precursor proteins to the cytoplasmic domains of the import receptors Tom70 and Tom20 is determined by cytoplasmic chaperones. EMBO J. 16 (1997) 4267-4275
    • (1997) EMBO J. , vol.16 , pp. 4267-4275
    • Komiya, T.1    Rospert, S.2    Schatz, G.3    Mihara, K.4
  • 26
    • 0031046892 scopus 로고    scopus 로고
    • Participation of the import receptor Tom20 in protein import into mammalian mitochondria: analyses in vitro and in cultured cells
    • Terada K., Kanazawa M., Yano M., Hanson B., Hoogenraad N., and Mori M. Participation of the import receptor Tom20 in protein import into mammalian mitochondria: analyses in vitro and in cultured cells. FEBS Lett. 403 (1997) 309-312
    • (1997) FEBS Lett. , vol.403 , pp. 309-312
    • Terada, K.1    Kanazawa, M.2    Yano, M.3    Hanson, B.4    Hoogenraad, N.5    Mori, M.6
  • 27
    • 0142027923 scopus 로고    scopus 로고
    • AIP is a mitochondrial import mediator that binds to both import receptor Tom20 and preproteins
    • Yano M., Terada K., and Mori M. AIP is a mitochondrial import mediator that binds to both import receptor Tom20 and preproteins. J. Cell Biol. 163 (2003) 45-56
    • (2003) J. Cell Biol. , vol.163 , pp. 45-56
    • Yano, M.1    Terada, K.2    Mori, M.3
  • 28
    • 0030830249 scopus 로고    scopus 로고
    • The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding
    • Terada K., Kanazawa M., Bukau B., and Mori M. The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding. J. Cell Biol. 139 (1997) 1089-1095
    • (1997) J. Cell Biol. , vol.139 , pp. 1089-1095
    • Terada, K.1    Kanazawa, M.2    Bukau, B.3    Mori, M.4
  • 29
    • 0034637603 scopus 로고    scopus 로고
    • Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70
    • Terada K., and Mori M. Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70. J. Biol. Chem. 275 (2000) 24728-24734
    • (2000) J. Biol. Chem. , vol.275 , pp. 24728-24734
    • Terada, K.1    Mori, M.2
  • 30
    • 0037428164 scopus 로고    scopus 로고
    • Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
    • Young J.C., Hoogenraad N.J., and Hartl F.U. Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 112 (2003) 41-50
    • (2003) Cell , vol.112 , pp. 41-50
    • Young, J.C.1    Hoogenraad, N.J.2    Hartl, F.U.3
  • 31
    • 0036558288 scopus 로고    scopus 로고
    • Characterization of rat TOM70 as a receptor of the preprotein translocase of the mitochondrial outer membrane
    • Suzuki H., Maeda M., and Mihara K. Characterization of rat TOM70 as a receptor of the preprotein translocase of the mitochondrial outer membrane. J. Cell Sci. 115 (2002) 1895-1905
    • (2002) J. Cell Sci. , vol.115 , pp. 1895-1905
    • Suzuki, H.1    Maeda, M.2    Mihara, K.3
  • 32
    • 0030045427 scopus 로고    scopus 로고
    • Cytoplasmic chaperones determine the targeting pathway of precursor proteins to mitochondria
    • Komiya T., Sakaguchi M., and Mihara K. Cytoplasmic chaperones determine the targeting pathway of precursor proteins to mitochondria. EMBO J. 15 (1996) 399-407
    • (1996) EMBO J. , vol.15 , pp. 399-407
    • Komiya, T.1    Sakaguchi, M.2    Mihara, K.3
  • 33
    • 0028948675 scopus 로고
    • The yeast mitochondrial protein import receptor Mas20p binds precursor proteins through electrostatic interaction with the positively charged presequence
    • Haucke V., Lithgow T., Rospert S., Hahne K., and Schatz G. The yeast mitochondrial protein import receptor Mas20p binds precursor proteins through electrostatic interaction with the positively charged presequence. J. Biol. Chem. 270 (1995) 5565-5570
    • (1995) J. Biol. Chem. , vol.270 , pp. 5565-5570
    • Haucke, V.1    Lithgow, T.2    Rospert, S.3    Hahne, K.4    Schatz, G.5
  • 34
    • 0027164641 scopus 로고
    • The mitochondrial receptor complex: a central role of MOM22 in mediating preprotein transfer from receptors to the general insertion pore
    • Kiebler M., Keil P., Schneider H., van der Klei I.J., Pfanner N., and Neupert W. The mitochondrial receptor complex: a central role of MOM22 in mediating preprotein transfer from receptors to the general insertion pore. Cell 74 (1993) 483-492
    • (1993) Cell , vol.74 , pp. 483-492
    • Kiebler, M.1    Keil, P.2    Schneider, H.3    van der Klei, I.J.4    Pfanner, N.5    Neupert, W.6
  • 35
    • 0037009129 scopus 로고    scopus 로고
    • The mitochondrial import machinery: preprotein-conducting channels with binding sites for presequences
    • Pfanner N., and Chacinska A. The mitochondrial import machinery: preprotein-conducting channels with binding sites for presequences. Biochim. Biophys. Acta 1592 (2002) 15-24
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 15-24
    • Pfanner, N.1    Chacinska, A.2
  • 36
    • 0031741738 scopus 로고    scopus 로고
    • Preprotein translocase of the outer mitochondrial membrane: molecular dissection and assembly of the general import pore complex
    • Dekker P.J., Ryan M.T., Brix J., Muller H., Honlinger A., and Pfanner N. Preprotein translocase of the outer mitochondrial membrane: molecular dissection and assembly of the general import pore complex. Mol. Cell. Biol. 18 (1998) 6515-6524
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6515-6524
    • Dekker, P.J.1    Ryan, M.T.2    Brix, J.3    Muller, H.4    Honlinger, A.5    Pfanner, N.6
  • 38
    • 0034531390 scopus 로고    scopus 로고
    • Characterization of Rat TOM40, a central component of the preprotein translocase of the mitochondrial outer membrane
    • Suzuki H., Okazawa Y., Komiya T., Saeki K., Mekada E., Kitada S., Ito A., and Mihara K. Characterization of Rat TOM40, a central component of the preprotein translocase of the mitochondrial outer membrane. J. Biol. Chem. 275 (2000) 37930-37936
    • (2000) J. Biol. Chem. , vol.275 , pp. 37930-37936
    • Suzuki, H.1    Okazawa, Y.2    Komiya, T.3    Saeki, K.4    Mekada, E.5    Kitada, S.6    Ito, A.7    Mihara, K.8
  • 40
    • 2442697922 scopus 로고    scopus 로고
    • Targeting and assembly of rat mitochondrial translocase of outer membrane 22 (TOM22) into the TOM complex
    • Nakamura Y., Suzuki H., Sakaguchi M., and Mihara K. Targeting and assembly of rat mitochondrial translocase of outer membrane 22 (TOM22) into the TOM complex. J. Biol. Chem. 279 (2004) 21223-21232
    • (2004) J. Biol. Chem. , vol.279 , pp. 21223-21232
    • Nakamura, Y.1    Suzuki, H.2    Sakaguchi, M.3    Mihara, K.4
  • 41
    • 9644263992 scopus 로고    scopus 로고
    • Membrane-embedded C-terminal segment of rat mitochondrial TOM40 constitutes protein-conducting pore with enriched beta-structure
    • Suzuki H., Kadowaki T., Maeda M., Sasaki H., Nabekura J., Sakaguchi M., and Mihara K. Membrane-embedded C-terminal segment of rat mitochondrial TOM40 constitutes protein-conducting pore with enriched beta-structure. J. Biol. Chem. 279 (2004) 50619-50629
    • (2004) J. Biol. Chem. , vol.279 , pp. 50619-50629
    • Suzuki, H.1    Kadowaki, T.2    Maeda, M.3    Sasaki, H.4    Nabekura, J.5    Sakaguchi, M.6    Mihara, K.7
  • 42
    • 0032188847 scopus 로고    scopus 로고
    • Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins
    • Hill K., Model K., Ryan M.T., Dietmeier K., Martin F., Wagner R., and Pfanner N. Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins. Nature 395 (1998) 516-521
    • (1998) Nature , vol.395 , pp. 516-521
    • Hill, K.1    Model, K.2    Ryan, M.T.3    Dietmeier, K.4    Martin, F.5    Wagner, R.6    Pfanner, N.7
  • 44
    • 27744543167 scopus 로고    scopus 로고
    • How does the TOM complex mediate insertion of precursor proteins into the mitochondrial outer membrane?
    • Rapaport D. How does the TOM complex mediate insertion of precursor proteins into the mitochondrial outer membrane?. J. Cell Biol. 171 (2005) 419-423
    • (2005) J. Cell Biol. , vol.171 , pp. 419-423
    • Rapaport, D.1
  • 48
    • 27844456862 scopus 로고    scopus 로고
    • Membrane protein insertion: mixing eukaryotic and prokaryotic concepts
    • Schleiff E., and Soll J. Membrane protein insertion: mixing eukaryotic and prokaryotic concepts. EMBO Rep. 6 (2005) 1023-1027
    • (2005) EMBO Rep. , vol.6 , pp. 1023-1027
    • Schleiff, E.1    Soll, J.2
  • 49
    • 0345861754 scopus 로고    scopus 로고
    • The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria
    • Gentle I., Gabriel K., Beech P., Waller R., and Lithgow T. The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria. J. Cell Biol. 164 (2004) 19-24
    • (2004) J. Cell Biol. , vol.164 , pp. 19-24
    • Gentle, I.1    Gabriel, K.2    Beech, P.3    Waller, R.4    Lithgow, T.5
  • 51
    • 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
  • 53
    • 0031737102 scopus 로고    scopus 로고
    • Characterization of the initial steps of precursor import into rat liver mitoplasts
    • Ishihara N., Komiya T., Sakaguchi M., Ito A., and Mihara K. Characterization of the initial steps of precursor import into rat liver mitoplasts. J. Biochem. (Tokyo) 124 (1998) 824-834
    • (1998) J. Biochem. (Tokyo) , vol.124 , pp. 824-834
    • Ishihara, N.1    Komiya, T.2    Sakaguchi, M.3    Ito, A.4    Mihara, K.5
  • 56
    • 0037111988 scopus 로고    scopus 로고
    • Tim50 is a subunit of the TIM23 complex that links protein translocation across the outer and inner mitochondrial membranes
    • Yamamoto H., Esaki M., Kanamori T., Tamura Y., Nishikawa S., and Endo T. Tim50 is a subunit of the TIM23 complex that links protein translocation across the outer and inner mitochondrial membranes. Cell 111 (2002) 519-528
    • (2002) Cell , vol.111 , pp. 519-528
    • Yamamoto, H.1    Esaki, M.2    Kanamori, T.3    Tamura, Y.4    Nishikawa, S.5    Endo, T.6
  • 57
    • 0029894716 scopus 로고    scopus 로고
    • Role of the intermembrane-space domain of the preprotein receptor Tom22 in protein import into mitochondria
    • Court D., Nargang F.E., Steiner H., Hodges R.S., Neupert W., and Lill R. Role of the intermembrane-space domain of the preprotein receptor Tom22 in protein import into mitochondria. Mol. Cell. Biol. 16 (1996) 4035-4042
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4035-4042
    • Court, D.1    Nargang, F.E.2    Steiner, H.3    Hodges, R.S.4    Neupert, W.5    Lill, R.6
  • 60
    • 33747378121 scopus 로고    scopus 로고
    • Mitochondrial preprotein translocases as dynamic molecular machines
    • van der Laan M., Rissler M., and Rehling P. Mitochondrial preprotein translocases as dynamic molecular machines. FEMS Yeast Res. 6 (2006) 849-861
    • (2006) FEMS Yeast Res. , vol.6 , pp. 849-861
    • van der Laan, M.1    Rissler, M.2    Rehling, P.3
  • 61
    • 0037418880 scopus 로고    scopus 로고
    • Regulated cycling of mitochondrial Hsp70 at the protein import channel
    • Liu Q., D'Silva P., Walter W., Marszalek J., and Craig E.A. Regulated cycling of mitochondrial Hsp70 at the protein import channel. Science 300 (2003) 139-141
    • (2003) Science , vol.300 , pp. 139-141
    • Liu, Q.1    D'Silva, P.2    Walter, W.3    Marszalek, J.4    Craig, E.A.5
  • 62
    • 0029856628 scopus 로고    scopus 로고
    • The nucleotide exchange factor MGE exerts a key function in the ATP-dependent cycle of mt-Hsp70-Tim44 interaction driving mitochondrial protein import
    • Schneider H.C., Westermann B., Neupert W., and Brunner M. The nucleotide exchange factor MGE exerts a key function in the ATP-dependent cycle of mt-Hsp70-Tim44 interaction driving mitochondrial protein import. EMBO J. 15 (1996) 5796-5803
    • (1996) EMBO J. , vol.15 , pp. 5796-5803
    • Schneider, H.C.1    Westermann, B.2    Neupert, W.3    Brunner, M.4
  • 63
    • 7544224771 scopus 로고    scopus 로고
    • Regulated interactions of mtHsp70 with Tim44 at the translocon in the mitochondrial inner membrane
    • D'Silva P., Liu Q., Walter W., and Craig E.A. Regulated interactions of mtHsp70 with Tim44 at the translocon in the mitochondrial inner membrane. Nat. Struct. Mol. Biol. 11 (2004) 1084-1091
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1084-1091
    • D'Silva, P.1    Liu, Q.2    Walter, W.3    Craig, E.A.4
  • 65
    • 0141865519 scopus 로고    scopus 로고
    • Tim14, a novel key component of the import motor of the TIM23 protein translocase of mitochondria
    • Mokranjac D., Sichting M., Neupert W., and Hell K. Tim14, a novel key component of the import motor of the TIM23 protein translocase of mitochondria. EMBO J. 22 (2003) 4945-4956
    • (2003) EMBO J. , vol.22 , pp. 4945-4956
    • Mokranjac, D.1    Sichting, M.2    Neupert, W.3    Hell, K.4
  • 67
    • 0345133332 scopus 로고    scopus 로고
    • J protein cochaperone of the mitochondrial inner membrane required for protein import into the mitochondrial matrix
    • D'Silva P.D., Schilke B., Walter W., Andrew A., and Craig E.A. J protein cochaperone of the mitochondrial inner membrane required for protein import into the mitochondrial matrix. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 13839-13844
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 13839-13844
    • D'Silva, P.D.1    Schilke, B.2    Walter, W.3    Andrew, A.4    Craig, E.A.5
  • 70
    • 24744446437 scopus 로고    scopus 로고
    • The import motor of the yeast mitochondrial TIM23 preprotein translocase contains two different J proteins, Tim14 and Mdj2
    • Mokranjac D., Sichting M., Popov-Celeketic D., Berg A., Hell K., and Neupert W. The import motor of the yeast mitochondrial TIM23 preprotein translocase contains two different J proteins, Tim14 and Mdj2. J. Biol. Chem. 280 (2005) 31608-31614
    • (2005) J. Biol. Chem. , vol.280 , pp. 31608-31614
    • Mokranjac, D.1    Sichting, M.2    Popov-Celeketic, D.3    Berg, A.4    Hell, K.5    Neupert, W.6
  • 71
    • 0037009089 scopus 로고    scopus 로고
    • Mitochondrial processing peptidases, Biochim
    • Gakh O., Cavadini P., and Isaya G. Mitochondrial processing peptidases, Biochim. Biophys. Acta 1592 (2002) 63-77
    • (2002) Biophys. Acta , vol.1592 , pp. 63-77
    • Gakh, O.1    Cavadini, P.2    Isaya, G.3
  • 72
    • 0024468352 scopus 로고
    • Purification and characterization of a processing protease from rat liver mitochondria
    • Ou W.J., Ito A., Okazaki H., and Omura T. Purification and characterization of a processing protease from rat liver mitochondria. EMBO J. 8 (1989) 2605-2612
    • (1989) EMBO J. , vol.8 , pp. 2605-2612
    • Ou, W.J.1    Ito, A.2    Okazaki, H.3    Omura, T.4
  • 73
    • 0028246650 scopus 로고
    • Rat liver mitochondrial processing peptidase. Both alpha- and beta-subunits are required for activity
    • Saavedra-Alanis V.M., Rysavy P., Rosenberg L.E., and Kalousek F. Rat liver mitochondrial processing peptidase. Both alpha- and beta-subunits are required for activity. J. Biol. Chem. 269 (1994) 9284-9288
    • (1994) J. Biol. Chem. , vol.269 , pp. 9284-9288
    • Saavedra-Alanis, V.M.1    Rysavy, P.2    Rosenberg, L.E.3    Kalousek, F.4
  • 74
    • 0036227884 scopus 로고    scopus 로고
    • Timing and structural consideration for the processing of mitochondrial matrix space proteins by the mitochondrial processing peptidase (MPP)
    • Mukhopadhyay A., Hammen P., Waltner-Law M., and Weiner H. Timing and structural consideration for the processing of mitochondrial matrix space proteins by the mitochondrial processing peptidase (MPP). Protein Sci. 11 (2002) 1026-1035
    • (2002) Protein Sci. , vol.11 , pp. 1026-1035
    • Mukhopadhyay, A.1    Hammen, P.2    Waltner-Law, M.3    Weiner, H.4
  • 75
    • 0037449819 scopus 로고    scopus 로고
    • Determination of the cleavage site of the presequence by mitochondrial processing peptidase on the substrate binding scaffold and the multiple subsites inside a molecular cavity
    • Kitada S., Yamasaki E., Kojima K., and Ito A. Determination of the cleavage site of the presequence by mitochondrial processing peptidase on the substrate binding scaffold and the multiple subsites inside a molecular cavity. J. Biol. Chem. 278 (2003) 1879-1885
    • (2003) J. Biol. Chem. , vol.278 , pp. 1879-1885
    • Kitada, S.1    Yamasaki, E.2    Kojima, K.3    Ito, A.4
  • 76
    • 0035964881 scopus 로고    scopus 로고
    • Glu(191) and Asp(195) in rat mitochondrial processing peptidase beta subunit are involved in effective cleavage of precursur protein through interaction with the proximal arginine
    • Kitada S., Kojima K., and Ito A. Glu(191) and Asp(195) in rat mitochondrial processing peptidase beta subunit are involved in effective cleavage of precursur protein through interaction with the proximal arginine. Biochem. Biophys. Res. Commun. 287 (2001) 594-599
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 594-599
    • Kitada, S.1    Kojima, K.2    Ito, A.3
  • 77
    • 0026638856 scopus 로고
    • Rat liver mitochondrial intermediate peptidase (MIP): purification and initial characterization
    • Kalousek F., Isaya G., and Rosenberg L.E. Rat liver mitochondrial intermediate peptidase (MIP): purification and initial characterization. EMBO J. 11 (1992) 2803-2809
    • (1992) EMBO J. , vol.11 , pp. 2803-2809
    • Kalousek, F.1    Isaya, G.2    Rosenberg, L.E.3
  • 78
    • 0037009130 scopus 로고    scopus 로고
    • Molecular chaperones as essential mediators of mitochondrial biogenesis
    • Voos W., and Rottgers K. Molecular chaperones as essential mediators of mitochondrial biogenesis. Biochim. Biophys. Acta 1592 (2002) 51
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 51
    • Voos, W.1    Rottgers, K.2
  • 79
    • 0030933229 scopus 로고    scopus 로고
    • Sequential action of two hsp70 complexes during protein import into mitochondria
    • Horst M., Oppliger W., Rospert S., Schonfeld H.J., Schatz G., and Azem A. Sequential action of two hsp70 complexes during protein import into mitochondria. EMBO J. 16 (1997) 1842-1849
    • (1997) EMBO J. , vol.16 , pp. 1842-1849
    • Horst, M.1    Oppliger, W.2    Rospert, S.3    Schonfeld, H.J.4    Schatz, G.5    Azem, A.6
  • 80
    • 0033582380 scopus 로고    scopus 로고
    • Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system
    • Kubo Y., Tsunehiro T., Nishikawa S., Nakai M., Ikeda E., Toh-e A., Morishima N., Shibata T., and Endo T. Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system. J. Mol. Biol. 286 (1999) 447-464
    • (1999) J. Mol. Biol. , vol.286 , pp. 447-464
    • Kubo, Y.1    Tsunehiro, T.2    Nishikawa, S.3    Nakai, M.4    Ikeda, E.5    Toh-e, A.6    Morishima, N.7    Shibata, T.8    Endo, T.9
  • 81
    • 0030686546 scopus 로고    scopus 로고
    • Purification and biochemical properties of Saccharomyces cerevisiae Mdj1p, the mitochondrial DnaJ homologue
    • Deloche O., Liberek K., Zylicz M., and Georgopoulos C. Purification and biochemical properties of Saccharomyces cerevisiae Mdj1p, the mitochondrial DnaJ homologue. J. Biol. Chem. 272 (1997) 28539-28544
    • (1997) J. Biol. Chem. , vol.272 , pp. 28539-28544
    • Deloche, O.1    Liberek, K.2    Zylicz, M.3    Georgopoulos, C.4
  • 82
    • 0028284879 scopus 로고
    • Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding
    • Rowley N., Prip-Buus C., Westermann B., Brown C., Schwarz E., Barrell B., and Neupert W. Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77 (1994) 249-259
    • (1994) Cell , vol.77 , pp. 249-259
    • Rowley, N.1    Prip-Buus, C.2    Westermann, B.3    Brown, C.4    Schwarz, E.5    Barrell, B.6    Neupert, W.7
  • 83
    • 0029860683 scopus 로고    scopus 로고
    • Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins
    • Westermann B., Gaume B., Herrmann J.M., Neupert W., and Schwarz E. Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins. Mol. Cell. Biol. 16 (1996) 7063-7071
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 7063-7071
    • Westermann, B.1    Gaume, B.2    Herrmann, J.M.3    Neupert, W.4    Schwarz, E.5
  • 84
    • 0026535927 scopus 로고
    • Identification of a mammalian 10-kDa heat shock protein, a mitochondrial chaperonin 10 homologue essential for assisted folding of trimeric ornithine transcarbamoylase in vitro
    • Hartman D.J., Hoogenraad N.J., Condron R., and Hoj P.B. Identification of a mammalian 10-kDa heat shock protein, a mitochondrial chaperonin 10 homologue essential for assisted folding of trimeric ornithine transcarbamoylase in vitro. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 3394-3398
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 3394-3398
    • Hartman, D.J.1    Hoogenraad, N.J.2    Condron, R.3    Hoj, P.B.4
  • 86
    • 23044498270 scopus 로고    scopus 로고
    • Down-regulation of Hsp60 expression by RNAi impairs folding of medium-chain acyl-CoA dehydrogenase wild-type and disease-associated proteins
    • Corydon T.J., Hansen J., Bross P., and Jensen T.G. Down-regulation of Hsp60 expression by RNAi impairs folding of medium-chain acyl-CoA dehydrogenase wild-type and disease-associated proteins. Mol. Genet. Metab. 85 (2005) 260-270
    • (2005) Mol. Genet. Metab. , vol.85 , pp. 260-270
    • Corydon, T.J.1    Hansen, J.2    Bross, P.3    Jensen, T.G.4
  • 88
    • 33746265142 scopus 로고    scopus 로고
    • GroEL-mediated protein folding: making the impossible, possible
    • Lin Z., and Rye H.S. GroEL-mediated protein folding: making the impossible, possible. Crit. Rev. Biochem. Mol. Biol. 41 (2006) 211-239
    • (2006) Crit. Rev. Biochem. Mol. Biol. , vol.41 , pp. 211-239
    • Lin, Z.1    Rye, H.S.2
  • 89
    • 0034836608 scopus 로고    scopus 로고
    • The effect of nucleotides and mitochondrial chaperonin 10 on the structure and chaperone activity of mitochondrial chaperonin 60
    • Levy-Rimler G., Viitanen P., Weiss C., Sharkia R., Greenberg A., Niv A., Lustig A., Delarea Y., and Azem A. The effect of nucleotides and mitochondrial chaperonin 10 on the structure and chaperone activity of mitochondrial chaperonin 60. Eur. J. Biochem. 268 (2001) 3465-3472
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3465-3472
    • Levy-Rimler, G.1    Viitanen, P.2    Weiss, C.3    Sharkia, R.4    Greenberg, A.5    Niv, A.6    Lustig, A.7    Delarea, Y.8    Azem, A.9
  • 90
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • Xu Z., Horwich A.L., and Sigler P.B. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388 (1997) 741-750
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 91
    • 0027427326 scopus 로고
    • The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding
    • Martin J., Mayhew M., Langer T., and Hartl F.U. The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding. Nature 366 (1993) 228-233
    • (1993) Nature , vol.366 , pp. 228-233
    • Martin, J.1    Mayhew, M.2    Langer, T.3    Hartl, F.U.4
  • 92
    • 33646945039 scopus 로고    scopus 로고
    • GroEL: More than just a folding cage
    • Radford S.E. GroEL: More than just a folding cage. Cell 125 (2006) 831-833
    • (2006) Cell , vol.125 , pp. 831-833
    • Radford, S.E.1
  • 94
    • 0022481113 scopus 로고
    • The presequences of two imported mitochondrial proteins contain information for intracellular and intramitochondrial sorting
    • van Loon A.P., Brandli A.W., and Schatz G. The presequences of two imported mitochondrial proteins contain information for intracellular and intramitochondrial sorting. Cell 44 (1986) 801-812
    • (1986) Cell , vol.44 , pp. 801-812
    • van Loon, A.P.1    Brandli, A.W.2    Schatz, G.3
  • 95
    • 0026611680 scopus 로고
    • Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism
    • Glick B.S., Brandt A., Cunningham K., Muller S., Hallberg R.L., and Schatz G. Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism. Cell 69 (1992) 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
  • 96
    • 0027362778 scopus 로고
    • Presequence and mature part of preproteins strongly influence the dependence of mitochondrial protein import on heat shock protein 70 in the matrix
    • Voos W., Gambill B.D., Guiard B., Pfanner N., and Craig E.A. Presequence and mature part of preproteins strongly influence the dependence of mitochondrial protein import on heat shock protein 70 in the matrix. J. Cell Biol. 123 (1993) 119-126
    • (1993) J. Cell Biol. , vol.123 , pp. 119-126
    • Voos, W.1    Gambill, B.D.2    Guiard, B.3    Pfanner, N.4    Craig, E.A.5
  • 97
    • 0033544854 scopus 로고    scopus 로고
    • Biogenesis of mitochondrial inner membrane proteins
    • Tokatlidis K., and Schatz G. Biogenesis of mitochondrial inner membrane proteins. J. Biol. Chem. 274 (1999) 35285-35288
    • (1999) J. Biol. Chem. , vol.274 , pp. 35285-35288
    • Tokatlidis, K.1    Schatz, G.2
  • 98
    • 0032568029 scopus 로고    scopus 로고
    • Carrier protein import into mitochondria mediated by the intermembrane proteins Tim10/Mrs11 and Tim12/Mrs5
    • Sirrenberg C., Endres M., Folsch H., Stuart R.A., Neupert W., and Brunner M. Carrier protein import into mitochondria mediated by the intermembrane proteins Tim10/Mrs11 and Tim12/Mrs5. Nature 391 (1998) 912-915
    • (1998) Nature , vol.391 , pp. 912-915
    • Sirrenberg, C.1    Endres, M.2    Folsch, H.3    Stuart, R.A.4    Neupert, W.5    Brunner, M.6
  • 99
    • 0043239359 scopus 로고    scopus 로고
    • Import of small Tim proteins into the mitochondrial intermembrane space
    • Lutz T., Neupert W., and Herrmann J.M. Import of small Tim proteins into the mitochondrial intermembrane space. EMBO J. 22 (2003) 4400-4408
    • (2003) EMBO J. , vol.22 , pp. 4400-4408
    • Lutz, T.1    Neupert, W.2    Herrmann, J.M.3
  • 100
    • 0037189583 scopus 로고    scopus 로고
    • The C66W mutation in the Deafness Dystonia Peptide 1 (DDP1) affects the formation of functional DDP1-TIM13 complexes in the mitochondrial intermembrane space
    • Hofmann S., Rothbauer U., Muhlenbein N., Neupert W., Gerbitz K.D., Brunner M., and Bauer M.F. The C66W mutation in the Deafness Dystonia Peptide 1 (DDP1) affects the formation of functional DDP1-TIM13 complexes in the mitochondrial intermembrane space. J. Biol. Chem. 277 (2002) 23287-23293
    • (2002) J. Biol. Chem. , vol.277 , pp. 23287-23293
    • Hofmann, S.1    Rothbauer, U.2    Muhlenbein, N.3    Neupert, W.4    Gerbitz, K.D.5    Brunner, M.6    Bauer, M.F.7
  • 101
    • 29544436323 scopus 로고    scopus 로고
    • Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller
    • Webb C.T., Gorman M.A., Lazarou M., Ryan M.T., and Gulbis J.M. Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller. Mol. Cell 21 (2006) 123-133
    • (2006) Mol. Cell , vol.21 , pp. 123-133
    • Webb, C.T.1    Gorman, M.A.2    Lazarou, M.3    Ryan, M.T.4    Gulbis, J.M.5
  • 103
    • 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., and Herrmann J.M. A disulfide relay system in the intermembrane space of mitochondria that mediates protein import. Cell 121 (2005) 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
  • 104
    • 26244464441 scopus 로고    scopus 로고
    • The essential mitochondrial protein Erv1 cooperates with Mia40 in biogenesis of intermembrane space proteins
    • Rissler M., Wiedemann N., Pfannschmidt S., Gabriel K., Guiard B., Pfanner N., and Chacinska A. The essential mitochondrial protein Erv1 cooperates with Mia40 in biogenesis of intermembrane space proteins. J. Mol. Biol. 353 (2005) 485-492
    • (2005) J. Mol. Biol. , vol.353 , pp. 485-492
    • Rissler, M.1    Wiedemann, N.2    Pfannschmidt, S.3    Gabriel, K.4    Guiard, B.5    Pfanner, N.6    Chacinska, A.7
  • 105
    • 27144438677 scopus 로고    scopus 로고
    • Erv1 mediates the Mia40-dependent protein import pathway and provides a functional link to the respiratory chain by shuttling electrons to cytochrome c
    • Allen S., Balabanidou V., Sideris D.P., Lisowsky T., and Tokatlidis K. Erv1 mediates the Mia40-dependent protein import pathway and provides a functional link to the respiratory chain by shuttling electrons to cytochrome c. J. Mol. Biol. 353 (2005) 937-944
    • (2005) J. Mol. Biol. , vol.353 , pp. 937-944
    • Allen, S.1    Balabanidou, V.2    Sideris, D.P.3    Lisowsky, T.4    Tokatlidis, K.5
  • 106
    • 30844449228 scopus 로고    scopus 로고
    • Chaperoning through the mitochondrial intermembrane space
    • Wiedemann N., Pfanner N., and Chacinska A. Chaperoning through the mitochondrial intermembrane space. Mol. Cell 21 (2006) 145-148
    • (2006) Mol. Cell , vol.21 , pp. 145-148
    • Wiedemann, N.1    Pfanner, N.2    Chacinska, A.3
  • 107
    • 0037009105 scopus 로고    scopus 로고
    • Protein import into and across the mitochondrial inner membrane: role of the TIM23 and TIM22 translocons
    • Jensen R., and Dunn C. Protein import into and across the mitochondrial inner membrane: role of the TIM23 and TIM22 translocons. Biochim. Biophys. Acta 1592 (2002) 25-34
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 25-34
    • Jensen, R.1    Dunn, C.2
  • 108
    • 0026015995 scopus 로고
    • An unusual mitochondrial import pathway for the precursor to yeast cytochrome c oxidase subunit Va
    • Miller B.R., and Cumsky M.G. An unusual mitochondrial import pathway for the precursor to yeast cytochrome c oxidase subunit Va. J. Cell Biol. 112 (1991) 833-841
    • (1991) J. Cell Biol. , vol.112 , pp. 833-841
    • Miller, B.R.1    Cumsky, M.G.2
  • 109
    • 0032478794 scopus 로고    scopus 로고
    • Sorting of d-lactate dehydrogenase to the inner membrane of mitochondria. Analysis of topogenic signal and energetic requirements
    • Rojo E.E., Guiard B., Neupert W., and Stuart R.A. Sorting of d-lactate dehydrogenase to the inner membrane of mitochondria. Analysis of topogenic signal and energetic requirements. J. Biol. Chem. 273 (1998) 8040-8047
    • (1998) J. Biol. Chem. , vol.273 , pp. 8040-8047
    • Rojo, E.E.1    Guiard, B.2    Neupert, W.3    Stuart, R.A.4
  • 110
    • 0028866982 scopus 로고
    • Topogenesis of cytochrome oxidase subunit II. Mechanisms of protein export from the mitochondrial matrix
    • Herrmann J.M., Koll H., Cook R.A., Neupert W., and Stuart R.A. Topogenesis of cytochrome oxidase subunit II. Mechanisms of protein export from the mitochondrial matrix. J. Biol. Chem. 270 (1995) 27079-27086
    • (1995) J. Biol. Chem. , vol.270 , pp. 27079-27086
    • Herrmann, J.M.1    Koll, H.2    Cook, R.A.3    Neupert, W.4    Stuart, R.A.5
  • 111
    • 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
  • 112
    • 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
  • 113
    • 0037009132 scopus 로고    scopus 로고
    • Insertion of proteins into the inner membrane of mitochondria: the role of the Oxa1 complex
    • Stuart R. Insertion of proteins into the inner membrane of mitochondria: the role of the Oxa1 complex. Biochim. Biophys. Acta 1592 (2002) 79
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 79
    • Stuart, R.1
  • 114
    • 0028109935 scopus 로고
    • Cloning of a human gene involved in cytochrome oxidase assembly by functional complementation of an oxa1- mutation in Saccharomyces cerevisiae
    • Bonnefoy N., Kermorgant M., Groudinsky O., Minet M., Slonimski P.P., and Dujardin G. Cloning of a human gene involved in cytochrome oxidase assembly by functional complementation of an oxa1- mutation in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 11978-11982
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 11978-11982
    • Bonnefoy, N.1    Kermorgant, M.2    Groudinsky, O.3    Minet, M.4    Slonimski, P.P.5    Dujardin, G.6
  • 115
    • 0035868763 scopus 로고    scopus 로고
    • Oxa1p acts as a general membrane insertion machinery for proteins encoded by mitochondrial DNA
    • Hell K., Neupert W., and Stuart R.A. Oxa1p acts as a general membrane insertion machinery for proteins encoded by mitochondrial DNA. EMBO J. 20 (2001) 1281-1288
    • (2001) EMBO J. , vol.20 , pp. 1281-1288
    • Hell, K.1    Neupert, W.2    Stuart, R.A.3
  • 116
    • 0030952628 scopus 로고    scopus 로고
    • Membrane translocation of mitochondrially coded Cox2p: distinct requirements for export of N and C termini and dependence on the conserved protein Oxa1p
    • He S., and Fox T.D. Membrane translocation of mitochondrially coded Cox2p: distinct requirements for export of N and C termini and dependence on the conserved protein Oxa1p. Mol. Biol. Cell 8 (1997) 1449-1460
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1449-1460
    • He, S.1    Fox, T.D.2
  • 118
    • 0037459118 scopus 로고    scopus 로고
    • Insertion of hydrophobic membrane proteins into the inner mitochondrial membrane-a guided tour
    • Rehling P., Pfanner N., and Meisinger C. Insertion of hydrophobic membrane proteins into the inner mitochondrial membrane-a guided tour. J. Mol. Biol. 326 (2003) 639-657
    • (2003) J. Mol. Biol. , vol.326 , pp. 639-657
    • Rehling, P.1    Pfanner, N.2    Meisinger, C.3
  • 119
    • 0042386354 scopus 로고    scopus 로고
    • Functional cooperation and separation of translocators in protein import into mitochondria, the double-membrane bounded organelles
    • Endo T., Yamamoto H., and Esaki M. Functional cooperation and separation of translocators in protein import into mitochondria, the double-membrane bounded organelles. J. Cell Sci. 116 (2003) 3259-3267
    • (2003) J. Cell Sci. , vol.116 , pp. 3259-3267
    • Endo, T.1    Yamamoto, H.2    Esaki, M.3
  • 120
    • 0032536045 scopus 로고    scopus 로고
    • Import of mitochondrial carriers mediated by essential proteins of the intermembrane space
    • Koehler C.M., Jarosch E., Tokatlidis K., Schmid K., Schweyen R.J., and Schatz G. Import of mitochondrial carriers mediated by essential proteins of the intermembrane space. Science 279 (1998) 369-373
    • (1998) Science , vol.279 , pp. 369-373
    • Koehler, C.M.1    Jarosch, E.2    Tokatlidis, K.3    Schmid, K.4    Schweyen, R.J.5    Schatz, G.6
  • 121
    • 0040610684 scopus 로고    scopus 로고
    • Functional staging of ADP/ATP carrier translocation across the outer mitochondrial membrane
    • Ryan M.T., Muller H., and Pfanner N. Functional staging of ADP/ATP carrier translocation across the outer mitochondrial membrane. J. Biol. Chem. 274 (1999) 20619-20627
    • (1999) J. Biol. Chem. , vol.274 , pp. 20619-20627
    • Ryan, M.T.1    Muller, H.2    Pfanner, N.3
  • 122
    • 0035726162 scopus 로고    scopus 로고
    • The essential function of the small Tim proteins in the TIM22 import pathway does not depend on formation of the soluble 70-kilodalton complex
    • Murphy M.P., Leuenberger D., Curran S.P., Oppliger W., and Koehler C.M. The essential function of the small Tim proteins in the TIM22 import pathway does not depend on formation of the soluble 70-kilodalton complex. Mol. Cell. Biol. 21 (2001) 6132-6138
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6132-6138
    • Murphy, M.P.1    Leuenberger, D.2    Curran, S.P.3    Oppliger, W.4    Koehler, C.M.5
  • 123
    • 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
    • Truscott 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
    • Truscott, K.N.1    Wiedemann, N.2    Rehling, P.3    Muller, H.4    Meisinger, C.5    Pfanner, N.6    Guiard, B.7
  • 124
    • 0033198845 scopus 로고    scopus 로고
    • Different import pathways through the mitochondrial intermembrane space for inner membrane proteins
    • Leuenberger D., Bally N.A., Schatz G., and Koehler C.M. Different import pathways through the mitochondrial intermembrane space for inner membrane proteins. EMBO J. 18 (1999) 4816-4822
    • (1999) EMBO J. , vol.18 , pp. 4816-4822
    • Leuenberger, D.1    Bally, N.A.2    Schatz, G.3    Koehler, C.M.4
  • 126
    • 0029162897 scopus 로고
    • An amino acid substitution in the pyruvate dehydrogenase E1 alpha gene, affecting mitochondrial import of the precursor protein
    • Takakubo F., Cartwright P., Hoogenraad N., Thorburn D.R., Collins F., Lithgow T., and Dahl H.H. An amino acid substitution in the pyruvate dehydrogenase E1 alpha gene, affecting mitochondrial import of the precursor protein. Am. J. Hum. Genet. 57 (1995) 772-780
    • (1995) Am. J. Hum. Genet. , vol.57 , pp. 772-780
    • Takakubo, F.1    Cartwright, P.2    Hoogenraad, N.3    Thorburn, D.R.4    Collins, F.5    Lithgow, T.6    Dahl, H.H.7
  • 127
    • 0024488710 scopus 로고
    • Lacticacidemia. Biochemical, clinical, and genetic considerations
    • Robinson B.H. Lacticacidemia. Biochemical, clinical, and genetic considerations. Adv. Hum. Genet. 18 (1989) 151-152
    • (1989) Adv. Hum. Genet. , vol.18 , pp. 151-152
    • Robinson, B.H.1
  • 129
    • 0023245015 scopus 로고
    • The human pyruvate dehydrogenase complex. Isolation of cDNA clones for the E1 alpha subunit, sequence analysis, and characterization of the mRNA
    • Dahl H.H., Hunt S.M., Hutchison W.M., and Brown G.K. The human pyruvate dehydrogenase complex. Isolation of cDNA clones for the E1 alpha subunit, sequence analysis, and characterization of the mRNA. J. Biol. Chem. 262 (1987) 7398-7403
    • (1987) J. Biol. Chem. , vol.262 , pp. 7398-7403
    • Dahl, H.H.1    Hunt, S.M.2    Hutchison, W.M.3    Brown, G.K.4
  • 130
    • 0022516472 scopus 로고
    • Peroxisomal alanine:glyoxylate aminotransferase deficiency in primary hyperoxaluria type I
    • Danpure C.J., and Jennings P.R. Peroxisomal alanine:glyoxylate aminotransferase deficiency in primary hyperoxaluria type I. FEBS Lett. 201 (1986) 20-24
    • (1986) FEBS Lett. , vol.201 , pp. 20-24
    • Danpure, C.J.1    Jennings, P.R.2
  • 131
    • 0024535978 scopus 로고
    • An enzyme trafficking defect in two patients with primary hyperoxaluria type 1: peroxisomal alanine/glyoxylate aminotransferase rerouted to mitochondria
    • Danpure C.J., Cooper P.J., Wise P.J., and Jennings P.R. An enzyme trafficking defect in two patients with primary hyperoxaluria type 1: peroxisomal alanine/glyoxylate aminotransferase rerouted to mitochondria. J. Cell Biol. 108 (1989) 1345-1352
    • (1989) J. Cell Biol. , vol.108 , pp. 1345-1352
    • Danpure, C.J.1    Cooper, P.J.2    Wise, P.J.3    Jennings, P.R.4
  • 132
    • 0025640818 scopus 로고
    • Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1
    • Purdue P.E., Takada Y., and Danpure C.J. Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1. J. Cell Biol. 111 (1990) 2341-2351
    • (1990) J. Cell Biol. , vol.111 , pp. 2341-2351
    • Purdue, P.E.1    Takada, Y.2    Danpure, C.J.3
  • 133
    • 0025746324 scopus 로고
    • Mistargeting of peroxisomal l-alanine:glyoxylate aminotransferase to mitochondria in primary hyperoxaluria patients depends upon activation of a cryptic mitochondrial targeting sequence by a point mutation
    • Purdue P.E., Allsop J., Isaya G., Rosenberg L.E., and Danpure C.J. Mistargeting of peroxisomal l-alanine:glyoxylate aminotransferase to mitochondria in primary hyperoxaluria patients depends upon activation of a cryptic mitochondrial targeting sequence by a point mutation. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 10900-10904
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 10900-10904
    • Purdue, P.E.1    Allsop, J.2    Isaya, G.3    Rosenberg, L.E.4    Danpure, C.J.5
  • 134
    • 0029144403 scopus 로고
    • Mammalian alanine/glyoxylate aminotransferase 1 is imported into peroxisomes via the PTS1 translocation pathway. Increased degeneracy and context specificity of the mammalian PTS1 motif and implications for the peroxisome-to-mitochondrion mistargeting of AGT in primary hyperoxaluria type 1
    • Motley A., Lumb M.J., Oatey P.B., Jennings P.R., De Zoysa P.A., Wanders R.J., Tabak H.F., and Danpure C.J. Mammalian alanine/glyoxylate aminotransferase 1 is imported into peroxisomes via the PTS1 translocation pathway. Increased degeneracy and context specificity of the mammalian PTS1 motif and implications for the peroxisome-to-mitochondrion mistargeting of AGT in primary hyperoxaluria type 1. J. Cell Biol. 131 (1995) 95-109
    • (1995) J. Cell Biol. , vol.131 , pp. 95-109
    • Motley, A.1    Lumb, M.J.2    Oatey, P.B.3    Jennings, P.R.4    De Zoysa, P.A.5    Wanders, R.J.6    Tabak, H.F.7    Danpure, C.J.8
  • 135
    • 0034680869 scopus 로고    scopus 로고
    • Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations
    • Lumb M.J., and Danpure C.J. Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations. J. Biol. Chem. 275 (2000) 36415-36422
    • (2000) J. Biol. Chem. , vol.275 , pp. 36415-36422
    • Lumb, M.J.1    Danpure, C.J.2
  • 136
    • 0029828820 scopus 로고    scopus 로고
    • Inhibition of alanine:glyoxylate aminotransferase 1 dimerization is a prerequisite for its peroxisome-to-mitochondrion mistargeting in primary hyperoxaluria type 1
    • Leiper J.M., Oatey P.B., and Danpure C.J. Inhibition of alanine:glyoxylate aminotransferase 1 dimerization is a prerequisite for its peroxisome-to-mitochondrion mistargeting in primary hyperoxaluria type 1. J. Cell Biol. 135 (1996) 939-951
    • (1996) J. Cell Biol. , vol.135 , pp. 939-951
    • Leiper, J.M.1    Oatey, P.B.2    Danpure, C.J.3
  • 137
    • 0033787313 scopus 로고    scopus 로고
    • Import of peroxisomal matrix and membrane proteins
    • Subramani S., Koller A., and Snyder W.B. Import of peroxisomal matrix and membrane proteins. Annu. Rev. Biochem. 69 (2000) 399-418
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 399-418
    • Subramani, S.1    Koller, A.2    Snyder, W.B.3
  • 138
    • 0023656946 scopus 로고
    • The role of protein structure in the mitochondrial import pathway. Unfolding of mitochondrially bound precursors is required for membrane translocation
    • Chen W.J., and Douglas M.G. The role of protein structure in the mitochondrial import pathway. Unfolding of mitochondrially bound precursors is required for membrane translocation. J. Biol. Chem. 262 (1987) 15605-15609
    • (1987) J. Biol. Chem. , vol.262 , pp. 15605-15609
    • Chen, W.J.1    Douglas, M.G.2
  • 140
    • 1242273641 scopus 로고    scopus 로고
    • Alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting in human hereditary kidney stone disease
    • Danpure C.J., Lumb M.J., Birdsey G.M., and Zhang X. Alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting in human hereditary kidney stone disease. Biochim. Biophys. Acta 1647 (2003) 70-75
    • (2003) Biochim. Biophys. Acta , vol.1647 , pp. 70-75
    • Danpure, C.J.1    Lumb, M.J.2    Birdsey, G.M.3    Zhang, X.4
  • 142
    • 0036361291 scopus 로고    scopus 로고
    • Animal models for mitochondrial disease
    • Wallace D.C. Animal models for mitochondrial disease. Methods Mol. Biol. 197 (2002) 3-54
    • (2002) Methods Mol. Biol. , vol.197 , pp. 3-54
    • Wallace, D.C.1
  • 145
    • 0037339203 scopus 로고    scopus 로고
    • The Ala16Val genetic dimorphism modulates the import of human manganese superoxide dismutase into rat liver mitochondria
    • Sutton A., Khoury H., Prip-Buus C., Cepanec C., Pessayre D., and Degoul F. The Ala16Val genetic dimorphism modulates the import of human manganese superoxide dismutase into rat liver mitochondria. Pharmacogenetics 13 (2003) 145-157
    • (2003) Pharmacogenetics , vol.13 , pp. 145-157
    • Sutton, A.1    Khoury, H.2    Prip-Buus, C.3    Cepanec, C.4    Pessayre, D.5    Degoul, F.6
  • 147
    • 0035045720 scopus 로고    scopus 로고
    • Homozygosity for alanine in the mitochondrial targeting sequence of superoxide dismutase and risk for severe alcoholic liver disease
    • Degoul F., Sutton A., Mansouri A., Cepanec C., Degott C., Fromenty B., Beaugrand M., Valla D., and Pessayre D. Homozygosity for alanine in the mitochondrial targeting sequence of superoxide dismutase and risk for severe alcoholic liver disease. Gastroenterology 120 (2001) 1468-1474
    • (2001) Gastroenterology , vol.120 , pp. 1468-1474
    • Degoul, F.1    Sutton, A.2    Mansouri, A.3    Cepanec, C.4    Degott, C.5    Fromenty, B.6    Beaugrand, M.7    Valla, D.8    Pessayre, D.9
  • 149
    • 0028332490 scopus 로고
    • Increased production of reactive oxygen species by rat liver mitochondria after chronic ethanol treatment
    • Kukielka E., Dicker E., and Cederbaum A.I. Increased production of reactive oxygen species by rat liver mitochondria after chronic ethanol treatment. Arch. Biochem. Biophys. 309 (1994) 377-386
    • (1994) Arch. Biochem. Biophys. , vol.309 , pp. 377-386
    • Kukielka, E.1    Dicker, E.2    Cederbaum, A.I.3
  • 150
    • 0033525773 scopus 로고    scopus 로고
    • Mitochondrial diseases in man and mouse
    • Wallace D.C. Mitochondrial diseases in man and mouse. Science 283 (1999) 1482-1488
    • (1999) Science , vol.283 , pp. 1482-1488
    • Wallace, D.C.1
  • 151
    • 0036083422 scopus 로고    scopus 로고
    • Alcohol and mitochondria: a dysfunctional relationship
    • Hoek J.B., Cahill A., and Pastorino J.G. Alcohol and mitochondria: a dysfunctional relationship. Gastroenterology 122 (2002) 2049-2063
    • (2002) Gastroenterology , vol.122 , pp. 2049-2063
    • Hoek, J.B.1    Cahill, A.2    Pastorino, J.G.3
  • 152
    • 0033517057 scopus 로고    scopus 로고
    • Polymorphisms in the SOD2 and HLA-DRB1 genes are associated with nonfamilial idiopathic dilated cardiomyopathy in Japanese
    • Hiroi S., Harada H., Nishi H., Satoh M., Nagai R., and Kimura A. Polymorphisms in the SOD2 and HLA-DRB1 genes are associated with nonfamilial idiopathic dilated cardiomyopathy in Japanese. Biochem. Biophys. Res. Commun. 261 (1999) 332-339
    • (1999) Biochem. Biophys. Res. Commun. , vol.261 , pp. 332-339
    • Hiroi, S.1    Harada, H.2    Nishi, H.3    Satoh, M.4    Nagai, R.5    Kimura, A.6
  • 153
    • 0037242288 scopus 로고    scopus 로고
    • The polymorphism of manganese superoxide dismutase is associated with diabetic nephropathy in Japanese type 2 diabetic patients
    • Nomiyama T., Tanaka Y., Piao L., Nagasaka K., Sakai K., Ogihara T., Nakajima K., Watada H., and Kawamori R. The polymorphism of manganese superoxide dismutase is associated with diabetic nephropathy in Japanese type 2 diabetic patients. J. Hum. Genet. 48 (2003) 138-141
    • (2003) J. Hum. Genet. , vol.48 , pp. 138-141
    • Nomiyama, T.1    Tanaka, Y.2    Piao, L.3    Nagasaka, K.4    Sakai, K.5    Ogihara, T.6    Nakajima, K.7    Watada, H.8    Kawamori, R.9
  • 158
    • 0042767609 scopus 로고    scopus 로고
    • Clinical and molecular findings in a patient with a novel mutation in the deafness-dystonia peptide (DDP1) gene
    • Binder J., Hofmann S., Kreisel S., Wohrle J.C., Bazner H., Krauss J.K., Hennerici M.G., and Bauer M.F. Clinical and molecular findings in a patient with a novel mutation in the deafness-dystonia peptide (DDP1) gene. Brain 126 (2003) 1814-1820
    • (2003) Brain , vol.126 , pp. 1814-1820
    • Binder, J.1    Hofmann, S.2    Kreisel, S.3    Wohrle, J.C.4    Bazner, H.5    Krauss, J.K.6    Hennerici, M.G.7    Bauer, M.F.8
  • 159
    • 13444267649 scopus 로고    scopus 로고
    • A novel intronic mutation in the DDP1 gene in a family with X-linked dystonia-deafness syndrome
    • Ezquerra M., Campdelacreu J., Munoz E., Tolosa E., and Marti M.J. A novel intronic mutation in the DDP1 gene in a family with X-linked dystonia-deafness syndrome. Arch. Neurol. 62 (2005) 306-308
    • (2005) Arch. Neurol. , vol.62 , pp. 306-308
    • Ezquerra, M.1    Campdelacreu, J.2    Munoz, E.3    Tolosa, E.4    Marti, M.J.5
  • 160
    • 0034039615 scopus 로고    scopus 로고
    • A de novo missense mutation in a critical domain of the X-linked DDP gene causes the typical deafness-dystonia-optic atrophy syndrome
    • Tranebjaerg L., Hamel B.C., Gabreels F.J., Renier W.O., and Van Ghelue M. A de novo missense mutation in a critical domain of the X-linked DDP gene causes the typical deafness-dystonia-optic atrophy syndrome. Eur. J. Hum. Genet. 8 (2000) 464-467
    • (2000) Eur. J. Hum. Genet. , vol.8 , pp. 464-467
    • Tranebjaerg, L.1    Hamel, B.C.2    Gabreels, F.J.3    Renier, W.O.4    Van Ghelue, M.5
  • 161
    • 0034795004 scopus 로고    scopus 로고
    • A novel deafness/dystonia peptide gene mutation that causes dystonia in female carriers of Mohr-Tranebjaerg syndrome
    • Swerdlow R.H., and Wooten G.F. A novel deafness/dystonia peptide gene mutation that causes dystonia in female carriers of Mohr-Tranebjaerg syndrome. Ann. Neurol. 50 (2001) 537-540
    • (2001) Ann. Neurol. , vol.50 , pp. 537-540
    • Swerdlow, R.H.1    Wooten, G.F.2
  • 162
    • 0034971212 scopus 로고    scopus 로고
    • A family with X-linked dystonia-deafness syndrome with a novel mutation of the DDP gene
    • Ujike H., Tanabe Y., Takehisa Y., Hayabara T., and Kuroda S. A family with X-linked dystonia-deafness syndrome with a novel mutation of the DDP gene. Arch. Neurol. 58 (2001) 1004-1007
    • (2001) Arch. Neurol. , vol.58 , pp. 1004-1007
    • Ujike, H.1    Tanabe, Y.2    Takehisa, Y.3    Hayabara, T.4    Kuroda, S.5
  • 163
    • 0001112103 scopus 로고    scopus 로고
    • Jensen syndrome is allelic to Mohr-Tranebjaerg syndrome and both are caused by stop mutations in the DDP gene.
    • (suppl)
    • Tranebjaerg L., Van Ghelue M., and Nilssen O. Jensen syndrome is allelic to Mohr-Tranebjaerg syndrome and both are caused by stop mutations in the DDP gene. Am. J. Hum. Genet. 61 (1997) A349 (suppl)
    • (1997) Am. J. Hum. Genet. , vol.61
    • Tranebjaerg, L.1    Van Ghelue, M.2    Nilssen, O.3
  • 164
    • 32444451348 scopus 로고    scopus 로고
    • A novel mutation in the gene encoding TIMM8a, a component of the mitochondrial protein translocase complexes, in a Spanish familial case of deafness-dystonia (Mohr-Tranebjaerg) syndrome
    • Aguirre L.A., del Castillo I., Macaya A., Meda C., Villamar M., Moreno-Pelayo M.A., and Moreno F. A novel mutation in the gene encoding TIMM8a, a component of the mitochondrial protein translocase complexes, in a Spanish familial case of deafness-dystonia (Mohr-Tranebjaerg) syndrome. Am. J. Med. Genet., A 140 (2006) 392-397
    • (2006) Am. J. Med. Genet., A , vol.140 , pp. 392-397
    • Aguirre, L.A.1    del Castillo, I.2    Macaya, A.3    Meda, C.4    Villamar, M.5    Moreno-Pelayo, M.A.6    Moreno, F.7
  • 166
    • 0036501592 scopus 로고    scopus 로고
    • Human deafness dystonia syndrome is caused by a defect in assembly of the DDP1/TIMM8a-TIMM13 complex
    • Roesch K., Curran S.P., Tranebjaerg L., and Koehler C.M. Human deafness dystonia syndrome is caused by a defect in assembly of the DDP1/TIMM8a-TIMM13 complex. Hum. Mol. Genet. 11 (2002) 477-486
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 477-486
    • Roesch, K.1    Curran, S.P.2    Tranebjaerg, L.3    Koehler, C.M.4
  • 167
    • 0346687594 scopus 로고    scopus 로고
    • The small Tim proteins and the twin Cx3C motif
    • Koehler C.M. The small Tim proteins and the twin Cx3C motif. Trends Biochem. Sci. 29 (2004) 1-4
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 1-4
    • Koehler, C.M.1
  • 168
    • 26244466764 scopus 로고    scopus 로고
    • Functional and mutational characterization of human MIA40 acting during import into the mitochondrial intermembrane space
    • Hofmann S., Rothbauer U., Muhlenbein N., Baiker K., Hell K., and Bauer M.F. Functional and mutational characterization of human MIA40 acting during import into the mitochondrial intermembrane space. J. Mol. Biol. 353 (2005) 517-528
    • (2005) J. Mol. Biol. , vol.353 , pp. 517-528
    • Hofmann, S.1    Rothbauer, U.2    Muhlenbein, N.3    Baiker, K.4    Hell, K.5    Bauer, M.F.6
  • 169
    • 5744230324 scopus 로고    scopus 로고
    • The calcium-binding aspartate/glutamate carriers, citrin and aralar1, are new substrates for the DDP1/TIMM8a-TIMM13 complex
    • Roesch K., Hynds P.J., Varga R., Tranebjaerg L., and Koehler C.M. The calcium-binding aspartate/glutamate carriers, citrin and aralar1, are new substrates for the DDP1/TIMM8a-TIMM13 complex. Hum. Mol. Genet. 13 (2004) 2101-2111
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 2101-2111
    • Roesch, K.1    Hynds, P.J.2    Varga, R.3    Tranebjaerg, L.4    Koehler, C.M.5
  • 170
    • 1842478040 scopus 로고    scopus 로고
    • The Tim8-Tim13 Complex of Neurospora crassa Functions in the Assembly of Proteins into Both Mitochondrial Membranes
    • Hoppins S.C., and Nargang F.E. The Tim8-Tim13 Complex of Neurospora crassa Functions in the Assembly of Proteins into Both Mitochondrial Membranes. J. Biol. Chem. 279 (2004) 12396-12405
    • (2004) J. Biol. Chem. , vol.279 , pp. 12396-12405
    • Hoppins, S.C.1    Nargang, F.E.2
  • 171
    • 2442421175 scopus 로고    scopus 로고
    • Biogenesis of the protein import channel Tom40 of the mitochondrial outer membrane: intermembrane space components are involved in an early stage of the assembly pathway
    • Wiedemann N., Truscott K.N., Pfannschmidt S., Guiard B., Meisinger C., and Pfanner N. Biogenesis of the protein import channel Tom40 of the mitochondrial outer membrane: intermembrane space components are involved in an early stage of the assembly pathway. J. Biol. Chem. 279 (2004) 18188-18194
    • (2004) J. Biol. Chem. , vol.279 , pp. 18188-18194
    • Wiedemann, N.1    Truscott, K.N.2    Pfannschmidt, S.3    Guiard, B.4    Meisinger, C.5    Pfanner, N.6
  • 172
    • 33646427709 scopus 로고    scopus 로고
    • Mutation of DNAJC19, a human homologue of yeast inner mitochondrial membrane co-chaperones, causes DCMA syndrome, a novel autosomal recessive Barth syndrome-like condition
    • Davey K.M., Parboosingh J.S., McLeod D.R., Chan A., Casey R., Ferreira P., Snyder F.F., Bridge P.J., and Bernier F.P. Mutation of DNAJC19, a human homologue of yeast inner mitochondrial membrane co-chaperones, causes DCMA syndrome, a novel autosomal recessive Barth syndrome-like condition. J. Med. Genet. 43 (2006) 385-393
    • (2006) J. Med. Genet. , vol.43 , pp. 385-393
    • Davey, K.M.1    Parboosingh, J.S.2    McLeod, D.R.3    Chan, A.4    Casey, R.5    Ferreira, P.6    Snyder, F.F.7    Bridge, P.J.8    Bernier, F.P.9
  • 175
    • 0028808082 scopus 로고
    • Morphology of the mitochondria in heat shock protein 60 deficient fibroblasts from mitochondrial myopathy patients. Effects of stress conditions
    • Huckriede A., Heikema A., Sjollema K., Briones P., and Agsteribbe E. Morphology of the mitochondria in heat shock protein 60 deficient fibroblasts from mitochondrial myopathy patients. Effects of stress conditions. Virchows Arch. 427 (1995) 159-165
    • (1995) Virchows Arch. , vol.427 , pp. 159-165
    • Huckriede, A.1    Heikema, A.2    Sjollema, K.3    Briones, P.4    Agsteribbe, E.5
  • 176
    • 0028131509 scopus 로고
    • Decreased synthesis and inefficient mitochondrial import of hsp60 in a patient with a mitochondrial encephalomyopathy
    • Huckriede A., and Agsteribbe E. Decreased synthesis and inefficient mitochondrial import of hsp60 in a patient with a mitochondrial encephalomyopathy. Biochim. Biophys. Acta 1227 (1994) 200-206
    • (1994) Biochim. Biophys. Acta , vol.1227 , pp. 200-206
    • Huckriede, A.1    Agsteribbe, E.2
  • 179
    • 0031205455 scopus 로고    scopus 로고
    • Mitochondrial DNA in aging and disease
    • Wallace D.C. Mitochondrial DNA in aging and disease. Sci. Am. 277 (1997) 40-47
    • (1997) Sci. Am. , vol.277 , pp. 40-47
    • Wallace, D.C.1
  • 181
    • 0034535899 scopus 로고    scopus 로고
    • Enhanced Mitochondrial DNA Repair and Cellular Survival after Oxidative Stress by Targeting the Human 8-Oxoguanine Glycosylase Repair Enzyme to Mitochondria
    • Dobson A.W., Xu Y., Kelley M.R., LeDoux S.P., and Wilson G.L. Enhanced Mitochondrial DNA Repair and Cellular Survival after Oxidative Stress by Targeting the Human 8-Oxoguanine Glycosylase Repair Enzyme to Mitochondria. J. Biol. Chem. 275 (2000) 37518-37523
    • (2000) J. Biol. Chem. , vol.275 , pp. 37518-37523
    • Dobson, A.W.1    Xu, Y.2    Kelley, M.R.3    LeDoux, S.P.4    Wilson, G.L.5
  • 182
    • 0141480060 scopus 로고    scopus 로고
    • Age-dependent deficiency in import of mitochondrial DNA glycosylases required for repair of oxidatively damaged bases
    • Szczesny B., Hazra T.K., Papaconstantinou J., Mitra S., and Boldogh I. Age-dependent deficiency in import of mitochondrial DNA glycosylases required for repair of oxidatively damaged bases. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 10670-10675
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 10670-10675
    • Szczesny, B.1    Hazra, T.K.2    Papaconstantinou, J.3    Mitra, S.4    Boldogh, I.5
  • 183
    • 0035242370 scopus 로고    scopus 로고
    • Oxidative stress inhibits the mitochondrial import of preproteins and leads to their degradation
    • Wright G., Terada K., Yano M., Sergeev I., and Mori M. Oxidative stress inhibits the mitochondrial import of preproteins and leads to their degradation. Exp. Cell Res. 263 (2001) 107-117
    • (2001) Exp. Cell Res. , vol.263 , pp. 107-117
    • Wright, G.1    Terada, K.2    Yano, M.3    Sergeev, I.4    Mori, M.5
  • 185
    • 33344476096 scopus 로고    scopus 로고
    • Mitochondrial membrane damage during aging process in rat heart: potential efficacy of l-carnitine and DL alpha lipoic acid
    • Savitha S., and Panneerselvam C. Mitochondrial membrane damage during aging process in rat heart: potential efficacy of l-carnitine and DL alpha lipoic acid. Mech. Ageing Dev. 127 (2006) 349-355
    • (2006) Mech. Ageing Dev. , vol.127 , pp. 349-355
    • Savitha, S.1    Panneerselvam, C.2
  • 186
    • 33644766960 scopus 로고    scopus 로고
    • Relationship between levels of oxidative DNA damage, lipid peroxidation and mitochondrial membrane potential in young and old F344 rats
    • Wong Y.T., Ruan R., and Tay F.E. Relationship between levels of oxidative DNA damage, lipid peroxidation and mitochondrial membrane potential in young and old F344 rats. Free Radical Res. 40 (2006) 393-402
    • (2006) Free Radical Res. , vol.40 , pp. 393-402
    • Wong, Y.T.1    Ruan, R.2    Tay, F.E.3
  • 187
    • 0035956929 scopus 로고    scopus 로고
    • Increased mitochondrial oxidative stress in the Sod2 (+/-) mouse results in the age-related decline of mitochondrial function culminating in increased apoptosis
    • Kokoszka J.E., Coskun P., Esposito L.A., and Wallace D.C. Increased mitochondrial oxidative stress in the Sod2 (+/-) mouse results in the age-related decline of mitochondrial function culminating in increased apoptosis. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 2278-2283
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 2278-2283
    • Kokoszka, J.E.1    Coskun, P.2    Esposito, L.A.3    Wallace, D.C.4
  • 189
    • 0033616726 scopus 로고    scopus 로고
    • Uncoupling of transfer of the presequence and unfolding of the mature domain in precursor translocation across the mitochondrial outer membrane
    • Kanamori T., Nishikawa S., Nakai M., Shin I., Schultz P.G., and Endo T. Uncoupling of transfer of the presequence and unfolding of the mature domain in precursor translocation across the mitochondrial outer membrane. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 3634-3639
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 3634-3639
    • Kanamori, T.1    Nishikawa, S.2    Nakai, M.3    Shin, I.4    Schultz, P.G.5    Endo, T.6
  • 190
    • 0030872409 scopus 로고    scopus 로고
    • Mitochondrial protein import. Tom40 plays a major role in targeting and translocation of preproteins by forming a specific binding site for the presequence
    • Rapaport D., Neupert W., and Lill R. Mitochondrial protein import. Tom40 plays a major role in targeting and translocation of preproteins by forming a specific binding site for the presequence. J. Biol. Chem. 272 (1997) 18725-18731
    • (1997) J. Biol. Chem. , vol.272 , pp. 18725-18731
    • Rapaport, D.1    Neupert, W.2    Lill, R.3
  • 191
    • 0032444931 scopus 로고    scopus 로고
    • Thyroid hormone modifies mitochondrial phenotype by increasing protein import without altering degradation
    • Craig E.E., Chesley A., and Hood D.A. Thyroid hormone modifies mitochondrial phenotype by increasing protein import without altering degradation. Am. J. Physiol. 275 (1998) C1508-C1515
    • (1998) Am. J. Physiol. , vol.275
    • Craig, E.E.1    Chesley, A.2    Hood, D.A.3
  • 192
    • 0037227619 scopus 로고    scopus 로고
    • Functional consequences of thyroid hormone-induced changes in the mitochondrial protein import pathway
    • Colavecchia M., Christie L.N., Kanwar Y.S., and Hood D.A. Functional consequences of thyroid hormone-induced changes in the mitochondrial protein import pathway. Am. J. Physiol. Endocrinol. Metab. 284 (2003) E29-E35
    • (2003) Am. J. Physiol. Endocrinol. Metab. , vol.284
    • Colavecchia, M.1    Christie, L.N.2    Kanwar, Y.S.3    Hood, D.A.4
  • 193
    • 0034128065 scopus 로고    scopus 로고
    • Effect of thyroid hormone on mtHsp70 expression, mitochondrial import and processing in cardiac muscle
    • Schneider J.J., and Hood D.A. Effect of thyroid hormone on mtHsp70 expression, mitochondrial import and processing in cardiac muscle. J. Endocrinol. 165 (2000) 9-17
    • (2000) J. Endocrinol. , vol.165 , pp. 9-17
    • Schneider, J.J.1    Hood, D.A.2
  • 194
    • 0029157324 scopus 로고
    • Expression of stress proteins and mitochondrial chaperonins in chronically stimulated skeletal muscle
    • Ornatsky O.I., Connor M.K., and Hood D.A. Expression of stress proteins and mitochondrial chaperonins in chronically stimulated skeletal muscle. Biochem. J. 311 Pt 1 (1995) 119-123
    • (1995) Biochem. J. , vol.311 , Issue.PART 1 , pp. 119-123
    • Ornatsky, O.I.1    Connor, M.K.2    Hood, D.A.3
  • 195
    • 0031831491 scopus 로고    scopus 로고
    • Contractile activity-induced adaptations in the mitochondrial protein import system
    • Takahashi M., Chesley A., Freyssenet D., and Hood D.A. Contractile activity-induced adaptations in the mitochondrial protein import system. Am. J. Physiol. 274 (1998) C1380-C1387
    • (1998) Am. J. Physiol. , vol.274
    • Takahashi, M.1    Chesley, A.2    Freyssenet, D.3    Hood, D.A.4
  • 196
    • 0033968990 scopus 로고    scopus 로고
    • Induction of mitochondrial stress proteins following treadmill running
    • Mattson J.P., Ross C.R., Kilgore J.L., and Musch T.I. Induction of mitochondrial stress proteins following treadmill running. Med. Sci. Sports Exerc. 32 (2000) 365-369
    • (2000) Med. Sci. Sports Exerc. , vol.32 , pp. 365-369
    • Mattson, J.P.1    Ross, C.R.2    Kilgore, J.L.3    Musch, T.I.4
  • 197
    • 0025782887 scopus 로고
    • Molecular and cellular adaptation of muscle in response to exercise: perspectives of various models
    • Booth F.W., and Thomason D.B. Molecular and cellular adaptation of muscle in response to exercise: perspectives of various models. Physiol. Rev. 71 (1991) 541-585
    • (1991) Physiol. Rev. , vol.71 , pp. 541-585
    • Booth, F.W.1    Thomason, D.B.2
  • 198
    • 0026450106 scopus 로고
    • Adaptation of mammalian skeletal muscle fibers to chronic electrical stimulation
    • Pette D., and Vrbova G. Adaptation of mammalian skeletal muscle fibers to chronic electrical stimulation. Rev. Physiol. Biochem. Pharmacol. 120 (1992) 115-202
    • (1992) Rev. Physiol. Biochem. Pharmacol. , vol.120 , pp. 115-202
    • Pette, D.1    Vrbova, G.2
  • 199
    • 0029914131 scopus 로고    scopus 로고
    • Protein import into subsarcolemmal and intermyofibrillar skeletal muscle mitochondria. Differential import regulation in distinct subcellular regions
    • Takahashi M., and Hood D.A. Protein import into subsarcolemmal and intermyofibrillar skeletal muscle mitochondria. Differential import regulation in distinct subcellular regions. J. Biol. Chem. 271 (1996) 27285-27291
    • (1996) J. Biol. Chem. , vol.271 , pp. 27285-27291
    • Takahashi, M.1    Hood, D.A.2
  • 200
    • 0018874511 scopus 로고
    • Populations of rat skeletal muscle mitochondria after exercise and immobilization
    • Krieger D.A., Tate C.A., McMillin-Wood J., and Booth F.W. Populations of rat skeletal muscle mitochondria after exercise and immobilization. J. Appl. Physiol. 48 (1980) 23-28
    • (1980) J. Appl. Physiol. , vol.48 , pp. 23-28
    • Krieger, D.A.1    Tate, C.A.2    McMillin-Wood, J.3    Booth, F.W.4
  • 201
    • 0034661510 scopus 로고    scopus 로고
    • Targeting and insertion of C-terminally anchored proteins to the mitochondrial outer membrane is specific and saturable but does not strictly require ATP or molecular chaperones
    • Lan L., Isenmann S., and Wattenberg B.W. Targeting and insertion of C-terminally anchored proteins to the mitochondrial outer membrane is specific and saturable but does not strictly require ATP or molecular chaperones. Biochem. J. 349 (2000) 611-621
    • (2000) Biochem. J. , vol.349 , pp. 611-621
    • Lan, L.1    Isenmann, S.2    Wattenberg, B.W.3
  • 202
    • 0027525536 scopus 로고
    • Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence
    • Nguyen M., Millar D.G., Yong V.W., Korsmeyer S.J., and Shore G.C. Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence. J. Biol. Chem. 268 (1993) 25265-25268
    • (1993) J. Biol. Chem. , vol.268 , pp. 25265-25268
    • Nguyen, M.1    Millar, D.G.2    Yong, V.W.3    Korsmeyer, S.J.4    Shore, G.C.5
  • 203
    • 0026580106 scopus 로고
    • The insertion of monoamine oxidase A into the outer membrane of rat liver mitochondria
    • Zhuang Z.P., Marks B., and McCauley R.B. The insertion of monoamine oxidase A into the outer membrane of rat liver mitochondria. J. Biol. Chem. 267 (1992) 591-596
    • (1992) J. Biol. Chem. , vol.267 , pp. 591-596
    • Zhuang, Z.P.1    Marks, B.2    McCauley, R.B.3
  • 204
    • 33646079874 scopus 로고    scopus 로고
    • Thermal adaptation of the yeast mitochondrial Hsp70 system is regulated by the reversible unfolding of its nucleotide exchange factor
    • Moro F., and Muga A. Thermal adaptation of the yeast mitochondrial Hsp70 system is regulated by the reversible unfolding of its nucleotide exchange factor. J. Mol. Biol. 358 (2006) 1367-1377
    • (2006) J. Mol. Biol. , vol.358 , pp. 1367-1377
    • Moro, F.1    Muga, A.2
  • 205
    • 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
  • 206
    • 0343330935 scopus 로고    scopus 로고
    • Nascent polypeptide-associated complex stimulates protein import into yeast mitochondria
    • Funfschilling U., and Rospert S. Nascent polypeptide-associated complex stimulates protein import into yeast mitochondria. Mol. Biol. Cell 10 (1999) 3289-3299
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3289-3299
    • Funfschilling, U.1    Rospert, S.2
  • 207
    • 0037051977 scopus 로고    scopus 로고
    • The nascent polypeptide-associated complex (NAC) promotes interaction of ribosomes with the mitochondrial surface in vivo
    • George R., Walsh P., Beddoe T., and Lithgow T. The nascent polypeptide-associated complex (NAC) promotes interaction of ribosomes with the mitochondrial surface in vivo. FEBS Lett. 516 (2002) 213-216
    • (2002) FEBS Lett. , vol.516 , pp. 213-216
    • George, R.1    Walsh, P.2    Beddoe, T.3    Lithgow, T.4
  • 208
    • 0032478067 scopus 로고    scopus 로고
    • The yeast nascent polypeptide-associated complex initiates protein targeting to mitochondria in vivo
    • George R., Beddoe T., Landl K., and Lithgow T. The yeast nascent polypeptide-associated complex initiates protein targeting to mitochondria in vivo. Proc. Natl. Acad. Sci .U. S. A. 95 (1998) 2296-2301
    • (1998) Proc. Natl. Acad. Sci .U. S. A. , vol.95 , pp. 2296-2301
    • George, R.1    Beddoe, T.2    Landl, K.3    Lithgow, T.4
  • 209
    • 33747358073 scopus 로고    scopus 로고
    • Import-associated translational inhibition: novel in vivo evidence for cotranslational protein import into Dictyostelium discoideum mitochondria
    • Ahmed A.U., Beech P.L., Lay S.T., Gilson P.R., and Fisher P.R. Import-associated translational inhibition: novel in vivo evidence for cotranslational protein import into Dictyostelium discoideum mitochondria. Eukaryot Cell 5 (2006) 1314-1327
    • (2006) Eukaryot Cell , vol.5 , pp. 1314-1327
    • Ahmed, A.U.1    Beech, P.L.2    Lay, S.T.3    Gilson, P.R.4    Fisher, P.R.5
  • 210
    • 14544302354 scopus 로고    scopus 로고
    • Co-translational protein targeting by the signal recognition particle
    • Shan S.O., and Walter P. Co-translational protein targeting by the signal recognition particle. FEBS Lett. 579 (2005) 921-926
    • (2005) FEBS Lett. , vol.579 , pp. 921-926
    • Shan, S.O.1    Walter, P.2
  • 211
    • 1642311878 scopus 로고    scopus 로고
    • Ribosomes specifically bind to mammalian mitochondria via protease-sensitive proteins on the outer membrane
    • MacKenzie J.A., and Payne R.M. Ribosomes specifically bind to mammalian mitochondria via protease-sensitive proteins on the outer membrane. J. Biol. Chem. 279 (2004) 9803-9810
    • (2004) J. Biol. Chem. , vol.279 , pp. 9803-9810
    • MacKenzie, J.A.1    Payne, R.M.2
  • 212
    • 0032479452 scopus 로고    scopus 로고
    • Ribosome binding to mitochondria is regulated by GTP and the transit peptide
    • Crowley K.S., and Payne R.M. Ribosome binding to mitochondria is regulated by GTP and the transit peptide. J. Biol. Chem. 273 (1998) 17278-17285
    • (1998) J. Biol. Chem. , vol.273 , pp. 17278-17285
    • Crowley, K.S.1    Payne, R.M.2
  • 213
  • 214
    • 0033200284 scopus 로고    scopus 로고
    • LETM1, a novel gene encoding a putative EF-hand Ca(2+)-binding protein, flanks the Wolf-Hirschhorn syndrome (WHS) critical region and is deleted in most WHS patients
    • Endele S., Fuhry M., Pak S.J., Zabel B.U., and Winterpacht A. LETM1, a novel gene encoding a putative EF-hand Ca(2+)-binding protein, flanks the Wolf-Hirschhorn syndrome (WHS) critical region and is deleted in most WHS patients. Genomics 60 (1999) 218-225
    • (1999) Genomics , vol.60 , pp. 218-225
    • Endele, S.1    Fuhry, M.2    Pak, S.J.3    Zabel, B.U.4    Winterpacht, A.5
  • 215
    • 3142664727 scopus 로고    scopus 로고
    • The LETM1/YOL027 gene family encodes a factor of the mitochondrial K+ homeostasis with a potential role in the Wolf-Hirschhorn syndrome
    • Nowikovsky K., Froschauer E.M., Zsurka G., Samaj J., Reipert S., Kolisek M., Wiesenberger G., and Schweyen R.J. The LETM1/YOL027 gene family encodes a factor of the mitochondrial K+ homeostasis with a potential role in the Wolf-Hirschhorn syndrome. J. Biol. Chem. 279 (2004) 30307-30315
    • (2004) J. Biol. Chem. , vol.279 , pp. 30307-30315
    • Nowikovsky, K.1    Froschauer, E.M.2    Zsurka, G.3    Samaj, J.4    Reipert, S.5    Kolisek, M.6    Wiesenberger, G.7    Schweyen, R.J.8
  • 216
    • 0347359154 scopus 로고    scopus 로고
    • LETM1, a gene deleted in Wolf-Hirschhorn syndrome, encodes an evolutionarily conserved mitochondrial protein
    • Schlickum S., Moghekar A., Simpson J.C., Steglich C., O'Brien R.J., Winterpacht A., and Endele S.U. LETM1, a gene deleted in Wolf-Hirschhorn syndrome, encodes an evolutionarily conserved mitochondrial protein. Genomics 83 (2004) 254-261
    • (2004) Genomics , vol.83 , pp. 254-261
    • Schlickum, S.1    Moghekar, A.2    Simpson, J.C.3    Steglich, C.4    O'Brien, R.J.5    Winterpacht, A.6    Endele, S.U.7
  • 219
    • 0023649886 scopus 로고
    • Structure and expression of a human gene coding for a 71 kd heat shock 'cognate' protein
    • Dworniczak B., and Mirault M.E. Structure and expression of a human gene coding for a 71 kd heat shock 'cognate' protein. Nucleic Acids Res. 15 (1987) 5181-5197
    • (1987) Nucleic Acids Res. , vol.15 , pp. 5181-5197
    • Dworniczak, B.1    Mirault, M.E.2
  • 220
    • 0034609954 scopus 로고    scopus 로고
    • Functional analysis of human metaxin in mitochondrial protein import in cultured cells and its relationship with the Tom complex
    • Abdul K.M., Terada K., Yano M., Ryan M.T., Streimann I., Hoogenraad N.J., and Mori M. Functional analysis of human metaxin in mitochondrial protein import in cultured cells and its relationship with the Tom complex. Biochem. Biophys. Res. Commun. 276 (2000) 1028-1034
    • (2000) Biochem. Biophys. Res. Commun. , vol.276 , pp. 1028-1034
    • Abdul, K.M.1    Terada, K.2    Yano, M.3    Ryan, M.T.4    Streimann, I.5    Hoogenraad, N.J.6    Mori, M.7
  • 221
    • 0033834702 scopus 로고    scopus 로고
    • Identification and functional analysis of human Tom22 for protein import into mitochondria
    • Yano M., Hoogenraad N., Terada K., and Mori M. Identification and functional analysis of human Tom22 for protein import into mitochondria. Mol. Cell. Biol. 20 (2000) 7205-7213
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7205-7213
    • Yano, M.1    Hoogenraad, N.2    Terada, K.3    Mori, M.4
  • 223
    • 0029091583 scopus 로고
    • Identification of the human mitochondrial protein import receptor, huMas20p. Complementation of delta mas20 in yeast
    • Goping I.S., Millar D.G., and Shore G.C. Identification of the human mitochondrial protein import receptor, huMas20p. Complementation of delta mas20 in yeast. FEBS Lett. 373 (1995) 45-50
    • (1995) FEBS Lett. , vol.373 , pp. 45-50
    • Goping, I.S.1    Millar, D.G.2    Shore, G.C.3
  • 224
    • 1842640408 scopus 로고    scopus 로고
    • Organization and function of the small Tim complexes acting along the import pathway of metabolite carriers into mammalian mitochondria
    • Muhlenbein N., Hofmann S., Rothbauer U., and Bauer M.F. Organization and function of the small Tim complexes acting along the import pathway of metabolite carriers into mammalian mitochondria. J. Biol. Chem. 279 (2004) 13540-13546
    • (2004) J. Biol. Chem. , vol.279 , pp. 13540-13546
    • Muhlenbein, N.1    Hofmann, S.2    Rothbauer, U.3    Bauer, M.F.4
  • 226
    • 0030569015 scopus 로고    scopus 로고
    • The preprotein translocase of the inner mitochondrial membrane: evolutionary conservation of targeting and assembly of Tim17
    • Bomer U., Rassow J., Zufall N., Pfanner N., Meijer M., and Maarse A.C. The preprotein translocase of the inner mitochondrial membrane: evolutionary conservation of targeting and assembly of Tim17. J. Mol. Biol. 262 (1996) 389-395
    • (1996) J. Mol. Biol. , vol.262 , pp. 389-395
    • Bomer, U.1    Rassow, J.2    Zufall, N.3    Pfanner, N.4    Meijer, M.5    Maarse, A.C.6
  • 229
    • 0035804671 scopus 로고    scopus 로고
    • Identification and characterization of a human mitochondrial homologue of the bacterial co-chaperone GrpE
    • Choglay A.A., Chapple J.P., Blatch G.L., and Cheetham M.E. Identification and characterization of a human mitochondrial homologue of the bacterial co-chaperone GrpE. Gene 267 (2001) 125-134
    • (2001) Gene , vol.267 , pp. 125-134
    • Choglay, A.A.1    Chapple, J.P.2    Blatch, G.L.3    Cheetham, M.E.4
  • 233
    • 0029655169 scopus 로고    scopus 로고
    • T. Nagase, N. Seki, A. Tanaka, K. Ishikawa, N. Nomura, Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1, DNA Res. 2 (1995) 167-74, 199-210.
  • 234
    • 0034655529 scopus 로고    scopus 로고
    • Functional and genomic analysis of the human mitochondrial intermediate peptidase, a putative protein partner of frataxin
    • Chew A., Sirugo G., Alsobrook II J.P., and Isaya G. Functional and genomic analysis of the human mitochondrial intermediate peptidase, a putative protein partner of frataxin. Genomics 65 (2000) 104-112
    • (2000) Genomics , vol.65 , pp. 104-112
    • Chew, A.1    Sirugo, G.2    Alsobrook II, J.P.3    Isaya, G.4
  • 235
    • 0024522738 scopus 로고
    • Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65-kilodalton mycobacterial antigen
    • Jindal S., Dudani A.K., Singh B., Harley C.B., and Gupta R.S. Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65-kilodalton mycobacterial antigen. Mol. Cell. Biol. 9 (1989) 2279-2283
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2279-2283
    • Jindal, S.1    Dudani, A.K.2    Singh, B.3    Harley, C.B.4    Gupta, R.S.5
  • 236
    • 0028926892 scopus 로고
    • Expression in Escherichia coli, purification and functional activity of recombinant human chaperonin 10
    • Legname G., Fossati G., Gromo G., Monzini N., Marcucci F., and Modena D. Expression in Escherichia coli, purification and functional activity of recombinant human chaperonin 10. FEBS Lett. 361 (1995) 211-214
    • (1995) FEBS Lett. , vol.361 , pp. 211-214
    • Legname, G.1    Fossati, G.2    Gromo, G.3    Monzini, N.4    Marcucci, F.5    Modena, D.6
  • 237
    • 0033587716 scopus 로고    scopus 로고
    • TID1, a human homolog of the Drosophila tumor suppressor l(2)tid, encodes two mitochondrial modulators of apoptosis with opposing functions
    • Syken J., De-Medina T., and Munger K. TID1, a human homolog of the Drosophila tumor suppressor l(2)tid, encodes two mitochondrial modulators of apoptosis with opposing functions. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 8499-8504
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 8499-8504
    • Syken, J.1    De-Medina, T.2    Munger, K.3
  • 238
    • 33744964531 scopus 로고    scopus 로고
    • Tid1 isoforms are mitochondrial DnaJ-like chaperones with unique carboxyl termini that determine cytosolic fate
    • Lu B., Garrido N., Spelbrink J.N., and Suzuki C.K. Tid1 isoforms are mitochondrial DnaJ-like chaperones with unique carboxyl termini that determine cytosolic fate. J. Biol. Chem. 281 (2006) 13150-13158
    • (2006) J. Biol. Chem. , vol.281 , pp. 13150-13158
    • Lu, B.1    Garrido, N.2    Spelbrink, J.N.3    Suzuki, C.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.