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Volumn 118, Issue 17, 2005, Pages 3985-3995

Import of rat mitochondrial citrate carrier (CIC) at increasing salt concentrations promotes presequence binding to import receptor Tom20 and inhibits membrane translocation

Author keywords

Citrate carrier; Membrane translocation; Mitochondria

Indexed keywords

CARRIER PROTEIN; CHAPERONE; CITRATE CARRIER PROTEIN; PHOSPHATE TRANSPORTER; PROTEIN PRECURSOR; TRANSLOCASE OF OUTER MITOCHONDRIAL MEMBRANE 20; UNCLASSIFIED DRUG;

EID: 26244443715     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.02526     Document Type: Article
Times cited : (13)

References (72)
  • 1
    • 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. (2000). Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20. Cell 100, 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
  • 2
    • 12844276571 scopus 로고    scopus 로고
    • Signal-anchored proteins follow a unique insertion pathway into the outer membrane of mitochondria
    • Ahting, U., Waizenegger, T., Neupert, W. and Rapaport, D. (2005). Signal-anchored proteins follow a unique insertion pathway into the outer membrane of mitochondria. J. Biol. Chem. 280, 48-53.
    • (2005) J. Biol. Chem. , vol.280 , pp. 48-53
    • Ahting, U.1    Waizenegger, T.2    Neupert, W.3    Rapaport, D.4
  • 3
    • 0030272378 scopus 로고    scopus 로고
    • Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria
    • Bauer, M. F., Sirrenberg, C., Neupert, W. and Brunner, M. (1996). Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria. Cell 87, 33-41.
    • (1996) Cell , vol.87 , pp. 33-41
    • Bauer, M.F.1    Sirrenberg, C.2    Neupert, W.3    Brunner, M.4
  • 4
    • 0001777212 scopus 로고    scopus 로고
    • Protein translocation into mitochondria: The role of TIM complexes
    • Bauer, M. F., Hofmann, S., Neupert, W. and Brunner, M. (2000). Protein translocation into mitochondria: the role of TIM complexes. Trends Cell Biol. 10, 25-31.
    • (2000) Trends Cell Biol. , vol.10 , pp. 25-31
    • Bauer, M.F.1    Hofmann, S.2    Neupert, W.3    Brunner, M.4
  • 5
    • 0029619088 scopus 로고
    • Acidic receptor domains on both sides of the outer membrane mediate translocation of precursor proteins into yeast mitochondria
    • Bolliger, L., Junne, T., Schatz, G. and Lithgow, T. (1995). Acidic receptor domains on both sides of the outer membrane mediate translocation of precursor proteins into yeast mitochondria. EMBO J. 14, 6318-6326.
    • (1995) EMBO J. , vol.14 , pp. 6318-6326
    • Bolliger, L.1    Junne, T.2    Schatz, G.3    Lithgow, T.4
  • 6
    • 0038889171 scopus 로고    scopus 로고
    • Separation of structural and dynamic functions of the mitochondrial translocase: Tim44 is crucial for the inner membrane import sites in translocation of tightly folded domains, but not of loosely folded preproteins
    • Bömer, U., Maarse, A. C., Martin, F., Geissler, A., Merlin, A., Schönfisch, B., Meijer, M., Pfanner, N. and Rassow, J. (1998). Separation of structural and dynamic functions of the mitochondrial translocase: Tim44 is crucial for the inner membrane import sites in translocation of tightly folded domains, but not of loosely folded preproteins. EMBO J. 17, 4226-4237.
    • (1998) EMBO J. , vol.17 , pp. 4226-4237
    • Bömer, U.1    Maarse, A.C.2    Martin, F.3    Geissler, A.4    Merlin, A.5    Schönfisch, B.6    Meijer, M.7    Pfanner, N.8    Rassow, J.9
  • 7
    • 0030769419 scopus 로고    scopus 로고
    • Differential recognition of preproteins by purified cytosolic domains of the mitochondrial import receptors Tom20, Tom22, and Tom70
    • Brix, J., Dietmeier, K. and Pfanner, N. (1997). Differential recognition of preproteins by purified cytosolic domains of the mitochondrial import receptors Tom20, Tom22, and Tom70. J. Biol. Chem. 272, 20730-20735.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20730-20735
    • Brix, J.1    Dietmeier, K.2    Pfanner, N.3
  • 8
    • 0040610676 scopus 로고    scopus 로고
    • Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 in a presequence-carrying preprotein and in a non-cleavable preprotein
    • Brix, J., Rüdiger, S., Bukau, B., Schneider-Mergener, J. and Pfanner, N. (1999). Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 in a presequence-carrying preprotein and in a non-cleavable preprotein. J. Biol. Chem. 274, 16522-16530.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16522-16530
    • Brix, J.1    Rüdiger, S.2    Bukau, B.3    Schneider-Mergener, J.4    Pfanner, N.5
  • 9
    • 0036499987 scopus 로고    scopus 로고
    • The Tim9p-Tim10p complex binds to the transmembrane domains of the ADP/ATP carrier
    • Curran, S. P., Leuenberger, D., Oppliger, W. and Koehler, C. M. (2002a). The Tim9p-Tim10p complex binds to the transmembrane domains of the ADP/ATP carrier. EMBO J. 21, 942-953.
    • (2002) EMBO J. , vol.21 , pp. 942-953
    • Curran, S.P.1    Leuenberger, D.2    Oppliger, W.3    Koehler, C.M.4
  • 10
    • 0037119946 scopus 로고    scopus 로고
    • The role of the Tim8p-Tim13p complex in a conserved import pathway for mitochondrial polytopic inner membrane proteins
    • Curran, S. P., Leuenberger, D., Schmidt, E. and Koehler, C. M. (2002b). The role of the Tim8p-Tim13p complex in a conserved import pathway for mitochondrial polytopic inner membrane proteins. J. Cell Biol. 158, 1017-1027.
    • (2002) J. Cell Biol. , vol.158 , pp. 1017-1027
    • Curran, S.P.1    Leuenberger, D.2    Schmidt, E.3    Koehler, C.M.4
  • 12
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K. A. (1990). Dominant forces in protein folding. Biochemistry 29, 7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 13
    • 0345189360 scopus 로고    scopus 로고
    • Tom40 protein import channel binds to non-native proteins and prevents their aggregation
    • Esaki, M., Kanamori, T., Nishikawa, S., Shin, I., Schulz, P. J. and Endo, T. (2003). Tom40 protein import channel binds to non-native proteins and prevents their aggregation. Nat. Struct. Biol. 10, 988-994.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 988-994
    • Esaki, M.1    Kanamori, T.2    Nishikawa, S.3    Shin, I.4    Schulz, P.J.5    Endo, T.6
  • 14
    • 0027490849 scopus 로고
    • A dual role for mitochondrial heat shock protein 70 in membrane translocation of preproteins
    • Gambill, B. D., Voos, W., Kang, P. J., Miao, B., Langer, T., Craig, E. A. and Pfanner, N. (1993). A dual role for mitochondrial heat shock protein 70 in membrane translocation of preproteins. J. Cell Biol. 123, 109-117.
    • (1993) J. Cell Biol. , vol.123 , pp. 109-117
    • Gambill, B.D.1    Voos, W.2    Kang, P.J.3    Miao, B.4    Langer, T.5    Craig, A.E.6    Pfanner, N.7
  • 15
    • 0034077456 scopus 로고    scopus 로고
    • Biogenesis of the yeast frataxin homolog Yfh1p. Tim44-dependent transfer to mtHsp70 facilitates folding of newly imported proteins in mitochondria
    • Geissler, A., Krimmer, T., Schönfisch, B., Meijer, M. and Rassow, J. (2000). Biogenesis of the yeast frataxin homolog Yfh1p. Tim44-dependent transfer to mtHsp70 facilitates folding of newly imported proteins in mitochondria. Eur. J. Biochem. 267, 3167-3180.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3167-3180
    • Geissler, A.1    Krimmer, T.2    Schönfisch, B.3    Meijer, M.4    Rassow, J.5
  • 16
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F. U. (1996). Molecular chaperones in cellular protein folding. Nature 381, 571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 18
    • 0028948675 scopus 로고
    • The yeast mitochondria 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. (1995). The yeast mitochondria protein import receptor Mas20p binds precursor proteins through electrostatic interaction with the positively charged presequence. J. Biol. Chem. 270, 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
  • 19
    • 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. (1997). Insertion into the mitochondrial inner membrane of a polytopic protein, the nuclear-encoded Oxa1p. EMBO J. 9, 2217-2226.
    • (1997) EMBO J. , vol.9 , pp. 2217-2226
    • Herrmann, J.M.1    Neupert, W.2    Stuart, R.A.3
  • 20
    • 0024327616 scopus 로고
    • Disrupted yeast mitochondria can import precursor proteins directly through their inner membrane
    • Hwang, S., Jascur, T., Vestweber, D., Pon, L. and Schatz, G. (1989). Disrupted yeast mitochondria can import precursor proteins directly through their inner membrane. J. Cell Biol. 109, 487-493.
    • (1989) J. Cell Biol. , vol.109 , pp. 487-493
    • Hwang, S.1    Jascur, T.2    Vestweber, D.3    Pon, L.4    Schatz, G.5
  • 21
    • 0027441813 scopus 로고
    • The mitochondrial tricarboxylate transport protein. cDNA cloning, primary structure, and comparison with other mitochondrial transport proteins
    • Kaplan, R. S., Mayor, J. A. and Wood, D. O. (1993). The mitochondrial tricarboxylate transport protein. cDNA cloning, primary structure, and comparison with other mitochondrial transport proteins. J. Biol. Chem. 268, 13682-13690.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13682-13690
    • Kaplan, R.S.1    Mayor, J.A.2    Wood, D.O.3
  • 22
    • 7544219638 scopus 로고    scopus 로고
    • New developments in mitochondrial assembly
    • Koehler, C. M. (2004). New developments in mitochondrial assembly. Annu. Rev. Cell Dev. Biol. 20, 309-335.
    • (2004) Annu. Rev. Cell Dev. Biol. , vol.20 , pp. 309-335
    • Koehler, C.M.1
  • 24
    • 0033230058 scopus 로고    scopus 로고
    • How membrane proteins travel across the mitochondrial intermembrane space
    • Koehler, C. M., Merchant, S. and Schatz, G. (1999). How membrane proteins travel across the mitochondrial intermembrane space. Trends Biochem. Sci. 24, 428-432.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 428-432
    • Koehler, C.M.1    Merchant, S.2    Schatz, G.3
  • 25
    • 0035931764 scopus 로고    scopus 로고
    • Biogenesis of porin of the outer mitochondrial membrane involves an import pathway via receptors and the general import pore of the TOM complex
    • Krimmer, T., Rapaport, D., Ryan, M. T., Meisinger, C., Kassenbrock, C. K., Blachly-Dyson, E., Forte, M., Douglas, M. G., Neupert, W. et al. (2001). Biogenesis of porin of the outer mitochondrial membrane involves an import pathway via receptors and the general import pore of the TOM complex. J. Cell Biol. 152, 289-300.
    • (2001) J. Cell Biol. , vol.152 , pp. 289-300
    • Krimmer, T.1    Rapaport, D.2    Ryan, M.T.3    Meisinger, C.4    Kassenbrock, C.K.5    Blachly-Dyson, E.6    Forte, M.7    Douglas, M.G.8    Neupert, W.9
  • 26
    • 0032569031 scopus 로고    scopus 로고
    • The import route of ADP/ATP carrier into mitochondria separates from the general import pathway of cleavable preproteins at the trans side of the outer membrane
    • Kübrich, M., Rassow, J., Voos, W., Pfanner, N. and Hönlinger, A. (1998). The import route of ADP/ATP carrier into mitochondria separates from the general import pathway of cleavable preproteins at the trans side of the outer membrane. J. Biol. Chem. 273, 16374-16381.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16374-16381
    • Kübrich, M.1    Rassow, J.2    Voos, W.3    Pfanner, N.4    Hönlinger, A.5
  • 27
    • 0347157958 scopus 로고    scopus 로고
    • The Alb3/Oxa1/YidC protein family: Membrane-localized chaperones facilitating membrane protein insertion?
    • Kuhn, A., Stuart, R., Henry, R. and Dalbey, R. E. (2003). The Alb3/Oxa1/YidC protein family: membrane-localized chaperones facilitating membrane protein insertion? Trends Cell Biol. 13, 510-516.
    • (2003) Trends Cell Biol. , vol.13 , pp. 510-516
    • Kuhn, A.1    Stuart, R.2    Henry, R.3    Dalbey, R.E.4
  • 28
    • 1942468196 scopus 로고    scopus 로고
    • The role and structure of mitochondrial carriers
    • Kunji, E. R. (2004). The role and structure of mitochondrial carriers. FEBS Lett. 564, 239-244.
    • (2004) FEBS Lett. , vol.564 , pp. 239-244
    • Kunji, E.R.1
  • 31
    • 0028264383 scopus 로고
    • Deletion of the receptor MOM19 strongly impairs import of cleavable preproteins into Saccharomyces cerevisiae mitochondria
    • Moczko, M., Ehmann, B., Gärtner, F., Hönlinger, A., Schäfer, E. and Pfanner, N. (1994). Deletion of the receptor MOM19 strongly impairs import of cleavable preproteins into Saccharomyces cerevisiae mitochondria. J. Biol. Chem. 269, 9045-9051.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9045-9051
    • Moczko, M.1    Ehmann, B.2    Gärtner, F.3    Hönlinger, A.4    Schäfer, E.5    Pfanner, N.6
  • 32
    • 1842326155 scopus 로고    scopus 로고
    • The intermembrane space domain of mitochondrial Tom22 functions as a trans binding site for preproteins with N-terminal targeting sequences
    • Moczko, M., Bömer, U., Kübrich, M., Hönlinger, A, Zufall, N. and Pfanner, N. (1997). The intermembrane space domain of mitochondrial Tom22 functions as a trans binding site for preproteins with N-terminal targeting sequences. Mol. Cell. Biol. 17, 6574-6584.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6574-6584
    • Moczko, M.1    Bömer, U.2    Kübrich, M.3    Hönlinger, A.4    Zufall, N.5    Pfanner, N.6
  • 33
    • 0036977273 scopus 로고    scopus 로고
    • Bcl-2 and porin follow different pathways of TOM-dependent insertion into the mitochondrial outer membrane
    • Motz, C., Martin, H., Krimmer, T. and Rassow, J. (2002). Bcl-2 and porin follow different pathways of TOM-dependent insertion into the mitochondrial outer membrane. J. Mol. Biol. 323, 729-738.
    • (2002) J. Mol. Biol. , vol.323 , pp. 729-738
    • Motz, C.1    Martin, H.2    Krimmer, T.3    Rassow, J.4
  • 34
    • 0037090477 scopus 로고    scopus 로고
    • VDAC and the bacterial porin PorB of Neisseria gonorrhoeae share mitochondrial import pathways
    • Müller, A., Rassow, J., Grimm, J., Machuy, N., Meyer, T. F. and Rudel, T. (2002). VDAC and the bacterial porin PorB of Neisseria gonorrhoeae share mitochondrial import pathways. EMBO J. 21, 1916-1929.
    • (2002) EMBO J. , vol.21 , pp. 1916-1929
    • Müller, A.1    Rassow, J.2    Grimm, J.3    Machuy, N.4    Meyer, T.F.5    Rudel, T.6
  • 35
    • 7444242630 scopus 로고    scopus 로고
    • The N-terminal extension of plant mitochondrial carrier proteins is removed by two-step processing: The first cleavage is by the mitochondrial processing peptidase
    • Murcha, M. W., Elhafez, D., Millar, A. H. and Whelan, J. (2004). The N-terminal extension of plant mitochondrial carrier proteins is removed by two-step processing: The first cleavage is by the mitochondrial processing peptidase. J. Mol. Biol. 344, 443-454.
    • (2004) J. Mol. Biol. , vol.344 , pp. 443-454
    • Murcha, M.W.1    Elhafez, D.2    Millar, A.H.3    Whelan, J.4
  • 36
    • 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. (2001). 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, 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
  • 37
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert, W. (1997). Protein import into mitochondria. Annu. Rev. Biochem. 66, 863-917.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 40
    • 0024219719 scopus 로고
    • Import pathways of precursor proteins into mitochondria: Multiple receptor sites are followed by a common membrane insertion site
    • Pfaller, R., Steger, H. F., Rassow, J., Pfanner, N. and Neupert, W. (1988). Import pathways of precursor proteins into mitochondria: multiple receptor sites are followed by a common membrane insertion site. J. Cell Biol. 107, 2488-2490.
    • (1988) J. Cell Biol. , vol.107 , pp. 2488-2490
    • Pfaller, R.1    Steger, H.F.2    Rassow, J.3    Pfanner, N.4    Neupert, W.5
  • 41
    • 0024558880 scopus 로고
    • Mitochondrial protein import. Bypass of proteinaceous surface receptors can occur with low specificity and efficiency
    • Pfaller, R., Pfanner, N. and Neupert, W. (1989). Mitochondrial protein import. Bypass of proteinaceous surface receptors can occur with low specificity and efficiency. J. Biol. Chem. 264, 34-39.
    • (1989) J. Biol. Chem. , vol.264 , pp. 34-39
    • Pfaller, R.1    Pfanner, N.2    Neupert, W.3
  • 42
    • 0023644933 scopus 로고
    • Distinct steps in the import of ADP/ATP carrier into mitochondria
    • Pfanner, N. and Neupert, W. (1987). Distinct steps in the import of ADP/ATP carrier into mitochondria. J. Biol. Chem. 262, 7528-7536.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7528-7536
    • Pfanner, N.1    Neupert, W.2
  • 43
    • 0035344460 scopus 로고    scopus 로고
    • Versatility of the mitochondrial protein import machinery
    • Pfanner, N. and Geissler, A. (2001). Versatility of the mitochondrial protein import machinery. Nat. Rev. Mol. Cell Biol. 2, 339-349.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 339-349
    • Pfanner, N.1    Geissler, A.2
  • 44
    • 0023659499 scopus 로고
    • Mitochondrial protein import: Nucleoside triphosphates are involved in conferring import-competence to precursors
    • Pfanner, N., Tropschug, M. and Neupert, W. (1987). Mitochondrial protein import: nucleoside triphosphates are involved in conferring import-competence to precursors. Cell 49, 815-823.
    • (1987) Cell , vol.49 , pp. 815-823
    • Pfanner, N.1    Tropschug, M.2    Neupert, W.3
  • 45
    • 0026057311 scopus 로고
    • Mitochondrial import receptors for precursor proteins
    • Pfanner, N., Söllner, T. and Neupert, W. (1991). Mitochondrial import receptors for precursor proteins. Trends Biochem. Sci. 16, 63-67.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 63-67
    • Pfanner, N.1    Söllner, T.2    Neupert, W.3
  • 47
    • 0242607644 scopus 로고    scopus 로고
    • Finding the right organene. Targeting signals in mitochondrial outer-membrane proteins
    • Rapaport, D. (2003). Finding the right organene. Targeting signals in mitochondrial outer-membrane proteins. EMBO Rep. 4, 948-952.
    • (2003) EMBO Rep. , vol.4 , pp. 948-952
    • Rapaport, D.1
  • 48
    • 0001858221 scopus 로고    scopus 로고
    • Protein folding and import into organelles
    • (ed. B. D. Hames and S. J. Higgins), Oxford: IRL Press
    • Rassow, J. (1999). Protein folding and import into organelles. In Post-Translational Processing: A Practical Approach (ed. B. D. Hames and S. J. Higgins), pp. 43-94. Oxford: IRL Press.
    • (1999) Post-Translational Processing: A Practical Approach , pp. 43-94
    • Rassow, J.1
  • 49
    • 0026040249 scopus 로고
    • Mitochondrial preproteins en route from the outer membrane to the inner membrane are exposed to the intermembrane space
    • Rassow, J. and Pfanner, N. (1991). Mitochondrial preproteins en route from the outer membrane to the inner membrane are exposed to the intermembrane space. FEBS Lett. 293, 85-88.
    • (1991) FEBS Lett. , vol.293 , pp. 85-88
    • Rassow, J.1    Pfanner, N.2
  • 50
    • 0034209222 scopus 로고    scopus 로고
    • The protein import machinery of the mitochondrial membranes
    • Rassow, J. and Pfanner, N. (2000). The protein import machinery of the mitochondrial membranes. Traffic 1, 457-464.
    • (2000) Traffic , vol.1 , pp. 457-464
    • Rassow, J.1    Pfanner, N.2
  • 51
    • 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. (2003). Insertion of hydrophobic membrane proteins into the inner mitochondrial membrane - a guided tour. J. Mol. Biol. 326, 639-657.
    • (2003) J. Mol. Biol. , vol.326 , pp. 639-657
    • Rehling, P.1    Pfanner, N.2    Meisinger, C.3
  • 53
    • 0035160744 scopus 로고    scopus 로고
    • Intramitochondrial dimerization of citrate synthase characterized by blue native electrophoresis
    • Reif, S., Voos, W. and Rassow, J. (2001). Intramitochondrial dimerization of citrate synthase characterized by blue native electrophoresis. Anal. Biochem. 288, 97-99.
    • (2001) Anal. Biochem. , vol.288 , pp. 97-99
    • Reif, S.1    Voos, W.2    Rassow, J.3
  • 54
    • 0023920458 scopus 로고
    • Mitochondrial presequences
    • Roise, D. and Schatz, G. (1988). Mitochondrial presequences. J. Biol. Chem. 263, 4509-4511.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4509-4511
    • Roise, D.1    Schatz, G.2
  • 55
    • 0023333813 scopus 로고
    • Sequence of the bovine mitochondrial phosphate carrier protein: Structural relationship to ADP/ATP translocase and the brown fat mitochondria uncoupling protein
    • Runswick, M. J., Powell, S. J., Nyren, P. and Walker, J. E. (1987). Sequence of the bovine mitochondrial phosphate carrier protein: structural relationship to ADP/ATP translocase and the brown fat mitochondria uncoupling protein. EMBO J. 6, 1367-1373.
    • (1987) EMBO J. , vol.6 , pp. 1367-1373
    • Runswick, M.J.1    Powell, S.J.2    Nyren, P.3    Walker, J.E.4
  • 56
    • 0040610684 scopus 로고    scopus 로고
    • Functional staging of ADP/ATP carrier translocation across the outer mitochondrial membrane
    • Ryan, M. T., Müller, H. and Pfanner, N. (1999). Functional staging of ADP/ATP carrier translocation across the outer mitochondrial membrane. J. Biol. Chem. 274, 20619-20627.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20619-20627
    • Ryan, M.T.1    Müller, H.2    Pfanner, N.3
  • 57
    • 0023277329 scopus 로고
    • 17th Sir Hans Krebs lecture. Signals guiding proteins to their correct locations in mitochondria
    • Schatz, G. (1987). 17th Sir Hans Krebs lecture. Signals guiding proteins to their correct locations in mitochondria. Eur. J. Biochem. 165, 1-6.
    • (1987) Eur. J. Biochem. , vol.165 , pp. 1-6
    • Schatz, G.1
  • 58
    • 1842368473 scopus 로고    scopus 로고
    • Just follow the acid chain
    • Schatz, G. (1997). Just follow the acid chain. Nature 388, 121-122.
    • (1997) Nature , vol.388 , pp. 121-122
    • Schatz, G.1
  • 61
    • 0025327946 scopus 로고
    • A mitochondrial import receptor for the ADP/ATP carrier
    • Söllner, T., Pfaller, R., Griffith, G., Pfanner, N. and Neupert, W. (1990). A mitochondrial import receptor for the ADP/ATP carrier. Cell 62, 107-115.
    • (1990) Cell , vol.62 , pp. 107-115
    • Söllner, T.1    Pfaller, R.2    Griffith, G.3    Pfanner, N.4    Neupert, W.5
  • 62
    • 0037379222 scopus 로고    scopus 로고
    • Mitochondrial protein import: Recognition of integral import signals of BCS1 by the TOM complex
    • Stan, T., Brix, J., Schneider-Mergener, J., Pfanner, N., Neupert, W. and Rapaport, D. (2003). Mitochondrial protein import: recognition of integral import signals of BCS1 by the TOM complex. Mol. Cell. Biol. 23, 2239-2250.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2239-2250
    • Stan, T.1    Brix, J.2    Schneider-Mergener, J.3    Pfanner, N.4    Neupert, W.5    Rapaport, D.6
  • 64
    • 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. (2002). Characterization of rat Tom70 as a receptor of the preprotein translocase of the mitochondrial outer membrane. J. Cell Sci. 115, 1895-1905.
    • (2002) J. Cell Sci. , vol.115 , pp. 1895-1905
    • Suzuki, H.1    Maeda, M.2    Mihara, K.3
  • 67
    • 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. (1993). 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, 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
  • 68
    • 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. (2001). The three modules of ADP/ATP carrier cooperate in receptor recruitment and translocation into mitochondria. EMBO J. 20, 951-960.
    • (2001) EMBO J. , vol.20 , pp. 951-960
    • Wiedemann, N.1    Pfanner, N.2    Ryan, M.T.3
  • 70
    • 0026647854 scopus 로고
    • The cleavable presequence is not essential for import and assembly of the phosphate carrier of mammalian mitochondria but enhances the specificity and efficiency of import
    • Zara, V., Palmieri, F., Mahlke, K. and Pfanner, N. (1992). The cleavable presequence is not essential for import and assembly of the phosphate carrier of mammalian mitochondria but enhances the specificity and efficiency of import. J. Biol. Chem. 267, 12077-12081.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12077-12081
    • Zara, V.1    Palmieri, F.2    Mahlke, K.3    Pfanner, N.4
  • 71
    • 26244446123 scopus 로고    scopus 로고
    • Import of metabolite carrier proteins into mitochondria
    • (ed. S. G. Pandalai), Kerala, India: Research Signpost
    • Zara, V., Ferramosca, A. and Rassow, J. (2003a). Import of metabolite carrier proteins into mitochondria. In Recent Research Developments in Molecular & Cellular Biology. Vol. 4 (ed. S. G. Pandalai), pp. 101-114. Kerala, India: Research Signpost.
    • (2003) Recent Research Developments in Molecular & Cellular Biology , vol.4 , pp. 101-114
    • Zara, V.1    Ferramosca, A.2    Rassow, J.3
  • 72
    • 0037225505 scopus 로고    scopus 로고
    • Biogenesis of rat mitochondrial citrate carrier (CIC): The N-terminal presequence facilitates the solubility of the preprotein but does not act as a targeting signal
    • Zara, V., Ferramosca, A., Palmisano, I., Palmieri, F. and Rassow, J. (2003b). Biogenesis of rat mitochondrial citrate carrier (CIC): The N-terminal presequence facilitates the solubility of the preprotein but does not act as a targeting signal. J. Mol. Biol. 325, 399-408.
    • (2003) J. Mol. Biol. , vol.325 , pp. 399-408
    • Zara, V.1    Ferramosca, A.2    Palmisano, I.3    Palmieri, F.4    Rassow, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.