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Volumn 581, Issue 15, 2007, Pages 2802-2810

A dynamic machinery for import of mitochondrial precursor proteins

Author keywords

Mitochondria; Mitochondrial intermembrane space import and assembly pathway; Presequence translocase associated motor complex; Protein import; Sorting and assembly; Translocase of inner membrane complex

Indexed keywords

CARRIER PROTEIN; CHAPERONE; CYTOCHROME C OXIDASE; HEAT SHOCK PROTEIN 70; MEMBRANE PROTEIN; MITOCHONDRIAL PROTEIN; PROTEIN SUBUNIT;

EID: 34249897492     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.03.004     Document Type: Short Survey
Times cited : (72)

References (63)
  • 2
    • 0035099421 scopus 로고    scopus 로고
    • Protein import channel of the outer mitochondrial membrane: a highly stable Tom40-Tom22 core structure differentially interacts with preproteins, small Tom proteins, and import receptors
    • Meisinger C., Ryan M.T., Hill K., Model K., Lim J.H., Sickmann A., Müller H., Meyer H.E., Wagner R., and Pfanner N. Protein import channel of the outer mitochondrial membrane: a highly stable Tom40-Tom22 core structure differentially interacts with preproteins, small Tom proteins, and import receptors. Mol. Cell Biol. 21 (2001) 2337-2348
    • (2001) Mol. Cell Biol. , vol.21 , pp. 2337-2348
    • Meisinger, C.1    Ryan, M.T.2    Hill, K.3    Model, K.4    Lim, J.H.5    Sickmann, A.6    Müller, H.7    Meyer, H.E.8    Wagner, R.9    Pfanner, N.10
  • 3
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • 10.1146/annurev.biochem.76.052705.163409
    • Neupert W., and Herrmann J.M. Translocation of proteins into mitochondria. Annu. Rev. Biochem. 76 (2007) 10.1146/annurev.biochem.76.052705.163409
    • (2007) Annu. Rev. Biochem. , vol.76
    • Neupert, W.1    Herrmann, J.M.2
  • 8
    • 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
  • 9
    • 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
  • 10
    • 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
  • 12
    • 0030845840 scopus 로고    scopus 로고
    • The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44
    • Dekker P.J., Martin F., Maarse A.C., Bömer U., Müller H., Guiard B., Meijer M., Rassow J., and Pfanner N. The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44. EMBO J. 16 (1997) 5408-5419
    • (1997) EMBO J. , vol.16 , pp. 5408-5419
    • Dekker, P.J.1    Martin, F.2    Maarse, A.C.3    Bömer, U.4    Müller, H.5    Guiard, B.6    Meijer, M.7    Rassow, J.8    Pfanner, N.9
  • 14
    • 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
  • 15
    • 0142105410 scopus 로고    scopus 로고
    • Mitochondrial translocation contact sites: separation of dynamic and stabilizing elements in formation of a TOM-TIM-preprotein supercomplex
    • Chacinska A., Rehling P., Guiard B., Frazier A.E., Schulze-Specking A., Pfanner N., Voos W., and Meisinger C. Mitochondrial translocation contact sites: separation of dynamic and stabilizing elements in formation of a TOM-TIM-preprotein supercomplex. EMBO J. 22 (2003) 5370-5381
    • (2003) EMBO J. , vol.22 , pp. 5370-5381
    • Chacinska, A.1    Rehling, P.2    Guiard, B.3    Frazier, A.E.4    Schulze-Specking, A.5    Pfanner, N.6    Voos, W.7    Meisinger, C.8
  • 17
    • 33750949389 scopus 로고    scopus 로고
    • A role for Tim21 in membrane-potential-dependent preprotein sorting in mitochondria
    • van der Laan M., Wiedemann N., Mick D.U., Guiard B., Rehling P., and Pfanner N. A role for Tim21 in membrane-potential-dependent preprotein sorting in mitochondria. Curr. Biol. 16 (2006) 2271-2276
    • (2006) Curr. Biol. , vol.16 , pp. 2271-2276
    • van der Laan, M.1    Wiedemann, N.2    Mick, D.U.3    Guiard, B.4    Rehling, P.5    Pfanner, N.6
  • 18
    • 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. USA 100 (2003) 13839-13844
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13839-13844
    • D'Silva, P.D.1    Schilke, B.2    Walter, W.3    Andrew, A.4    Craig, E.A.5
  • 19
    • 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
  • 22
    • 1442335996 scopus 로고    scopus 로고
    • The J-domain related co-chaperone Tim16 is a constituent of the mitochondrial TIM23 preprotein translocase
    • Kozany C., Mokranjac D., Sichting M., Neupert W., and Hell K. The J-domain related co-chaperone Tim16 is a constituent of the mitochondrial TIM23 preprotein translocase. Nat. Struct. Mol. Biol. 11 (2004) 234-241
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 234-241
    • Kozany, C.1    Mokranjac, D.2    Sichting, M.3    Neupert, W.4    Hell, K.5
  • 24
    • 33749360278 scopus 로고    scopus 로고
    • Structure and function of Tim14 and Tim16, the J and J-like components of the mitochondrial protein import motor
    • Mokranjac D., Bourenkov G., Hell K., Neupert W., and Groll M. Structure and function of Tim14 and Tim16, the J and J-like components of the mitochondrial protein import motor. EMBO J. 25 (2006) 4675-4685
    • (2006) EMBO J. , vol.25 , pp. 4675-4685
    • Mokranjac, D.1    Bourenkov, G.2    Hell, K.3    Neupert, W.4    Groll, M.5
  • 26
    • 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
  • 27
    • 0036306343 scopus 로고    scopus 로고
    • Protein translocase of the outer mitochondrial membrane: role of import receptors in the structural organization of the TOM complex
    • Model K., Prinz T., Ruiz T., Radermacher M., Krimmer T., Kühlbrandt W., Pfanner N., and Meisinger C. Protein translocase of the outer mitochondrial membrane: role of import receptors in the structural organization of the TOM complex. J. Mol. Biol. 316 (2002) 657-666
    • (2002) J. Mol. Biol. , vol.316 , pp. 657-666
    • Model, K.1    Prinz, T.2    Ruiz, T.3    Radermacher, M.4    Krimmer, T.5    Kühlbrandt, W.6    Pfanner, N.7    Meisinger, C.8
  • 28
    • 0032188847 scopus 로고    scopus 로고
    • Tom40 form 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 form 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
  • 31
    • 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., Müller H., Hönlinger 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    Müller, H.4    Hönlinger, A.5    Pfanner, N.6
  • 32
    • 0029927409 scopus 로고    scopus 로고
    • Tom7 modulates the dynamics of the mitochondrial outer membrane translocase and plays a pathway-related role in protein import
    • Hönlinger A., Bömer U., Alconada A., Eckerskorn C., Lottspeich F., Dietmeier K., and Pfanner N. Tom7 modulates the dynamics of the mitochondrial outer membrane translocase and plays a pathway-related role in protein import. EMBO J. 15 (1996) 2125-2137
    • (1996) EMBO J. , vol.15 , pp. 2125-2137
    • Hönlinger, A.1    Bömer, U.2    Alconada, A.3    Eckerskorn, C.4    Lottspeich, F.5    Dietmeier, K.6    Pfanner, N.7
  • 33
    • 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
  • 35
    • 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
  • 36
    • 33846002342 scopus 로고    scopus 로고
    • The N-terminal domain of Tob55 has a receptor-like function in the biogenesis of mitochondrial β-barrel proteins
    • Habib S.J., Waizenegger T., Niewienda A., Paschen S.A., Neupert W., and Rapaport D. The N-terminal domain of Tob55 has a receptor-like function in the biogenesis of mitochondrial β-barrel proteins. J. Cell Biol. 176 (2007) 77-88
    • (2007) J. Cell Biol. , vol.176 , pp. 77-88
    • Habib, S.J.1    Waizenegger, T.2    Niewienda, A.3    Paschen, S.A.4    Neupert, W.5    Rapaport, D.6
  • 37
    • 2542499525 scopus 로고    scopus 로고
    • Sam35 of the mitochondrial protein sorting and assembly machinery is a peripheral outer membrane protein essential for cell viability
    • Milenkovic D., Kozjak V., Wiedemann N., Lohaus C., Meyer H.E., Guiard B., Pfanner N., and Meisinger C. Sam35 of the mitochondrial protein sorting and assembly machinery is a peripheral outer membrane protein essential for cell viability. J. Biol. Chem. 279 (2004) 22781-22785
    • (2004) J. Biol. Chem. , vol.279 , pp. 22781-22785
    • Milenkovic, D.1    Kozjak, V.2    Wiedemann, N.3    Lohaus, C.4    Meyer, H.E.5    Guiard, B.6    Pfanner, N.7    Meisinger, C.8
  • 39
    • 0344392841 scopus 로고    scopus 로고
    • A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to the cytoskeleton-based segregation machinery
    • Boldogh I.R., Nowakowski D.W., Yang H.C., Chung H., Karmon S., Royes P., and Pon L.A. A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to the cytoskeleton-based segregation machinery. Mol. Biol. Cell 14 (2003) 4618-4627
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4618-4627
    • Boldogh, I.R.1    Nowakowski, D.W.2    Yang, H.C.3    Chung, H.4    Karmon, S.5    Royes, P.6    Pon, L.A.7
  • 41
    • 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
  • 42
    • 0036224573 scopus 로고    scopus 로고
    • Oxidative protein folding in bacteria
    • Collet J.F., and Bardwell J.C. Oxidative protein folding in bacteria. Mol. Microbiol. 44 (2002) 1-8
    • (2002) Mol. Microbiol. , vol.44 , pp. 1-8
    • Collet, J.F.1    Bardwell, J.C.2
  • 43
    • 0034866458 scopus 로고    scopus 로고
    • An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/s proteins
    • Lange H., Lisowsky T., Gerber J., Mühlenhoff U., Kispal G., and Lill R. An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/s proteins. EMBO Rep. 2 (2001) 715-720
    • (2001) EMBO Rep. , vol.2 , pp. 715-720
    • Lange, H.1    Lisowsky, T.2    Gerber, J.3    Mühlenhoff, U.4    Kispal, G.5    Lill, R.6
  • 45
    • 0023659499 scopus 로고
    • Mitochondrial protein import: nucleoside triphosphates are involved in conferring import-competence to precursors
    • Pfanner N., Tropschug M., and Neupert W. Mitochondrial protein import: nucleoside triphosphates are involved in conferring import-competence to precursors. Cell 49 (1987) 815-823
    • (1987) Cell , vol.49 , pp. 815-823
    • Pfanner, N.1    Tropschug, M.2    Neupert, W.3
  • 46
    • 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. Mitochondrial preproteins en route from the outer membrane to the inner membrane are exposed to the intermembrane space. FEBS Lett. 293 (1991) 85-88
    • (1991) FEBS Lett. , vol.293 , pp. 85-88
    • Rassow, J.1    Pfanner, N.2
  • 47
    • 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. The Tim9p-Tim10p complex binds to the transmembrane domains of the ADP/ATP carrier. EMBO J. 21 (2002) 942-953
    • (2002) EMBO J. , vol.21 , pp. 942-953
    • Curran, S.P.1    Leuenberger, D.2    Oppliger, W.3    Koehler, C.M.4
  • 50
    • 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. Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria. Cell 87 (1996) 33-41
    • (1996) Cell , vol.87 , pp. 33-41
    • Bauer, M.F.1    Sirrenberg, C.2    Neupert, W.3    Brunner, M.4
  • 51
    • 14844334925 scopus 로고    scopus 로고
    • Conserved N-terminal negative charges in the Tim17 subunit of the TIM23 translocase play a critical role in the import of preproteins into mitochondria
    • Meier S., Neupert W., and Herrmann J.M. Conserved N-terminal negative charges in the Tim17 subunit of the TIM23 translocase play a critical role in the import of preproteins into mitochondria. J. Biol. Chem. 280 (2005) 7777-7785
    • (2005) J. Biol. Chem. , vol.280 , pp. 7777-7785
    • Meier, S.1    Neupert, W.2    Herrmann, J.M.3
  • 52
    • 33947509012 scopus 로고    scopus 로고
    • Tim17p regulates the twin pore structure and voltage gating of the mitochondrial import complex TIM23
    • Martinez-Caballero S., Grigoriev S.M., Herrmann J.M., Campo M.L., and Kinnally K.W. Tim17p regulates the twin pore structure and voltage gating of the mitochondrial import complex TIM23. J. Biol. Chem. 282 (2007) 3584-3593
    • (2007) J. Biol. Chem. , vol.282 , pp. 3584-3593
    • Martinez-Caballero, S.1    Grigoriev, S.M.2    Herrmann, J.M.3    Campo, M.L.4    Kinnally, K.W.5
  • 53
    • 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., Zufall N., Hönlinger A., and Pfanner N. The intermembrane space domain of mitochondrial Tom22 functions as a trans binding site for preproteins with N-terminal targeting sequences. Mol. Cell. Biol. 17 (1997) 6574-6584
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6574-6584
    • Moczko, M.1    Bömer, U.2    Kübrich, M.3    Zufall, N.4    Hönlinger, A.5    Pfanner, N.6
  • 54
    • 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
  • 57
    • 0033612301 scopus 로고    scopus 로고
    • The protein import motor of mitochondria: unfolding and trapping of preproteins are distinct and separable functions of matrix Hsp70
    • Voisine C., Craig E.A., Zufall N., von Ahsen O., Pfanner N., and Voos W. The protein import motor of mitochondria: unfolding and trapping of preproteins are distinct and separable functions of matrix Hsp70. Cell 97 (1999) 565-574
    • (1999) Cell , vol.97 , pp. 565-574
    • Voisine, C.1    Craig, E.A.2    Zufall, N.3    von Ahsen, O.4    Pfanner, N.5    Voos, W.6
  • 58
    • 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
  • 59
    • 4444315535 scopus 로고    scopus 로고
    • The presequence translocase-associated protein import motor of mitochondria: Pam16 functions in an antagonistic manner to Pam18
    • Li Y., Dudek J., Guiard B., Pfanner N., Rehling P., and Voos W. The presequence translocase-associated protein import motor of mitochondria: Pam16 functions in an antagonistic manner to Pam18. J. Biol. Chem. 279 (2004) 38047-38054
    • (2004) J. Biol. Chem. , vol.279 , pp. 38047-38054
    • Li, Y.1    Dudek, J.2    Guiard, B.3    Pfanner, N.4    Rehling, P.5    Voos, W.6
  • 60
    • 9644255736 scopus 로고    scopus 로고
    • Zim17, a novel zinc finger protein essential for protein import into mitochondria
    • Burri L., Vascotto K., Fredersdorf S., Tiedt R., Hall M.N., and Lithgow T. Zim17, a novel zinc finger protein essential for protein import into mitochondria. J. Biol. Chem. 279 (2004) 50243-50249
    • (2004) J. Biol. Chem. , vol.279 , pp. 50243-50249
    • Burri, L.1    Vascotto, K.2    Fredersdorf, S.3    Tiedt, R.4    Hall, M.N.5    Lithgow, T.6
  • 61
    • 11844292805 scopus 로고    scopus 로고
    • Identification of a novel member of yeast mitochondrial Hsp70-associated motor and chaperone proteins that facilitates protein translocation across the inner membrane
    • Yamamoto H., Momose T., Yatsukawa Y., Ohshima C., Ishikawa D., Sato T., Tamura Y., Ohwa Y., and Endo T. Identification of a novel member of yeast mitochondrial Hsp70-associated motor and chaperone proteins that facilitates protein translocation across the inner membrane. FEBS Lett. 579 (2005) 507-511
    • (2005) FEBS Lett. , vol.579 , pp. 507-511
    • Yamamoto, H.1    Momose, T.2    Yatsukawa, Y.3    Ohshima, C.4    Ishikawa, D.5    Sato, T.6    Tamura, Y.7    Ohwa, Y.8    Endo, T.9
  • 62
    • 16344363965 scopus 로고    scopus 로고
    • Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1
    • Sichting M., Mokranjac D., Azem A., Neupert W., and Hell K. Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1. EMBO J. 24 (2005) 1046-1056
    • (2005) EMBO J. , vol.24 , pp. 1046-1056
    • Sichting, M.1    Mokranjac, D.2    Azem, A.3    Neupert, W.4    Hell, K.5


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