메뉴 건너뛰기




Volumn 74, Issue 4, 1998, Pages 1732-1743

Strong precursor-pore interactions constrain models for mitochondrial protein import

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 70;

EID: 0031918163     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77884-1     Document Type: Article
Times cited : (46)

References (79)
  • 1
    • 0030841365 scopus 로고    scopus 로고
    • The mitochondrial hsp70 chaperone system: Effect of adenine nucleotides, peptide substrate, and mGrpE on the oligomeric state of mhsp70
    • Azem, A., W. Oppliger, A. Lustig, P. Jenö, B. Feifel, G. Schatz, and M. Horst. 1997. The mitochondrial hsp70 chaperone system: effect of adenine nucleotides, peptide substrate, and mGrpE on the oligomeric state of mhsp70. J. Biol. Chem. 272:20901-20906.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20901-20906
    • Azem, A.1    Oppliger, W.2    Lustig, A.3    Jenö, P.4    Feifel, B.5    Schatz, G.6    Horst, M.7
  • 2
    • 0027484417 scopus 로고
    • Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP
    • Blond-Elguindi, S., S. E. Cwjrla, W. J. Dower, R. J. Lipshutz, S. R. Sprang, J. F. Sambrook, and M.-J. H. Gething. 1993. Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell. 75:717-728.
    • (1993) Cell , vol.75 , pp. 717-728
    • Blond-Elguindi, S.1    Cwjrla, S.E.2    Dower, W.J.3    Lipshutz, R.J.4    Sprang, S.R.5    Sambrook, J.F.6    Gething, M.-J.H.7
  • 4
    • 0040667180 scopus 로고    scopus 로고
    • Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane
    • Borner, U., M. Meijer, A. C. Maarse, A. Hönlinger, P. J. T. Dekker, N. Pfanncr, and J. Rassow. 1997. Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane. EMBO J. 16:2205-2216.
    • (1997) EMBO J , vol.16 , pp. 2205-2216
    • Borner, U.1    Meijer, M.2    Maarse, A.C.3    Hönlinger, A.4    Dekker, P.J.T.5    Pfanncr, N.6    Rassow, J.7
  • 5
  • 6
    • 18344407941 scopus 로고
    • Measurement of the isometric force exerted by a single kinesin molecule
    • Coppin, C. M., J. T. Finer, J. A. Spudich, and R. D. Vale. 1995. Measurement of the isometric force exerted by a single kinesin molecule. Biophys. J. 68:2425-2445.
    • (1995) Biophys. J. , vol.68 , pp. 2425-2445
    • Coppin, C.M.1    Finer, J.T.2    Spudich, J.A.3    Vale, R.D.4
  • 7
    • 0003932766 scopus 로고
    • W. H. Freeman, New York
    • Creighton, T. 1993. Proteins. W. H. Freeman, New York.
    • (1993) Proteins
    • Creighton, T.1
  • 8
    • 0031577340 scopus 로고    scopus 로고
    • Role of mitochondrial GrpE and phosphate in the ATPase cycle of matrix Hsp70
    • Dekker, P. J. T., and N. Pfanner. 1997. Role of mitochondrial GrpE and phosphate in the ATPase cycle of matrix Hsp70. J. Mol. Biol. 270: 321-327.
    • (1997) J. Mol. Biol. , vol.270 , pp. 321-327
    • Dekker, P.J.T.1    Pfanner, N.2
  • 9
    • 0041339442 scopus 로고
    • Modeling complex systems: Stochastic processes, stochastic differential equations, and Fokker-Planck equations
    • L. Nadel and D. Stein, editors. Addison-Wesley, Redwood City, CA
    • Doering, C. 1990. Modeling complex systems: stochastic processes, stochastic differential equations, and Fokker-Planck equations. In 1990 Lectures in Complex Systems. L. Nadel and D. Stein, editors. Addison-Wesley, Redwood City, CA. 3-51.
    • (1990) 1990 Lectures in Complex Systems , pp. 3-51
    • Doering, C.1
  • 11
    • 0023989329 scopus 로고
    • Unfolding and refolding of a purified precursor protein during import into mitochondria
    • Eilers, M., S. Hwang, and G. Schatz. 1988. Unfolding and refolding of a purified precursor protein during import into mitochondria. EMBO J. 7:1139-1145.
    • (1988) EMBO J , vol.7 , pp. 1139-1145
    • Eilers, M.1    Hwang, S.2    Schatz, G.3
  • 12
    • 0028932523 scopus 로고
    • Characterization of single actin-myosin interactions
    • Finer, J. T., A. D. Mehta, and J. A. Spudich. 1995. Characterization of single actin-myosin interactions. Biophys. J. 68:2915-2975.
    • (1995) Biophys. J. , vol.68 , pp. 2915-2975
    • Finer, J.T.1    Mehta, A.D.2    Spudich, J.A.3
  • 13
    • 0028261701 scopus 로고
    • Single myosin molecule mechanics: Piconewton forces and nanometre steps
    • Finer, J. T., R. M. Simmons, and J. A. Spudich. 1994. Single myosin molecule mechanics: piconewton forces and nanometre steps. Nature. 368:113-119.
    • (1994) Nature , vol.368 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 14
    • 0026059137 scopus 로고
    • Peptidebinding specificity of the molecular chaperone BiP
    • Flynn, G. C., J. Pohl, M. T. Flocco, and J. E. Rothman. 1991. Peptidebinding specificity of the molecular chaperone BiP. Nature. 353: 726-730.
    • (1991) Nature , vol.353 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 15
    • 0027490849 scopus 로고
    • A dual role for mitochondrial heat shock protein 70 in membrane translocation of preproteins
    • Gambill, B. D., W. Voos, P. J. Kang, B. Miao, T. Langer, E. A. Craig, and N. Pfanner. 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, E.A.6    Pfanner, N.7
  • 16
    • 0028834046 scopus 로고
    • Can Hsp70 proteins act as force-generating motors?
    • Click, B. S. 1995. Can Hsp70 proteins act as force-generating motors? Cell. 80:11-14.
    • (1995) Cell , vol.80 , pp. 11-14
    • Click, B.S.1
  • 18
    • 0027332553 scopus 로고
    • 2 to the mitochondrial intermembrane space: The tightly folded heme-binding domain makes import dependent upon matrix ATP
    • 2 to the mitochondrial intermembrane space: the tightly folded heme-binding domain makes import dependent upon matrix ATP. Protein Sci. 2:1901-1917.
    • (1993) Protein Sci , vol.2 , pp. 1901-1917
    • Click, B.S.1    Wachter, C.2    Reid, G.A.3    Schatz, G.4
  • 19
    • 0028085844 scopus 로고
    • Different peptide binding specificities of hsp70 family members
    • Gragerov, A., and M. E. Gottesman. 1994. Different peptide binding specificities of hsp70 family members. J. Mol. Biol. 241:133-135.
    • (1994) J. Mol. Biol. , vol.241 , pp. 133-135
    • Gragerov, A.1    Gottesman, M.E.2
  • 20
    • 0028850872 scopus 로고
    • Effect of nucleotide on the binding of peptides to 70-kDa heat shock protein
    • Greene, L. E., R. Zinner, S. Naficy, and E. Eisenberg. 1995. Effect of nucleotide on the binding of peptides to 70-kDa heat shock protein. J. Biol. Chem. 270:2967-2973.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2967-2973
    • Greene, L.E.1    Zinner, R.2    Naficy, S.3    Eisenberg, E.4
  • 21
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
    • Harrison, C. J., M. Hayer-Hartl, M. Di Liberto, F.-U. Hartl, and J. Kuriyan. 1997. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science, 276: 431-435.
    • (1997) Science , vol.276 , pp. 431-435
    • Harrison, C.J.1    Hayer-Hartl, M.2    Di Liberto, M.3    Hartl, F.-U.4    Kuriyan, J.5
  • 22
    • 0031025479 scopus 로고    scopus 로고
    • What is the driving force for protein import into mitochondria?
    • Horst, M., A. Azem, G. Schatz., and B. S. Glick. 1997. What is the driving force for protein import into mitochondria? Biochim. Biophys. Acta. 1318:71-78.
    • (1997) Biochim. Biophys. Acta. , vol.1318 , pp. 71-78
    • Horst, M.1    Azem, A.2    Schatz, G.3    Glick, B.S.4
  • 23
    • 0029875083 scopus 로고    scopus 로고
    • The mitochondrial protein import motor: Dissociation of mitochondrial hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysis
    • Horst, M., W. Oppliger, B. Feifel, G. Schatz, and B. S. Glick. 1996. The mitochondrial protein import motor: dissociation of mitochondrial hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysis. Protein Sci. 5:759-767.
    • (1996) Protein Sci , vol.5 , pp. 759-767
    • Horst, M.1    Oppliger, W.2    Feifel, B.3    Schatz, G.4    Glick, B.S.5
  • 24
    • 0028145209 scopus 로고
    • The force exerted by single kinesin molecule against a viscous load
    • Hunt, A., F. Gittes, and J. Howard. 1994. The force exerted by single kinesin molecule against a viscous load. Biophys. J. 67:766-781.
    • (1994) Biophys. J. , vol.67 , pp. 766-781
    • Hunt, A.1    Gittes, F.2    Howard, J.3
  • 25
    • 0021676056 scopus 로고
    • The cleavable prepiece of an imported mitochondrial protein is sufficient to direct cytosolic dihydrofolate reductase into the mitochondrial matrix
    • Hurt, E. C., B. Pesold-Hurt, and G. Schatz. 1984. The cleavable prepiece of an imported mitochondrial protein is sufficient to direct cytosolic dihydrofolate reductase into the mitochondrial matrix. FEBS Lett. 178: 306-310.
    • (1984) FEBS Lett , vol.178 , pp. 306-310
    • Hurt, E.C.1    Pesold-Hurt, B.2    Schatz, G.3
  • 26
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • Huxley, A., and R. Simmons. 1971. Proposed mechanism of force generation in striated muscle. Nature. 233:533-538.
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.1    Simmons, R.2
  • 27
    • 0024853819 scopus 로고
    • Translocation of proteins across the mitochondrial inner membrane, but not into the outer membrane, requires nucleoside triphosphates in the matrix
    • Hwang, S. T., and G. Schatz. 1989. Translocation of proteins across the mitochondrial inner membrane, but not into the outer membrane, requires nucleoside triphosphates in the matrix. Proc. Natl. Acad. Sci. USA. 86:8432-8436.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8432-8436
    • Hwang, S.T.1    Schatz, G.2
  • 28
    • 0025833743 scopus 로고
    • Protein import into the yeast mitochondrial matrix. A new translocation intermediate between the two mitochondrial membranes
    • Hwang, S. T., C. Wachter, and G. Schatz. 1991. Protein import into the yeast mitochondrial matrix. A new translocation intermediate between the two mitochondrial membranes. J. Biol. Chem. 266:21083-21089.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21083-21089
    • Hwang, S.T.1    Wachter, C.2    Schatz, G.3
  • 29
    • 0028914392 scopus 로고
    • Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins
    • Jordan, R., and R. McMacken. 1995. Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins. J. Biol. Chem. 270:4563-4569.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4563-4569
    • Jordan, R.1    McMacken, R.2
  • 30
    • 0025039149 scopus 로고
    • Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
    • Kang, P.-J., J. Ostermann, J. Shilling, W. Neupert, E. A. Craig, and N. Pfanner. 1990. Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature. 348:137-143.
    • (1990) Nature , vol.348 , pp. 137-143
    • Kang, P.-J.1    Ostermann, J.2    Shilling, J.3    Neupert, W.4    Craig, E.A.5    Pfanner, N.6
  • 31
    • 15844372190 scopus 로고    scopus 로고
    • A bipartite signaling mechanism involved in DnaJ-mediated activation of Escherichia coli DnaK protein
    • Karzai, A. W., and R. McMacken. 1996. A bipartite signaling mechanism involved in DnaJ-mediated activation of Escherichia coli DnaK protein. J. Biol. Chem. 271:11236-11246.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11236-11246
    • Karzai, A.W.1    McMacken, R.2
  • 32
    • 0028556615 scopus 로고
    • Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane
    • Kronidou, N. G., W. Oppliger, L. Bolliger, K. Hannavy, B. S. Glick, G. Schatz, and M. Horst. 1994. Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane. Proc. Natl. Acad. Sci. USA. 91:12818-12822.
    • (1994) Proc. Natl. Acad. Sci. USA. , vol.91 , pp. 12818-12822
    • Kronidou, N.G.1    Oppliger, W.2    Bolliger, L.3    Hannavy, K.4    Glick, B.S.5    Schatz, G.6    Horst, M.7
  • 33
    • 0028850629 scopus 로고
    • Mitochondrial GrpE modulates the function of matrix Hsp70 in translocation and maturation of preproteins
    • Laloraya, S., P. J. T. Dekker, W. Voos, E. A. Craig, and N. Pfanner. 1995. Mitochondrial GrpE modulates the function of matrix Hsp70 in translocation and maturation of preproteins. Mol. Cell. Biol. 15:7098-7105.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 7098-7105
    • Laloraya, S.1    Dekker, P.J.T.2    Voos, W.3    Craig, E.A.4    Pfanner, N.5
  • 34
    • 0028356858 scopus 로고
    • A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocation
    • Laloraya, S., B. D. Gambill, and E. A. Craig. 1994. A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocation. Proc. Natl. Acad. Sci. USA. 91:6481-6485.
    • (1994) Proc. Natl. Acad. Sci. USA. , vol.91 , pp. 6481-6485
    • Laloraya, S.1    Gambill, B.D.2    Craig, E.A.3
  • 35
    • 0025730978 scopus 로고
    • Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaJ
    • Liberek, K., J. Marszalek, D. Ang, C. Georgopoulos, and M. Zylicz. 1991. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaJ. Proc. Natl. Acad. Sci. USA. 88:2874-2878.
    • (1991) Proc. Natl. Acad. Sci. USA. , vol.88 , pp. 2874-2878
    • Liberek, K.1    Marszalek, J.2    Ang, D.3    Georgopoulos, C.4    Zylicz, M.5
  • 37
    • 0030781431 scopus 로고    scopus 로고
    • Active unfolding of precursor proteins during mitochondrial protein import
    • Matouschek, A., A. Azem, K. Ratliff, B. S. Glick, K. Schmid, and G. Schatz. 1997. Active unfolding of precursor proteins during mitochondrial protein import. EMBO J. 16:6727-6736.
    • (1997) EMBO J , vol.16 , pp. 6727-6736
    • Matouschek, A.1    Azem, A.2    Ratliff, K.3    Glick, B.S.4    Schmid, K.5    Schatz, G.6
  • 39
    • 0028796617 scopus 로고
    • Mitochondrial protein import: Reversible binding of the presequence at the trans side of the outer membrane drives partial translocation and unfolding
    • Mayer, A., W. Neupert, and R. Lill. 1995. Mitochondrial protein import: reversible binding of the presequence at the trans side of the outer membrane drives partial translocation and unfolding. Cell. 80:127-137.
    • (1995) Cell , vol.80 , pp. 127-137
    • Mayer, A.1    Neupert, W.2    Lill, R.3
  • 40
    • 0029013908 scopus 로고
    • The role of ATP in the functional cycle of the DnaK chaperone system
    • McCarty, J. S., A. Buchberger, J. Reinstein, and B. Bukau. 1995. The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol. 249:126-137.
    • (1995) J. Mol. Biol. , vol.249 , pp. 126-137
    • McCarty, J.S.1    Buchberger, A.2    Reinstein, J.3    Bukau, B.4
  • 41
    • 0031556950 scopus 로고    scopus 로고
    • Mgel functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae
    • Miao, B., J. E. Davis, and E. A. Craig. 1997. Mgel functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae. J. Mol. Biol. 265:541-552.
    • (1997) J. Mol. Biol. , vol.265 , pp. 541-552
    • Miao, B.1    Davis, J.E.2    Craig, E.A.3
  • 42
    • 0028275755 scopus 로고
    • Yge1p. a eukaryotic GrpE homolog, is localized in the mitochondrial matrix and interacts with mitochondrial Hsp70
    • Nakai, M., Y. Kato, E. Ikeda, A. Toh-e, and T. Endo. 1994. Yge1p. a eukaryotic GrpE homolog, is localized in the mitochondrial matrix and interacts with mitochondrial Hsp70. Biochem. Biophys. Res. Commun. 200:435-442.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 435-442
    • Nakai, M.1    Kato, Y.2    Ikeda, E.3    Toh-e, A.4    Endo, T.5
  • 43
    • 0025114862 scopus 로고
    • How do polypeptides cross the mitochondrial membranes?
    • Neupert, W., F.-U. Hartl, E. A. Craig, and N. Pfanner. 1990. How do polypeptides cross the mitochondrial membranes? Cell. 63:447-450.
    • (1990) Cell , vol.63 , pp. 447-450
    • Neupert, W.1    Hartl, F.-U.2    Craig, E.A.3    Pfanner, N.4
  • 44
    • 6144254211 scopus 로고    scopus 로고
    • Polymer translocation through a membrane pore
    • Park, P., and W. Sung. 1996. Polymer translocation through a membrane pore. Phys. Rev. Lett. 77:783-786.
    • (1996) Phys. Rev. Lett. , vol.77 , pp. 783-786
    • Park, P.1    Sung, W.2
  • 45
    • 0027194759 scopus 로고
    • Cellular motions and thermal fluctuations: The Brownian ratchet
    • Peskin, C., G. Odell, and G. Oster. 1993. Cellular motions and thermal fluctuations: the Brownian ratchet. Biophys. J. 65:316-324.
    • (1993) Biophys. J. , vol.65 , pp. 316-324
    • Peskin, C.1    Odell, G.2    Oster, G.3
  • 46
    • 0028952024 scopus 로고
    • Coordinated hydrolysis explains the mechanical behavior of kinesin
    • Peskin, C., and G. Oster. 1995. Coordinated hydrolysis explains the mechanical behavior of kinesin. Biophys. J. 68:202S-210S.
    • (1995) Biophys. J. , vol.68
    • Peskin, C.1    Oster, G.2
  • 47
    • 0029240213 scopus 로고
    • Pulling in the proteins
    • Pfanner, N., and M. Meijer. 1995. Pulling in the proteins. Curr. Biol. 5:132-135.
    • (1995) Curr. Biol. , vol.5 , pp. 132-135
    • Pfanner, N.1    Meijer, M.2
  • 49
    • 0024999562 scopus 로고
    • Polypeptides traverse the mitochondrial envelope in an extended state
    • Rassow, J., F.-U. Hartl, B. Guiard, N. Pfanner, and W. Neupert. 1990. Polypeptides traverse the mitochondrial envelope in an extended state. FEBS Lett. 275:190-194.
    • (1990) FEBS Lett , vol.275 , pp. 190-194
    • Rassow, J.1    Hartl, F.-U.2    Guiard, B.3    Pfanner, N.4    Neupert, W.5
  • 50
    • 0028046847 scopus 로고
    • Mitochondrial protein import: Biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44
    • Rassow, J., A. C. Maarse, E. Krainer, M. Kübrich, H. Müller, M. Meijer, E. A. Craig, and N. Pfanner. 1994. Mitochondrial protein import: biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44. J. Cell Biol. 127:1547-1556.
    • (1994) J. Cell Biol. , vol.127 , pp. 1547-1556
    • Rassow, J.1    Maarse, A.C.2    Krainer, E.3    Kübrich, M.4    Müller, H.5    Meijer, M.6    Craig, E.A.7    Pfanner, N.8
  • 51
    • 0028227216 scopus 로고
    • Phylogenetic analysis of the stress-70 protein family
    • Rensing, S. A., and U. G. Maier. 1994. Phylogenetic analysis of the stress-70 protein family. J. Mol. Evol. 39:80-86.
    • (1994) J. Mol. Evol. , vol.39 , pp. 80-86
    • Rensing, S.A.1    Maier, U.G.2
  • 53
    • 0028284879 scopus 로고
    • Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding
    • Rowley, N., C. Prip-Buus, B. Westermann, C. Brown, E. Schwarz, B. Barrell, and W. Neupert. 1994. Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell, 77:249-259.
    • (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
  • 54
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz, G., and B. Dobberstein. 1996. Common principles of protein translocation across membranes. Science. 271:1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 55
    • 0025673942 scopus 로고
    • A precursor protein partly translocated into yeast mitochondria is bound to a 70 kd mitochondrial stress protein
    • Scherer, P. E., U. C. Krieg, S. T. Hwang, D. Vestweber, and G. Schatz. 1990. A precursor protein partly translocated into yeast mitochondria is bound to a 70 kd mitochondrial stress protein. EMBO J. 9:4315-4322.
    • (1990) EMBO J , vol.9 , pp. 4315-4322
    • Scherer, P.E.1    Krieg, U.C.2    Hwang, S.T.3    Vestweber, D.4    Schatz, G.5
  • 56
    • 0022404366 scopus 로고
    • Transport of proteins into mitochondria: Translocational intermediates spanning contact sites between outer and inner membranes
    • Schleyer, M., and W. Neupert. 1985. Transport of proteins into mitochondria: translocational intermediates spanning contact sites between outer and inner membranes. Cell. 43:339-350.
    • (1985) Cell , vol.43 , pp. 339-350
    • Schleyer, M.1    Neupert, W.2
  • 57
    • 0028268243 scopus 로고
    • Kinetics of molecular chaperone action
    • Schmid, D., A. Baici, H. Gehring, and P. Christen. 1994. Kinetics of molecular chaperone action. Science. 263:971-973.
    • (1994) Science , vol.263 , pp. 971-973
    • Schmid, D.1    Baici, A.2    Gehring, H.3    Christen, P.4
  • 59
    • 0029856628 scopus 로고    scopus 로고
    • The nucleotide exchange factor MCE exerts a key function in the ATP-dependent cycle of mt-Hsp70-Tim44 interaction driving mitochondrial protein import
    • Schneider, H.-C., B. Westermann. W. Neupert, and M. Brunner. 1996. The nucleotide exchange factor MCE exerts a key function in the ATP-dependent cycle of mt-Hsp70-Tim44 interaction driving mitochondrial protein import. EMBO J. 15:5796-5803.
    • (1996) EMBO J , vol.15 , pp. 5796-5803
    • Schneider, H.-C.1    Westermann, B.2    Neupert, W.3    Brunner, M.4
  • 62
    • 0028075752 scopus 로고
    • How molecular motors work
    • Spudich, J. A. 1994. How molecular motors work. Nature. 372:515-518.
    • (1994) Nature , vol.372 , pp. 515-518
    • Spudich, J.A.1
  • 63
    • 0027958293 scopus 로고
    • Mitochondrial molecular chaperones: Their role in protein translocation
    • Stuart, R. A., D. M. Cyr, E. A. Craig, and W. Neupert. 1994. Mitochondrial molecular chaperones: their role in protein translocation. Trends Biochem. Sci. 19:87-92.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 87-92
    • Stuart, R.A.1    Cyr, D.M.2    Craig, E.A.3    Neupert, W.4
  • 64
    • 0028362896 scopus 로고
    • Force and velocity measured for single kinesin molecules
    • Svodoba, K., and S. Block. 1994. Force and velocity measured for single kinesin molecules. Cell. 77:773-784.
    • (1994) Cell , vol.77 , pp. 773-784
    • Svodoba, K.1    Block, S.2
  • 65
    • 0028113846 scopus 로고
    • Fluctuation analysis of motor protein movement and single enzyme kinetics
    • Svodoba, K., P. Mitra, and S. Block. 1994. Fluctuation analysis of motor protein movement and single enzyme kinetics. Proc. Natl. Acad. Sci. USA. 91:11782-11786.
    • (1994) Proc. Natl. Acad. Sci. USA. , vol.91 , pp. 11782-11786
    • Svodoba, K.1    Mitra, P.2    Block, S.3
  • 66
    • 0028151509 scopus 로고
    • The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system - DnaK, DnaJ, and GrpE
    • Szabo, A., T. Langer, H. Schröder, J. Flanagan, B. Bukau, and F. U. Hartl. 1994. The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system - DnaK, DnaJ, and GrpE. Proc. Natl. Acad. Sci. USA. 91:10345-10349.
    • (1994) Proc. Natl. Acad. Sci. USA. , vol.91 , pp. 10345-10349
    • Szabo, A.1    Langer, T.2    Schröder, H.3    Flanagan, J.4    Bukau, B.5    Hartl, F.U.6
  • 67
    • 0029670827 scopus 로고    scopus 로고
    • The Δ ψ and Hsp70/MIM44-dependent reaction cycle driving early steps of protein import into mitochondria
    • Ungermann, C., B. Guiard, W. Neupert, and D. M. Cyr. 1996. The Δ ψ and Hsp70/MIM44-dependent reaction cycle driving early steps of protein import into mitochondria. EMBO J. 15:734-744.
    • (1996) EMBO J , vol.15 , pp. 734-744
    • Ungermann, C.1    Guiard, B.2    Neupert, W.3    Cyr, D.M.4
  • 68
    • 0028117097 scopus 로고
    • The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria
    • Ungermann, C., W. Neupert, and D. M. Cyr. 1994. The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria. Science. 266:1250-1253.
    • (1994) Science , vol.266 , pp. 1250-1253
    • Ungermann, C.1    Neupert, W.2    Cyr, D.M.3
  • 69
    • 0027964873 scopus 로고
    • Getting a grip on myosin
    • Vale, R. D. 1994. Getting a grip on myosin. Cell. 78:733-737.
    • (1994) Cell , vol.78 , pp. 733-737
    • Vale, R.D.1
  • 70
    • 0024202929 scopus 로고
    • A chimeric mitochondrial precursor protein with internal disulfide bridges blocks import of authentic precursors into mitochondria and allows quantitation of import sites
    • Vestweber, D., and G. Schatz. 1988a. A chimeric mitochondrial precursor protein with internal disulfide bridges blocks import of authentic precursors into mitochondria and allows quantitation of import sites. J. Cell Biol. 107:2037-2043.
    • (1988) J. Cell Biol. , vol.107 , pp. 2037-2043
    • Vestweber, D.1    Schatz, G.2
  • 71
    • 0024211154 scopus 로고
    • Mitochondria can import artificial precursor proteins containing a branched polypeptide chain or a carboxy-terminal stilbene disulfonate
    • Vestweber, D., and G. Schatz. 1988b. Mitochondria can import artificial precursor proteins containing a branched polypeptide chain or a carboxy-terminal stilbene disulfonate. J. Cell Biol. 107:2045-2049.
    • (1988) J. Cell Biol. , vol.107 , pp. 2045-2049
    • Vestweber, D.1    Schatz, G.2
  • 72
    • 0024536726 scopus 로고
    • DNA-protein conjugates can enter mitochondria via the protein import pathway
    • Vestweber, D., and G. Schatz. 1989. DNA-protein conjugates can enter mitochondria via the protein import pathway. Nature. 338:170-172.
    • (1989) Nature , vol.338 , pp. 170-172
    • Vestweber, D.1    Schatz, G.2
  • 73
    • 0029583409 scopus 로고
    • The mitochondrial protein import machinery. Role of ATP in dissociation of ihe Hsp70-Mim44 complex
    • von Ahnsen, O., W. Voos, H. Henninger, and N. Pfanner. 1995. The mitochondrial protein import machinery. Role of ATP in dissociation of ihe Hsp70-Mim44 complex. J. Biol. Chem. 270:29848-29853.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29848-29853
    • Von Ahnsen, O.1    Voos, W.2    Henninger, H.3    Pfanner, N.4
  • 74
    • 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., B. D. Gambill, B. Guiard, N. Pfanner, and E. A. Craig. 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
  • 76
    • 0028289504 scopus 로고
    • Protein import into mitochondria: The requirement for external ATP is precursor-specific whereas intramitochondrial ATP is universally needed for translocation into the matrix
    • Wachter, C., G. Schatz, and B. S. Glick. 1994. Protein import into mitochondria: the requirement for external ATP is precursor-specific whereas intramitochondrial ATP is universally needed for translocation into the matrix. Mol. Biol. Cell. 5:465-474.
    • (1994) Mol. Biol. Cell. , vol.5 , pp. 465-474
    • Wachter, C.1    Schatz, G.2    Glick, B.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.