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Volumn 15, Issue 4, 1996, Pages 735-744

The ΔΨ- and Hsp70/MIM44-dependent reaction cycle driving early steps of protein import into mitochondria

Author keywords

Membrane potential; MIM44; Mitochondrial protein import; Molecular ratchet model; mtHsp70

Indexed keywords

ADENOSINE TRIPHOSPHATE; HEAT SHOCK PROTEIN 70;

EID: 0029670827     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00409.x     Document Type: Article
Times cited : (91)

References (51)
  • 1
    • 0025303147 scopus 로고
    • Interaction of Hsp70 with newly synthesized proteins: Implication for protein folding and assembly
    • Beckmann, R.P., Mizzen, L.A. and Welch, W.J (1990) Interaction of Hsp70 with newly synthesized proteins: implication for protein folding and assembly. Science, 248, 850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzen, L.A.2    Welch, W.J.3
  • 2
    • 0029070886 scopus 로고
    • The MIM complex mediates preprotein translocation across the mitochondnal inner membrane and couples it to the mt-Hsp70/MIM44 driving system
    • Berthold, J., Bauer, M.F , Schneider, H.C., Klaus, C , Neupert, W. and Brunner, M. (1995) The MIM complex mediates preprotein translocation across the mitochondnal inner membrane and couples it to the mt-Hsp70/MIM44 driving system. Cell, 81, 1085-1094.
    • (1995) Cell , vol.81 , pp. 1085-1094
    • Berthold, J.1    Bauer, M.F.2    Schneider, H.C.3    Klaus, C.4    Neupert, W.5    Brunner, M.6
  • 3
    • 0027484417 scopus 로고
    • Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP
    • Blond-Elguindi, S., Cwirla, S.E., Dower, W.J., Lipshutz, R.J., Sprang, S.R., Sambrook, J.F. and Gething, M.-J.H. (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    Cwirla, S.E.2    Dower, W.J.3    Lipshutz, R.J.4    Sprang, S.R.5    Sambrook, J.F.6    Gething, M.-J.H.7
  • 5
    • 0027102871 scopus 로고
    • YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism
    • Caplan, A.J., Cyr, D.M. and Douglas, M.G. (1992) YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell, 71, 1143-1155
    • (1992) Cell , vol.71 , pp. 1143-1155
    • Caplan, A.J.1    Cyr, D.M.2    Douglas, M.G.3
  • 6
    • 0024298706 scopus 로고
    • 70K heat shock related proteins stimulate protein translocation into microsomes
    • Chirico, W.J., Waters, M.G. and Blobel, G. (1988) 70K heat shock related proteins stimulate protein translocation into microsomes. Nature, 332, 805-809.
    • (1988) Nature , vol.332 , pp. 805-809
    • Chirico, W.J.1    Waters, M.G.2    Blobel, G.3
  • 7
    • 0027515288 scopus 로고
    • A matrix ATP requirement for presequence translocation across the inner membrane of mitochondria
    • Cyr, D.M., Stuart, R.A. and Neupert, W. (1993) A matrix ATP requirement for presequence translocation across the inner membrane of mitochondria. J. Biol. Chem., 268, 23751-23754.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23751-23754
    • Cyr, D.M.1    Stuart, R.A.2    Neupert, W.3
  • 8
    • 0028353336 scopus 로고
    • DnaJ-like proteins: Molecular chaperones and specific regulators of Hsp70
    • Cyr, D.M., Langer, T. and Douglas, M.G. (1994) DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem. Sci., 19, 176-181.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 176-181
    • Cyr, D.M.1    Langer, T.2    Douglas, M.G.3
  • 9
    • 0028817866 scopus 로고
    • Analysis of mitochondrial import pathway in Saccharomyces cerevisiae with translocation intermediates
    • Cyr, D.M., Ungermann, C. and Neupert, W. (1995) Analysis of mitochondrial import pathway in Saccharomyces cerevisiae with translocation intermediates. Methods Enzymol., 260, 241-252.
    • (1995) Methods Enzymol. , vol.260 , pp. 241-252
    • Cyr, D.M.1    Ungermann, C.2    Neupert, W.3
  • 10
    • 0020479807 scopus 로고
    • 2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria
    • 2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. J. Biol. Chem., 257, 13028-13033.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13028-13033
    • Daum, G.1    Böhni, P.C.2    Schatz, G.3
  • 11
    • 0024298711 scopus 로고
    • A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
    • Deshaies, R.J., Koch, B.D., Werner-Washburne, M., Craig, E.A. and Schekman, R. (1988) A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature, 332, 800-805.
    • (1988) Nature , vol.332 , pp. 800-805
    • Deshaies, R.J.1    Koch, B.D.2    Werner-Washburne, M.3    Craig, E.A.4    Schekman, R.5
  • 12
    • 0022515029 scopus 로고
    • Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria
    • Eilers, M. and Schatzm G. (1986) Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria. Nature, 322, 228-232.
    • (1986) Nature , vol.322 , pp. 228-232
    • Eilers, M.1    Schatzm, G.2
  • 13
    • 0026059137 scopus 로고
    • Peptide-binding specifity of the molecular chaperone BiP
    • Flynn, G.C., Pohl, J , Flocco, M.T. and Rothman, J.E. (1991) Peptide-binding specifity 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
  • 14
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman, J., Nimmesgern, E., Ohtsuka, K. and Hartl, F.-U. (1994) Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature, 370, 111-117.
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgern, E.2    Ohtsuka, K.3    Hartl, F.-U.4
  • 15
    • 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, E.A.6    Pfanner, N.7
  • 16
    • 0027333423 scopus 로고
    • Role of the major heat shock proteins as molecular chaperones
    • Georgopoulos, C. and Welch, W.J. (1993) Role of the major heat shock proteins as molecular chaperones Annu. Rev. Cell Biol., 9, 601-634.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 601-634
    • Georgopoulos, C.1    Welch, W.J.2
  • 17
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.-J. and Sambrook, J. (1992) Protein folding in the cell. Nature, 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.-J.1    Sambrook, J.2
  • 18
    • 0028834046 scopus 로고
    • Can Hsp70 proteins act as force-generating motors?
    • Glick, B.S. (1995) Can Hsp70 proteins act as force-generating motors? Cell, 80, 11-14.
    • (1995) Cell , vol.80 , pp. 11-14
    • Glick, B.S.1
  • 19
    • 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
    • Glick, B.S.1    Wachter, C.2    Reid, G.A.3    Schatz, G.4
  • 20
    • 0027418577 scopus 로고
    • A mitochondrial import factor purified from rat liver cytosol is an ATP-dependent conformational modulator for precursor proteins
    • Hachiya, N., Alam, R., Sakasegawa, Y., Sakaguchi, M., Mihara, K. and Omura, T. (1993) A mitochondrial import factor purified from rat liver cytosol is an ATP-dependent conformational modulator for precursor proteins. EMBO J., 12, 1579-1586
    • (1993) EMBO J. , vol.12 , pp. 1579-1586
    • Hachiya, N.1    Alam, R.2    Sakasegawa, Y.3    Sakaguchi, M.4    Mihara, K.5    Omura, T.6
  • 21
    • 0029096887 scopus 로고
    • Reconstitution of the initial steps of mitochondrial protein import
    • Hachiya, N , Mihara, K., Suda, K., Horst, M., Schatz, G. and Lithgow, T. (1995) Reconstitution of the initial steps of mitochondrial protein import. Nature, 376, 705-709.
    • (1995) Nature , vol.376 , pp. 705-709
    • Hachiya, N.1    Mihara, K.2    Suda, K.3    Horst, M.4    Schatz, G.5    Lithgow, T.6
  • 23
    • 0028073776 scopus 로고
    • Mitochondrial Hsp70 a molecular chaperone for proteins encoded by mitochondrial DNA
    • Hermann, J.M., Stuart, R.A., Craig, E.A. and Neupert, W. (1994) Mitochondrial Hsp70 a molecular chaperone for proteins encoded by mitochondrial DNA J. Cell Biol., 127, 893-902.
    • (1994) J. Cell Biol. , vol.127 , pp. 893-902
    • Hermann, J.M.1    Stuart, R.A.2    Craig, E.A.3    Neupert, W.4
  • 24
    • 0025039149 scopus 로고
    • Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
    • Kang, P.J., Ostermann, J., Shilling, J., Neupert, W., Craig, E.A. and Pfanner, N. (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
  • 25
    • 0025606107 scopus 로고
    • Identification of a mitochondrial receptor complex required for recognition and membrane insertion of precursor proteins
    • Kiebler, M., Pfaller, R., Sollner, T., Griffiths, G., Horstmann, H., Pfanner, N. and Neupert, W. (1990) Identification of a mitochondrial receptor complex required for recognition and membrane insertion of precursor proteins Nature, 348, 610-616.
    • (1990) Nature , vol.348 , pp. 610-616
    • Kiebler, M.1    Pfaller, R.2    Sollner, T.3    Griffiths, G.4    Horstmann, H.5    Pfanner, N.6    Neupert, W.7
  • 26
    • 0028556615 scopus 로고
    • Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane
    • Kronidou, N.G., Opplinger, W , Bolliger, L., Hannavy, K., Glick, B.S., Schatz, G. and Horst, M. (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    Opplinger, W.2    Bolliger, L.3    Hannavy, K.4    Glick, B.S.5    Schatz, G.6    Horst, M.7
  • 27
    • 0028356858 scopus 로고
    • A role for a eucaryotic GrpE-related protein, Mge1p, in protein translocation
    • Laloraya, S., Gambill, B.D. and Craig, E.A. (1994) A role for a eucaryotic 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
  • 28
    • 0026596223 scopus 로고
    • Successive action of DnaK (Hsp70), DnaJ and GroEL (Hsp60) along the pathway of chaperone-assisted protein folding
    • Langer, T., Lu, C., Echols, H., Flanagan, J., Hayer-Hartl, M.K. and Hartl, F.-U. (1992) Successive action of DnaK (Hsp70), DnaJ and GroEL (Hsp60) along the pathway of chaperone-assisted protein folding. Nature, 356, 683-689.
    • (1992) Nature , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Hayer-Hartl, M.K.5    Hartl, F.-U.6
  • 29
    • 0026600222 scopus 로고
    • The DnaK chaperone modulates the heat shock response of Escherichia coli by binding to the σ32 transcription factor
    • Liberek, K., Galitsky, T.P., Zylicz, M. and Georgopoulos, C. (1992) The DnaK chaperone modulates the heat shock response of Escherichia coli by binding to the σ32 transcription factor. Proc. Natl Acad Sci. USA, 89, 3516-3520.
    • (1992) Proc. Natl Acad Sci. USA , vol.89 , pp. 3516-3520
    • Liberek, K.1    Galitsky, T.P.2    Zylicz, M.3    Georgopoulos, C.4
  • 30
    • 0028926261 scopus 로고
    • The protein import receptor of mitochondria
    • Lithgow, T., Glick, B.S. and Schatz, G. (1995) The protein import receptor of mitochondria. Trends Biochem. Sci., 20, 98-101.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 98-101
    • Lithgow, T.1    Glick, B.S.2    Schatz, G.3
  • 31
    • 0028268243 scopus 로고
    • Kinetics of molecular chaperone action
    • Schmid, D., Baici, A., Gehring, H. and Christen, P. (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
  • 32
    • 0025114862 scopus 로고
    • How do polypeptides cross mitochondrial membranes?
    • Neupert, W., Hartl, F.-U., Craig, E.A. and Pfanner, N. (1990) How do polypeptides cross 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
  • 33
    • 0026063035 scopus 로고
    • Interaction of hsp70 with unfolded proteins: Effects of temperature and nucleotides on the kinetics of binding
    • Palleros, D.R , Welch, W.J. and Fink, A.L. (1991) Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding. Proc. Natl Acad. Sci. USA, 88, 5719-5723.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 5719-5723
    • Palleros, D.R.1    Welch, W.J.2    Fink, A.L.3
  • 35
    • 0029240213 scopus 로고
    • Protein sorting: Pulling in the proteins
    • Pfanner, N. and Meijer, M. (1995) Protein sorting: pulling in the proteins. Curr. Biol., 5, 132-135.
    • (1995) Curr. Biol. , vol.5 , pp. 132-135
    • Pfanner, N.1    Meijer, M.2
  • 36
    • 0027963264 scopus 로고
    • The protein import machinery of the mitochondrial inner membrane
    • Pfanner, N., Craig, E.A and Meijer, M. (1994) The protein import machinery of the mitochondrial inner membrane. Trends Biochem. Sci., 19, 368-372.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 368-372
    • Pfanner, N.1    Craig, E.A.2    Meijer, M.3
  • 37
    • 0024999562 scopus 로고
    • Polypeptides traverse the mitochondrial envelope in an extended state
    • Rassow, J., Hartl, F.-U., Guiard, B., Pfanner, N. and Neupert, W. (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
  • 38
    • 0028046847 scopus 로고
    • Mitochondrial protein import: Biochemical and genetical evidence for !he interaction of matrix hsp70 and the inner membrane protein MIM44
    • Rassow, J , Maarse, A C., Krainer, E., Kübrich, M., Müller, H., Meijer, M., Craig, E.A. and Pfanner, N. (1994) Mitochondrial protein import: biochemical and genetical evidence for !he 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
  • 39
    • 0022404366 scopus 로고
    • Transport of proteins into mitochondria: Translocational intermediates spanning contact sites between outer and inner membranes
    • Schleyer, M. and Neupert, W. (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
  • 40
    • 0028268243 scopus 로고
    • Kinetics of molecular chaperone action
    • Schmid, D., Baici, A., Gehring, H. and Christen, P. (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
  • 42
    • 0027322148 scopus 로고
    • 2 into the mitochondrial intermembrane space: Specific recognition of the sorting signal
    • 2 into the mitochondrial intermembrane space: specific recognition of the sorting signal. EMBO J., 12, 2295-2302
    • (1993) EMBO J. , vol.12 , pp. 2295-2302
    • Schwarz, E.1    Seytter, T.2    Guiard, B.3    Neupert, W.4
  • 43
    • 0027169533 scopus 로고
    • Eucaryotic DnaJ homologs and the specificity of Hsp70 activity
    • Silver, P.A. and Way, J.C. (1993) Eucaryotic DnaJ homologs and the specificity of Hsp70 activity. Cell, 74, 5-6.
    • (1993) Cell , vol.74 , pp. 5-6
    • Silver, P.A.1    Way, J.C.2
  • 44
    • 0025931801 scopus 로고
    • Analysis of mitochondnal protein import using translocation intermediates and specific antibodies
    • Söllner, T., Rassow, J. and Pfanner, N. (1991) Analysis of mitochondnal protein import using translocation intermediates and specific antibodies. Methods Cell Biol., 34, 345-358.
    • (1991) Methods Cell Biol. , vol.34 , pp. 345-358
    • Söllner, T.1    Rassow, J.2    Pfanner, N.3
  • 45
    • 0026502349 scopus 로고
    • Mapping of the protein import machinery in the mitochondrial outer membrane by crosslinking of translocation intermediates
    • Söllner, T., Rassow, J., Wiedmann, M., Schlossmann, J , Keil, P., Neupert, W and Pfanner, N. (1992) Mapping of the protein import machinery in the mitochondrial outer membrane by crosslinking of translocation intermediates. Nature, 355, 84-87.
    • (1992) Nature , vol.355 , pp. 84-87
    • Söllner, T.1    Rassow, J.2    Wiedmann, M.3    Schlossmann, J.4    Keil, P.5    Neupert, W.6    Pfanner, N.7
  • 46
    • 0027958293 scopus 로고
    • Mitochondrial molecular chaperones: Their role in protein translocation
    • Stuart, R.A., Cyr, D.M., Craig, E.A. and Neupert, W. (1994a) 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
  • 47
    • 0028098073 scopus 로고
    • The requirement of matrix ATP for the import of precursor proteins into the mitochondnal matrix and intermembrane space
    • Stuart, R.A., Gruhler, A., van der Klei, I.J., Guiard, B., Koll, H. and Neupert, W. (1994b) The requirement of matrix ATP for the import of precursor proteins into the mitochondnal matrix and intermembrane space. Eur J. Biochem., 220, 9-18.
    • (1994) Eur J. Biochem. , vol.220 , pp. 9-18
    • Stuart, R.A.1    Gruhler, A.2    Van Der Klei, I.J.3    Guiard, B.4    Koll, H.5    Neupert, W.6
  • 48
    • 0028117097 scopus 로고
    • The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria
    • Ungermann, C., Neupert, W. and Cyr, D.M. (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
  • 49
    • 0020338406 scopus 로고
    • The imported preprotein of the proteolipid subunit of the mitochondrial ATP synthase from Neurospora crassa, Molecular cloning and sequencing of the mRNA
    • Viebrock, A., Perz, A. and Sebald, W (1982) The imported preprotein of the proteolipid subunit of the mitochondrial ATP synthase from Neurospora crassa, Molecular cloning and sequencing of the mRNA. EMBO J., 1, 565-571.
    • (1982) EMBO J. , vol.1 , pp. 565-571
    • Viebrock, A.1    Perz, A.2    Sebald, W.3
  • 50
    • 0027946910 scopus 로고
    • Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria
    • Wagner, I., Arlt, H., Langer, T. and Neupert, W. (1994) Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J., 13, 5135-5145.
    • (1994) EMBO J. , vol.13 , pp. 5135-5145
    • Wagner, I.1    Arlt, H.2    Langer, T.3    Neupert, W.4
  • 51
    • 0029020451 scopus 로고
    • The role of GrpE homologue, Mge1p, in mediating protein import and protein folding in mitochondria
    • Westermann, B., Prip-Buus, C., Neupert, W. and Schwarz, E (1995) The role of GrpE homologue, Mge1p, in mediating protein import and protein folding in mitochondria. EMBO J., 14, 3452-3460.
    • (1995) EMBO J. , vol.14 , pp. 3452-3460
    • Westermann, B.1    Prip-Buus, C.2    Neupert, W.3    Schwarz, E.4


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