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Volumn 30, Issue 2, 1998, Pages 329-340

Genetic and biochemical characterization of mutations affecting the carboxy-terminal domain of the Escherichia coil molecular chaperone DnaJ

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; HEAT SHOCK PROTEIN; LUCIFERASE;

EID: 0031784282     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1998.01067.x     Document Type: Article
Times cited : (41)

References (47)
  • 1
    • 15844404388 scopus 로고    scopus 로고
    • Structure-function analysis of the zinc finger region of the DnaJ molecular chaperone
    • Banecki, B., Liberek, K., Wall, D., Wawrzynów, A., Georgopoulos, C., Bertoli, E., et al. (1996) Structure-function analysis of the zinc finger region of the DnaJ molecular chaperone. J Biol Chem 271: 14840-14848.
    • (1996) J Biol Chem , vol.271 , pp. 14840-14848
    • Banecki, B.1    Liberek, K.2    Wall, D.3    Wawrzynów, A.4    Georgopoulos, C.5    Bertoli, E.6
  • 2
    • 0242634430 scopus 로고
    • A module of the dnaJ heat shock proteins found in malaria parasites
    • Bork, P., Sander, C., Valencia, A., and Bukau, B. (1992) A module of the dnaJ heat shock proteins found in malaria parasites. Trends Biochem Sci 17: 129.
    • (1992) Trends Biochem Sci , vol.17 , pp. 129
    • Bork, P.1    Sander, C.2    Valencia, A.3    Bukau, B.4
  • 3
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau, B., and Horwich, A.L. (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92: 351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 4
    • 0028061311 scopus 로고
    • Heat shock proteins and molecular chaperones: Mediators of protein conformation and turnover in the cell
    • Craig, E.A., Weissman, J.S., and Norwich, A.L. (1994) Heat shock proteins and molecular chaperones: mediators of protein conformation and turnover in the cell. Cell 78: 365-372.
    • (1994) Cell , vol.78 , pp. 365-372
    • Craig, E.A.1    Weissman, J.S.2    Norwich, A.L.3
  • 5
    • 0029793330 scopus 로고    scopus 로고
    • Purification and biochemical properties of Saccharomyces cerevisiae's Mge1p, the mitochondrial cochaperone of Ssc1p
    • Deloche, O., and Georgopoulos, C. (1996) Purification and biochemical properties of Saccharomyces cerevisiae's Mge1p, the mitochondrial cochaperone of Ssc1p. J Biol Chem 271: 23960-23966.
    • (1996) J Biol Chem , vol.271 , pp. 23960-23966
    • Deloche, O.1    Georgopoulos, C.2
  • 7
    • 0005403121 scopus 로고
    • Escherichia coli mutants blocked in lambda DNA synthesis
    • Hershey, A.D. (ed.). Cold Spring Harbor, NY: Cold Spring Harbor Press
    • Georgopoulos, C., and Herskowitz, I. (1971) Escherichia coli mutants blocked in lambda DNA synthesis. In The Bacteriophage Lambda. Hershey, A.D. (ed.). Cold Spring Harbor, NY: Cold Spring Harbor Press, pp. 553-564.
    • (1971) The Bacteriophage Lambda , pp. 553-564
    • Georgopoulos, C.1    Herskowitz, I.2
  • 8
    • 0026483711 scopus 로고
    • Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli
    • Gragerov, A., Nudler, E., Komissarova, N., Gaitanaris, G.A., Gottesman, M.E., and Nikiforov, V. (1992) Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli. Proc Natl Acad Sci USA 89: 10341-10344.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10341-10344
    • Gragerov, A.1    Nudler, E.2    Komissarova, N.3    Gaitanaris, G.A.4    Gottesman, M.E.5    Nikiforov, V.6
  • 9
    • 0001241680 scopus 로고    scopus 로고
    • Function and regulation of the heat shock proteins
    • Neidhardt, F.C., Curtiss R. III, Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., et al. (eds). Washington DC: American Society for Microbiology Press
    • Gross, C.A. (1996) Function and regulation of the heat shock proteins. In Escherichia coli and Salmonella. Neidhardt, F.C., Curtiss R. III, Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., et al. (eds). Washington DC: American Society for Microbiology Press, pp. 1382-1399.
    • (1996) Escherichia Coli and Salmonella , pp. 1382-1399
    • Gross, C.A.1
  • 10
    • 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., Hayer-Hartl, M., Di Liberto, M., Hartl, F.-U., and Kuriyan, J. (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
  • 11
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.-U. (1996) Molecular chaperones in cellular protein folding. Nature 381: 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.-U.1
  • 12
    • 0027425585 scopus 로고
    • Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides
    • Hendrick, J.P., Langer, T., Davis, T.A., Hartl, F.-U., and Wiedman, M. (1993) Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides. Proc Natl Acad Sci USA 90: 10216-10220.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10216-10220
    • Hendrick, J.P.1    Langer, T.2    Davis, T.A.3    Hartl, F.-U.4    Wiedman, M.5
  • 13
    • 15844372190 scopus 로고    scopus 로고
    • A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein
    • Karzai, A.W., and McMacken, R. (1996) A bipartite signaling mechanism involved in DnaJ-mediated activation of the 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
  • 14
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A., Roberts, J.D., and Zakour, R.A. (1987) Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol 154: 367-383.
    • (1987) Methods Enzymol , vol.154 , pp. 367-383
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0026596223 scopus 로고
    • Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
    • Langer, T., Lu, C., Echols, H., Flanagan, J., Hayer, M.K., and Hartl, F.-U. (1992) Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated 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, M.K.5    Hartl, F.-U.6
  • 17
    • 0027504094 scopus 로고
    • Autoregulation of the Escherichia coli heat shock response by the DnaK and DnaJ heat shock proteins
    • Liberek, K., and Georgopoulos, C. (1993) Autoregulation of the Escherichia coli heat shock response by the DnaK and DnaJ heat shock proteins. Proc Natl Acad Sci USA 90: 11019-11023.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11019-11023
    • Liberek, K.1    Georgopoulos, C.2
  • 18
    • 0025730978 scopus 로고
    • E. coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
    • Liberek, K., Marszalek, J., Ang, D., Georgopoulos, C., and Zylicz, M. (1991) E. coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. 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
  • 20
    • 0024151897 scopus 로고
    • The heat-shock proteins
    • Lindquist, S., and Craig, E.A. (1988) The heat-shock proteins. Annu Rev Genet 22: 631-677.
    • (1988) Annu Rev Genet , vol.22 , pp. 631-677
    • Lindquist, S.1    Craig, E.A.2
  • 21
    • 0032489556 scopus 로고    scopus 로고
    • The conserved carboxyl terminus and zinc finger-like domain of the co-chaperone Ydj1 assist Hsp70 in protein folding
    • Lu, Z., and Cyr, D.M. (1998) The conserved carboxyl terminus and zinc finger-like domain of the co-chaperone Ydj1 assist Hsp70 in protein folding. J Biol Chem 273: 5970-5978.
    • (1998) J Biol Chem , vol.273 , pp. 5970-5978
    • Lu, Z.1    Cyr, D.M.2
  • 22
    • 0024555841 scopus 로고
    • Reconstitution of a nine-protein system that initiates bacteriophage λ DNA replication
    • Mensa-Wilmot, K., Seaby, R., Atfano, C., Wold, M.S., Gomes, B., and McMacken, R. (1989) Reconstitution of a nine-protein system that initiates bacteriophage λ DNA replication. J Biol Chem 264: 2853-2861.
    • (1989) J Biol Chem , vol.264 , pp. 2853-2861
    • Mensa-Wilmot, K.1    Seaby, R.2    Atfano, C.3    Wold, M.S.4    Gomes, B.5    McMacken, R.6
  • 23
    • 0030462757 scopus 로고    scopus 로고
    • Identification and characterization of HslV HslU (ClpQ ClpY) proteins in Escherichia coli
    • Missiakas, D., Schwager, F., Betton, J.M., Georgopoulos, C., and Raina, S. (1996) Identification and characterization of HslV HslU (ClpQ ClpY) proteins in Escherichia coli. EMBO J 15: 6899-6909.
    • (1996) EMBO J , vol.15 , pp. 6899-6909
    • Missiakas, D.1    Schwager, F.2    Betton, J.M.3    Georgopoulos, C.4    Raina, S.5
  • 24
    • 0027537708 scopus 로고
    • Initiation of λ DNA replication: The Escherichia coli small heat-shock proteins, DnaJ and GrpE, increase DnaK's affinity for the λP protein
    • Osipiuk, J., Georgopoulos, C., and Zylicz, M. (1993) Initiation of λ DNA replication: the Escherichia coli small heat-shock proteins, DnaJ and GrpE, increase DnaK's affinity for the λP protein. J Biol Chem 268: 4821-4827.
    • (1993) J Biol Chem , vol.268 , pp. 4821-4827
    • Osipiuk, J.1    Georgopoulos, C.2    Zylicz, M.3
  • 25
    • 0030581175 scopus 로고    scopus 로고
    • NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone
    • Pellacchia, M., Szyperski, T., Wall, D., Georgopoulos, C., and Wüthrich, K. (1996) NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone. J Mol Biol 260: 236-250.
    • (1996) J Mol Biol , vol.260 , pp. 236-250
    • Pellacchia, M.1    Szyperski, T.2    Wall, D.3    Georgopoulos, C.4    Wüthrich, K.5
  • 26
    • 0030581148 scopus 로고    scopus 로고
    • Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain
    • Qian, Y.Q., Patel, D., Hartl, F.-U., and McColl, D.J. (1996) Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain. J Mol Biol 260: 224-235.
    • (1996) J Mol Biol , vol.260 , pp. 224-235
    • Qian, Y.Q.1    Patel, D.2    Hartl, F.-U.3    McColl, D.J.4
  • 27
    • 0031106824 scopus 로고    scopus 로고
    • Molecular chaperones: Towards a characterization of the heat-shock protein 70 family
    • Rassow, J., von Ahsen, O., Bömer, U., and Pfanner, N. (1997) Molecular chaperones: towards a characterization of the heat-shock protein 70 family. Trends Cell Biol 7: 129-133.
    • (1997) Trends Cell Biol , vol.7 , pp. 129-133
    • Rassow, J.1    Von Ahsen, O.2    Bömer, U.3    Pfanner, N.4
  • 28
    • 0017395649 scopus 로고
    • Initiation of the DNA replication of bacteriophage lambda in Escherichia coli K12
    • Saito, H., and Uchida, H. (1977) Initiation of the DNA replication of bacteriophage lambda in Escherichia coli K12. J Mol Biol 113: 1-25.
    • (1977) J Mol Biol , vol.113 , pp. 1-25
    • Saito, H.1    Uchida, H.2
  • 29
    • 0027427986 scopus 로고
    • DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage
    • Schröder, H., Langer, T., Hartl, F.-U., and Bukau, B. (1993) DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J 12: 4137-4144.
    • (1993) EMBO J , vol.12 , pp. 4137-4144
    • Schröder, H.1    Langer, T.2    Hartl, F.-U.3    Bukau, B.4
  • 30
    • 0025164669 scopus 로고
    • The isolation and characterization of dnaJ null mutants of Escherichia coli
    • Sell, S.M., Eisen, C., Ang, D., Zylicz, M., and Georgopoulos, C. (1990) The isolation and characterization of dnaJ null mutants of Escherichia coli. J Bacteriol 172: 4827-4835.
    • (1990) J Bacteriol , vol.172 , pp. 4827-4835
    • Sell, S.M.1    Eisen, C.2    Ang, D.3    Zylicz, M.4    Georgopoulos, C.5
  • 31
    • 0026707466 scopus 로고
    • DnaK, DnaJ, and GrpE are required for flagellum synthesis in Escherichia coli
    • Shi, W., Zhou, Y., Wild, J., Adler, J., and Gross, C.A. (1992) DnaK, DnaJ, and GrpE are required for flagellum synthesis in Escherichia coli. J Bacteriol 174: 6256-6263.
    • (1992) J Bacteriol , vol.174 , pp. 6256-6263
    • Shi, W.1    Zhou, Y.2    Wild, J.3    Adler, J.4    Gross, C.A.5
  • 32
    • 0027169533 scopus 로고
    • Eukaryotic DnaJ homologs and the specificity of Hsp70 activity
    • Silver, P.A., and Way, J.C. (1993) Eukaryotic 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
  • 34
    • 0017359310 scopus 로고
    • A new host gene (groPC) necessary for lambda DNA replication
    • Sunshine, M., Feiss, M., Stuart, J., and Yochem, J. (1977) A new host gene (groPC) necessary for lambda DNA replication. Mol Gen Genet 151: 27-34.
    • (1977) Mol Gen Genet , vol.151 , pp. 27-34
    • Sunshine, M.1    Feiss, M.2    Stuart, J.3    Yochem, J.4
  • 35
    • 0028151509 scopus 로고
    • The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system-DnaK, DnaJ, and GrpE
    • Szabo, A., Langer, T., Schröder, H., Flanagan, J., Bukau, B., and Hartl, F.-U. (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
  • 36
    • 0030030946 scopus 로고    scopus 로고
    • A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrate
    • Szabo, A., Korszun, R., Hartl, F.-U., and Flanagan, J. (1996) A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrate. EMBO J 15: 408-417.
    • (1996) EMBO J , vol.15 , pp. 408-417
    • Szabo, A.1    Korszun, R.2    Hartl, F.-U.3    Flanagan, J.4
  • 37
    • 0027987996 scopus 로고
    • NMR structure determination of the Escherichia coli DnaJ molecular chaperone: Secondary structure and backbone fold of the N-terminal region (residues 2-108), containing the highly conserved J-domain
    • Szyperski, T., Pellacchia, M., Wall, D., Georgopoulos, C., and Wüthrich, K. (1994) NMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108), containing the highly conserved J-domain. Proc Natl Acad Sci USA 91: 11343-11347.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11343-11347
    • Szyperski, T.1    Pellacchia, M.2    Wall, D.3    Georgopoulos, C.4    Wüthrich, K.5
  • 38
    • 0029034167 scopus 로고
    • A study of the double mutation of dnaJ and cbpA, whose gene products function as molecular chaperones in Escherichia coli
    • Ueguchi, C., Shiozawa, T., Kakeda, M., Yamada, H., and Mizuno, T. (1995) A study of the double mutation of dnaJ and cbpA, whose gene products function as molecular chaperones in Escherichia coli. J Bacteriol 177: 3894-3896.
    • (1995) J Bacteriol , vol.177 , pp. 3894-3896
    • Ueguchi, C.1    Shiozawa, T.2    Kakeda, M.3    Yamada, H.4    Mizuno, T.5
  • 39
    • 0028170215 scopus 로고
    • 2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for X replication
    • 2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for X replication. J Biol Chem 269: 5446-5451.
    • (1994) J Biol Chem , vol.269 , pp. 5446-5451
    • Wall, D.1    Zylicz, M.2    Georgopoulos, C.3
  • 40
    • 0028930540 scopus 로고
    • The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone
    • Wall, D., Zylicz, M., and Georgopoulos, C. (1995) The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone. J Biol Chem 270: 2139-2144.
    • (1995) J Biol Chem , vol.270 , pp. 2139-2144
    • Wall, D.1    Zylicz, M.2    Georgopoulos, C.3
  • 41
    • 0029094250 scopus 로고
    • Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates
    • Wawrzynów, A., and Zylicz, M. (1995) Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates. J Biol Chem 270: 19300-19306.
    • (1995) J Biol Chem , vol.270 , pp. 19300-19306
    • Wawrzynów, A.1    Zylicz, M.2
  • 42
    • 0029860683 scopus 로고    scopus 로고
    • Role of the mitochondrial DnaJ homolog Mdjlp as a chaperone for mitochondrially synthesized and imported proteins
    • Westermann, B., Gaume, B., Herrmann, J.M., Neupert, W., and Schwarz, E. (1996) Role of the mitochondrial DnaJ homolog Mdjlp as a chaperone for mitochondrially synthesized and imported proteins. Mol Cell Biol 16: 7063-7071.
    • (1996) Mol Cell Biol , vol.16 , pp. 7063-7071
    • Westermann, B.1    Gaume, B.2    Herrmann, J.M.3    Neupert, W.4    Schwarz, E.5
  • 43
    • 0026454375 scopus 로고
    • DnaJ, DnaK, and GrpE heat shock proteins are required in oriP1 DNA replication solely at the RepA monomerization step
    • Wickner, S., Skowyra, D., Hoskins, J., and McKenney, K. (1992) DnaJ, DnaK, and GrpE heat shock proteins are required in oriP1 DNA replication solely at the RepA monomerization step. Proc Natl Acad Sci USA 89: 10345-10349.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10345-10349
    • Wickner, S.1    Skowyra, D.2    Hoskins, J.3    McKenney, K.4
  • 44
    • 0029893301 scopus 로고    scopus 로고
    • Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli
    • Wild, J., Rossmeissl, P., Walter, W.A., and Gross, C.A. (1996) Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli. J Bacteriol 178: 3608-3613.
    • (1996) J Bacteriol , vol.178 , pp. 3608-3613
    • Wild, J.1    Rossmeissl, P.2    Walter, W.A.3    Gross, C.A.4
  • 45
    • 0027385183 scopus 로고
    • Regulation of the heat-shock response in bacteria
    • Yura, T., Nagai, H., and Mori, H. (1993) Regulation of the heat-shock response in bacteria. Annu Rev Microbiol 47: 321-350.
    • (1993) Annu Rev Microbiol , vol.47 , pp. 321-350
    • Yura, T.1    Nagai, H.2    Mori, H.3
  • 46
    • 0024316732 scopus 로고
    • Initiation of λ DNA replication with purified host- and bacteriophage-encoded proteins: The role of the dnaK, dnaJ and grpE heat shock proteins
    • Zylicz, M., Ang, D., Liberek, K., and Georgopoulos, C. (1989) Initiation of λ DNA replication with purified host-and bacteriophage-encoded proteins: the role of the dnaK, dnaJ and grpE heat shock proteins, EMBO J 8: 1601-1608.
    • (1989) EMBO J , vol.8 , pp. 1601-1608
    • Zylicz, M.1    Ang, D.2    Liberek, K.3    Georgopoulos, C.4
  • 47
    • 0021880465 scopus 로고
    • Purification and properties of the dnaJ replication protein of Escherichia coli
    • Zylicz, M., Yamamoto, T., McKittrick, N., Sell, S., and Georgopoulos, C. (1985) Purification and properties of the dnaJ replication protein of Escherichia coli. J Biol Chem 260: 7591-7598.
    • (1985) J Biol Chem , vol.260 , pp. 7591-7598
    • Zylicz, M.1    Yamamoto, T.2    McKittrick, N.3    Sell, S.4    Georgopoulos, C.5


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