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Volumn 252, Issue 1, 1998, Pages 45-50

Kinetics and specificity of reductive acylation of wild-type and mutated lipoyl domains of 2-oxo-acid dehydrogenase complexes from Azotobacter vinelandii

Author keywords

Azotobacter vinelandii; Lipoyl domain; Multienzyme complex; Mutagenesis; Recognition

Indexed keywords

2 OXOACID DEHYDROGENASE; BACTERIAL ENZYME; COENZYME A; MUTANT PROTEIN; OXOGLUTARATE DEHYDROGENASE; PYRUVATE DEHYDROGENASE COMPLEX;

EID: 0032519817     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2520045.x     Document Type: Article
Times cited : (44)

References (44)
  • 1
    • 0019201384 scopus 로고
    • Elementary steps in the reaction mechanism of the pyruvate dehydrogenase complex from Escherichia coli: Kinetics of acetylation and deacetylation
    • Akiyama, S. K. & Hammes, G. G. (1980) Elementary steps in the reaction mechanism of the pyruvate dehydrogenase complex from Escherichia coli: kinetics of acetylation and deacetylation. Biochemistry 19, 4208-4213.
    • (1980) Biochemistry , vol.19 , pp. 4208-4213
    • Akiyama, S.K.1    Hammes, G.G.2
  • 3
    • 0017403869 scopus 로고
    • Self-assembly and catalytic activity of the pyruvate dehydrogenase multienzyme complex of Escherichia coli
    • Bates, D. L., Danson, M. J., Hale, G., Hooper, E. A. & Perham, R. N. (1977) Self-assembly and catalytic activity of the pyruvate dehydrogenase multienzyme complex of Escherichia coli, Nature 268, 313-316.
    • (1977) Nature , vol.268 , pp. 313-316
    • Bates, D.L.1    Danson, M.J.2    Hale, G.3    Hooper, E.A.4    Perham, R.N.5
  • 4
    • 0028175871 scopus 로고
    • 15N nuclear magnetic resonance assignments and secondary structure of the N-terminal lipoyl domain of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii
    • 15N nuclear magnetic resonance assignments and secondary structure of the N-terminal lipoyl domain of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii, Eur. J. Biochem. 221, 87-100.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 87-100
    • Berg, A.1    De Kok, A.2    Vervoort, J.3
  • 5
    • 0028973108 scopus 로고
    • 15N nuclear magnetic resonance assignments and secondary structure of the lipoyl domain of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. Evidence for high structural similarity with the lipoyl domain of the pyruvate dehydrogenase complex
    • 15N nuclear magnetic resonance assignments and secondary structure of the lipoyl domain of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. Evidence for high structural similarity with the lipoyl domain of the pyruvate dehydrogenase complex, Eur. J. Biochem. 234, 148-159.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 148-159
    • Berg, A.1    Smits, O.2    De Kok, A.3    Vervoort, J.4
  • 6
    • 0030598920 scopus 로고    scopus 로고
    • Solution structure of the lipoyl domain of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii
    • Berg, A., Vervoort, J. & de Kok, A. (1996) Solution structure of the lipoyl domain of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii, J. Mol. Biol. 261, 432-442.
    • (1996) J. Mol. Biol. , vol.261 , pp. 432-442
    • Berg, A.1    Vervoort, J.2    De Kok, A.3
  • 7
    • 0031053675 scopus 로고    scopus 로고
    • Three-dimensional structure in solution of the N-terminal lipoyl domain of the pyruvate dehydrogenase complex from Azotobacter vinelandii
    • Berg, A., Vervoort, J. & de Kok, A. (1997a) Three-dimensional structure in solution of the N-terminal lipoyl domain of the pyruvate dehydrogenase complex from Azotobacter vinelandii, Eur. J. Biochem. 244, 352-360.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 352-360
    • Berg, A.1    Vervoort, J.2    De Kok, A.3
  • 8
    • 0030789108 scopus 로고    scopus 로고
    • 2-Oxo acid dehydrogenase multienzyme complexes. The central role of the lipoyl domain
    • Berg, A. & de Kok, A. (1997b) 2-Oxo acid dehydrogenase multienzyme complexes. The central role of the lipoyl domain, Biol. Chem. Hoppe-Seyler 378, 617-634.
    • (1997) Biol. Chem. Hoppe-Seyler , vol.378 , pp. 617-634
    • Berg, A.1    De Kok, A.2
  • 10
    • 0021475003 scopus 로고
    • The composition of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Does a unifying model exist for the complexes from gram-negative bacteria?
    • Bosma, H. J., de Kok, A., Westphal, A. H. & Veeger, C. (1984) The composition of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Does a unifying model exist for the complexes from gram-negative bacteria? Eur. J. Biochem. 142, 541-549.
    • (1984) Eur. J. Biochem. , vol.142 , pp. 541-549
    • Bosma, H.J.1    De Kok, A.2    Westphal, A.H.3    Veeger, C.4
  • 11
    • 0016707585 scopus 로고
    • The pyruvate dehydrogenase complex from Azotobacter vinelandii. 2. Regulation of the activity
    • Bresters, T. W., de Kok, A. & Veeger, C. (1975) The pyruvate dehydrogenase complex from Azotobacter vinelandii. 2. Regulation of the activity, Eur. J. Biochem. 59, 347-353.
    • (1975) Eur. J. Biochem. , vol.59 , pp. 347-353
    • Bresters, T.W.1    De Kok, A.2    Veeger, C.3
  • 12
    • 0011386550 scopus 로고
    • Acyl group and electron pair relay system: A network of interacting lipoyl moieties in the pyruvate and α-ketoglutarate dehydrogenase complexes from Escherichia coli
    • Collins, J. H. & Reed, L. J. (1977) Acyl group and electron pair relay system: a network of interacting lipoyl moieties in the pyruvate and α-ketoglutarate dehydrogenase complexes from Escherichia coli, Proc. Natl Acad. Sci. USA 74, 4223-4227.
    • (1977) Proc. Natl Acad. Sci. USA , vol.74 , pp. 4223-4227
    • Collins, J.H.1    Reed, L.J.2
  • 13
    • 0004257138 scopus 로고
    • Rapid intramolecular coupling of active sites in the pyruvate dehydrogenase complex of Escherichia coli: Mechanism for rate enhancement in a multimeric structure
    • Danson, M. J., Fersht, A. R. & Perham, R. N. (1978) Rapid intramolecular coupling of active sites in the pyruvate dehydrogenase complex of Escherichia coli: mechanism for rate enhancement in a multimeric structure, Proc. Natl Acad. Sci. USA 75, 5386-5390.
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 5386-5390
    • Danson, M.J.1    Fersht, A.R.2    Perham, R.N.3
  • 14
    • 0027340272 scopus 로고
    • Three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzuyme complex
    • Dardel, F., Davis, A. L., Laue, E. D. & Perham, R. N. (1993) Three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzuyme complex, J. Mol. Biol. 229, 1037-1048.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1037-1048
    • Dardel, F.1    Davis, A.L.2    Laue, E.D.3    Perham, R.N.4
  • 15
    • 0017719163 scopus 로고
    • Determination of the chain stoichiometries from the number of reactive sulfhydryl groups in the pyruvate dehydrogenase complexes of Azotobacter vinelandii and Escherichia coli
    • De Abreu, R. A., de Kok, A., de Graaf-Hess, A. C. & Veeger, C. (1977) Determination of the chain stoichiometries from the number of reactive sulfhydryl groups in the pyruvate dehydrogenase complexes of Azotobacter vinelandii and Escherichia coli, Eur. J. Biochem. 81, 357-364.
    • (1977) Eur. J. Biochem. , vol.81 , pp. 357-364
    • De Abreu, R.A.1    De Kok, A.2    De Graaf-Hess, A.C.3    Veeger, C.4
  • 16
    • 0022211469 scopus 로고
    • Hybrid pyruvate dehydrogenase complexes reconstituted from components of the complexes from Eschericha coli and Azotobacter vinehtndii
    • de Kok, A. & Westphal, A. H. (1985) Hybrid pyruvate dehydrogenase complexes reconstituted from components of the complexes from Eschericha coli and Azotobacter vinehtndii, Eur. J. Biochem. 152, 35-41.
    • (1985) Eur. J. Biochem. , vol.152 , pp. 35-41
    • De Kok, A.1    Westphal, A.H.2
  • 17
    • 77049162117 scopus 로고
    • A micro biuret method for protein determination: Determination of total protein in cerebrospinal fluid
    • Goa. J. (1953) A micro biuret method for protein determination: determination of total protein in cerebrospinal fluid, Scand. J. Clin. Lab. Invest. 5, 218-222.
    • (1953) Scand. J. Clin. Lab. Invest. , vol.5 , pp. 218-222
    • Goa, J.1
  • 18
    • 0024560461 scopus 로고
    • Kinetics and specificity of reductive acylation of lipoyl domains from 2-oxo acid dehydrogenase multienzyme complexes
    • Graham, L. D., Packman, L. C. & Perham, R. N. (1989) Kinetics and specificity of reductive acylation of lipoyl domains from 2-oxo acid dehydrogenase multienzyme complexes, Biochemistry 28, 1574-1581.
    • (1989) Biochemistry , vol.28 , pp. 1574-1581
    • Graham, L.D.1    Packman, L.C.2    Perham, R.N.3
  • 19
    • 0025252199 scopus 로고
    • Interactions of lipoyl domains with the E1p subunits of the pyruvate dehydrogenase multienzyme complex from Escherichia coli
    • Graham, L. D. & Perham, R. N. (1990) Interactions of lipoyl domains with the E1p subunits of the pyruvate dehydrogenase multienzyme complex from Escherichia coli, FEBS Lett. 262, 241-244.
    • (1990) FEBS Lett. , vol.262 , pp. 241-244
    • Graham, L.D.1    Perham, R.N.2
  • 20
    • 0029071184 scopus 로고
    • Three-dimensional structure of a lipoyl domain from dihydrolipoyl acetyltransferase component of the pyruvate dehydrogenase multienzyme complex of Escherichia coli
    • Green, J. D. F., Laue, E. D., Perham, R. N., Ali, S. T. & Guest, J. R. (1995) Three-dimensional structure of a lipoyl domain from dihydrolipoyl acetyltransferase component of the pyruvate dehydrogenase multienzyme complex of Escherichia coli, J. Mol. Biol. 248, 328-343.
    • (1995) J. Mol. Biol. , vol.248 , pp. 328-343
    • Green, J.D.F.1    Laue, E.D.2    Perham, R.N.3    Ali, S.T.4    Guest, J.R.5
  • 21
    • 6844222403 scopus 로고
    • The structure of acetyldihydrolipoic acid
    • Hale, G. & Dixon, H. B. F. (1981) The structure of acetyldihydrolipoic acid, Biochem. J. 193, 1034-1035.
    • (1981) Biochem. J. , vol.193 , pp. 1034-1035
    • Hale, G.1    Dixon, H.B.F.2
  • 22
    • 0023461081 scopus 로고
    • The domain structure of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii
    • Hanemaaijer, R., de Kok, A., Jolles, J. & Veeger, C. (1987) The domain structure of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii, Eur. J. Biochem. 169, 245-252.
    • (1987) Eur. J. Biochem. , vol.169 , pp. 245-252
    • Hanemaaijer, R.1    De Kok, A.2    Jolles, J.3    Veeger, C.4
  • 23
    • 0023772112 scopus 로고
    • The dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Molecular cloning and sequence analysis
    • Hanemaaijer, R., Janssen, A., de Kok, A. & Veeger, C. (1988) The dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Molecular cloning and sequence analysis, Eur. J. Biochem. 172, 593-599.
    • (1988) Eur. J. Biochem. , vol.172 , pp. 593-599
    • Hanemaaijer, R.1    Janssen, A.2    De Kok, A.3    Veeger, C.4
  • 24
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 25
    • 0025643362 scopus 로고
    • A general method for rapid site-directed mutagenesis using the polymerase chain reaction
    • Landt, O., Grunert, H. P. & Hahn, U. (1990) A general method for rapid site-directed mutagenesis using the polymerase chain reaction. Gene 96, 125-128.
    • (1990) Gene , vol.96 , pp. 125-128
    • Landt, O.1    Grunert, H.P.2    Hahn, U.3
  • 27
    • 0026510711 scopus 로고
    • Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex
    • Mattevi, A., Obmolova, G., Schulze, E., Kalk, K. H., Westphal, A. H., de Kok, A. & Hol, W. G. J. (1992b) Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex, Science 255, 1544-1550.
    • (1992) Science , vol.255 , pp. 1544-1550
    • Mattevi, A.1    Obmolova, G.2    Schulze, E.3    Kalk, K.H.4    Westphal, A.H.5    De Kok, A.6    Hol, W.G.J.7
  • 28
    • 0023813683 scopus 로고
    • Investigation of the mechanism of active site coupling in the pyruvate dehydrogenase multienzyme complex of Escherichia coli by protein engineering
    • Miles, J. S., Guest, J. R., Radford, S. E. & Perham, R. N. (1988) Investigation of the mechanism of active site coupling in the pyruvate dehydrogenase multienzyme complex of Escherichia coli by protein engineering, J. Mol. Biol. 202, 97-106.
    • (1988) J. Mol. Biol. , vol.202 , pp. 97-106
    • Miles, J.S.1    Guest, J.R.2    Radford, S.E.3    Perham, R.N.4
  • 29
    • 0021444159 scopus 로고
    • Repeating functional domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli
    • Packman, L. C., Hale, G. & Perham, R. N. (1984a) Repeating functional domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli, EMBO J. 3, 1315-1319.
    • (1984) EMBO J. , vol.3 , pp. 1315-1319
    • Packman, L.C.1    Hale, G.2    Perham, R.N.3
  • 30
    • 0021303989 scopus 로고
    • 1H-n.m.r. spectroscopy of the pyruvate dehydrogenase complex of Bacillus stearothermophilus
    • 1H-n.m.r. spectroscopy of the pyruvate dehydrogenase complex of Bacillus stearothermophilus, Biohem. J. 217, 219-227.
    • (1984) Biohem. J. , vol.217 , pp. 219-227
    • Packman, L.C.1    Perham, R.N.2    Roberts, G.C.K.3
  • 31
    • 0026079562 scopus 로고
    • Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: A paradigm in the design of a multifunctional protein
    • Perham, R. N. (1991) Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: a paradigm in the design of a multifunctional protein, Biochemistry 30, 8501-8512.
    • (1991) Biochemistry , vol.30 , pp. 8501-8512
    • Perham, R.N.1
  • 32
    • 0024346166 scopus 로고
    • Antibodies against an inter-domain segment of polypeptide chain inhibit active-site coupling in the pyruvate dehydrogenase multienzyme complex
    • Radford, S. E., Perham, R. N., Ullrich, S. J. & Appella, E. (1989) Antibodies against an inter-domain segment of polypeptide chain inhibit active-site coupling in the pyruvate dehydrogenase multienzyme complex, FEBS Lett. 250, 336-340.
    • (1989) FEBS Lett. , vol.250 , pp. 336-340
    • Radford, S.E.1    Perham, R.N.2    Ullrich, S.J.3    Appella, E.4
  • 33
    • 2642644904 scopus 로고
    • Multienzyme complexes
    • Reed, L. J. (1974) Multienzyme complexes, Acc. Chem. Res. 7, 40-46.
    • (1974) Acc. Chem. Res. , vol.7 , pp. 40-46
    • Reed, L.J.1
  • 34
    • 0030598366 scopus 로고    scopus 로고
    • Three-dimensional structure of the lipoyl domain from the dihydrolipoyl succinyltransferase component of the 2-oxo-glutarate dehydrogenase multienzyme complex of Escherichia coli
    • Ricaud, P. M., Howard, M. J., Roberts, E. L., Broadhurst, R. W. & Perham, R. N. (1996) Three-dimensional structure of the lipoyl domain from the dihydrolipoyl succinyltransferase component of the 2-oxo-glutarate dehydrogenase multienzyme complex of Escherichia coli, J. Mol. Biol. 264, 179-190.
    • (1996) J. Mol. Biol. , vol.264 , pp. 179-190
    • Ricaud, P.M.1    Howard, M.J.2    Roberts, E.L.3    Broadhurst, R.W.4    Perham, R.N.5
  • 35
    • 0024438186 scopus 로고
    • Partial complementation of pyruvate dehydrogenase deficiency by independently expressed lipoyl and catalytic domains of the dihydrolipoamide acetyltransferase component
    • Russell, G. C., Williamson, R. A. & Guest, J. R. (1989) Partial complementation of pyruvate dehydrogenase deficiency by independently expressed lipoyl and catalytic domains of the dihydrolipoamide acetyltransferase component, FEMS Microbiol. Lett. 60, 267-272.
    • (1989) FEMS Microbiol. Lett. , vol.60 , pp. 267-272
    • Russell, G.C.1    Williamson, R.A.2    Guest, J.R.3
  • 36
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulphatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H. & von Jagow, G. (1987) Tricine-sodium dodecyl sulphatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 37
    • 0026551488 scopus 로고
    • Reconstitution of pyruvate dehydrogenase multienzyme complexes based on chimeric core structures from Azotobacter vinelandii and Escherichia coli
    • Schulze, E., Westphal, A. H., Veeger, C. & de Kok, A. (1992) Reconstitution of pyruvate dehydrogenase multienzyme complexes based on chimeric core structures from Azotobacter vinelandii and Escherichia coli, Eur. J. Biochem. 206, 427-435.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 427-435
    • Schulze, E.1    Westphal, A.H.2    Veeger, C.3    De Kok, A.4
  • 38
    • 0014952583 scopus 로고
    • Regulation of the activity of the pyruvate dehydrogenase complex of Escherichia coli
    • Schwartz, E. R. & Reed, L. J. (1970) Regulation of the activity of the pyruvate dehydrogenase complex of Escherichia coli, Biochemistry 9, 1434-1439.
    • (1970) Biochemistry , vol.9 , pp. 1434-1439
    • Schwartz, E.R.1    Reed, L.J.2
  • 39
    • 0021451569 scopus 로고
    • Nucleotide sequence of the sucB gene encoding the dihydrolipoamide succinyltransferase of Escherichia coli K12 and homology with the corresponding acetyltransferase
    • Spencer, M. E., Darlison, M. G., Stephens, P. E., Duckenfield, I. K. & Guest, J. R. (1984) Nucleotide sequence of the sucB gene encoding the dihydrolipoamide succinyltransferase of Escherichia coli K12 and homology with the corresponding acetyltransferase, Eur. J. Biochem. 141, 361-374.
    • (1984) Eur. J. Biochem. , vol.141 , pp. 361-374
    • Spencer, M.E.1    Darlison, M.G.2    Stephens, P.E.3    Duckenfield, I.K.4    Guest, J.R.5
  • 40
    • 0022411103 scopus 로고
    • α-Ketoglutarate dehydrogenase complex of Escherichia coli. A hybrid complex containing pyruvate dehydrogenase subunits from pyruvate dehydrogenase complex
    • Steginsky, C. A., Gruys, K. J. & Frey, P. A. (1985) α-Ketoglutarate dehydrogenase complex of Escherichia coli. A hybrid complex containing pyruvate dehydrogenase subunits from pyruvate dehydrogenase complex, J. Biol. Chem. 260, 13690-13693.
    • (1985) J. Biol. Chem. , vol.260 , pp. 13690-13693
    • Steginsky, C.A.1    Gruys, K.J.2    Frey, P.A.3
  • 41
    • 0020789034 scopus 로고
    • The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component
    • Stephens, P. E., Darlison, M. G., Lewis, H. M. & Guest, J. R. (1983) The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component, Eur. J. Biochem. 133, 481-489.
    • (1983) Eur. J. Biochem. , vol.133 , pp. 481-489
    • Stephens, P.E.1    Darlison, M.G.2    Lewis, H.M.3    Guest, J.R.4
  • 42
    • 0030298405 scopus 로고    scopus 로고
    • Recognition of a surface loop of the lipoyl domain underlies substrate channelling in the pyruvate dehydrogenase multienzyme complex
    • Wallis, N. G., Allen, M. D., Broadhurst, R. W., Lessard, I. A. D. & Perham, R. N. (1996) Recognition of a surface loop of the lipoyl domain underlies substrate channelling in the pyruvate dehydrogenase multienzyme complex, J. Mol. Biol. 263, 463-474.
    • (1996) J. Mol. Biol. , vol.263 , pp. 463-474
    • Wallis, N.G.1    Allen, M.D.2    Broadhurst, R.W.3    Lessard, I.A.D.4    Perham, R.N.5
  • 43
    • 0025038023 scopus 로고
    • The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 2. Molecular cloning and sequence analysis of the gene encoding the succinyltransferase component
    • Westphal, A. H. & de Kok. A. (1990) The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 2. Molecular cloning and sequence analysis of the gene encoding the succinyltransferase component, Eur. J. Biochem. 187, 235-239.
    • (1990) Eur. J. Biochem. , vol.187 , pp. 235-239
    • Westphal, A.H.1    De Kok, A.2
  • 44
    • 0022889369 scopus 로고
    • Dihydrolipoyl transacetylase of Escherichia coli. Formation of 8-S-acetyldihydrolipoamide
    • Yang, Y.-S. & Frey, P. A. (1986) Dihydrolipoyl transacetylase of Escherichia coli. Formation of 8-S-acetyldihydrolipoamide, Biochemistry 25, 8173-8178.
    • (1986) Biochemistry , vol.25 , pp. 8173-8178
    • Yang, Y.-S.1    Frey, P.A.2


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