메뉴 건너뛰기




Volumn 370, Issue 3, 2007, Pages 541-554

Substrate and Product Complexes of Escherichia coli Adenylosuccinate Lyase Provide New Insights into the Enzymatic Mechanism

Author keywords

adenylosuccinate lyase; argininosuccinate lyase fumarase C superfamily; purine biosynthesis; elimination

Indexed keywords

ADENYLOSUCCINATE LYASE;

EID: 34250158440     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.04.052     Document Type: Article
Times cited : (41)

References (51)
  • 1
    • 0032570893 scopus 로고    scopus 로고
    • Identification of new mutations in the adenylosuccinate lyase gene associated with impaired enzyme activity in lymphocytes and red blood cells
    • Verginelli D., Luckow B., Crifo C., Salerno C., and Gross M. Identification of new mutations in the adenylosuccinate lyase gene associated with impaired enzyme activity in lymphocytes and red blood cells. Biochim. Biophys. Acta 1406 (1998) 81-84
    • (1998) Biochim. Biophys. Acta , vol.1406 , pp. 81-84
    • Verginelli, D.1    Luckow, B.2    Crifo, C.3    Salerno, C.4    Gross, M.5
  • 5
    • 0030855248 scopus 로고    scopus 로고
    • The structure of l-aspartate ammonia-lyase from Escherichia coli
    • Shi W., Dunbar J., Jayasekera M.M., Viola R.E., and Farber G.K. The structure of l-aspartate ammonia-lyase from Escherichia coli. Biochemistry 36 (1997) 9136-9144
    • (1997) Biochemistry , vol.36 , pp. 9136-9144
    • Shi, W.1    Dunbar, J.2    Jayasekera, M.M.3    Viola, R.E.4    Farber, G.K.5
  • 6
    • 0028518695 scopus 로고
    • The structure of avian eye lens delta-crystallin reveals a new fold for a superfamily of oligomeric enzymes
    • Simpson A., Bateman O., Driessen H., Lindley P., Moss D., Mylvaganam S., et al. The structure of avian eye lens delta-crystallin reveals a new fold for a superfamily of oligomeric enzymes. Nature Struct. Biol. 1 (1994) 724-734
    • (1994) Nature Struct. Biol. , vol.1 , pp. 724-734
    • Simpson, A.1    Bateman, O.2    Driessen, H.3    Lindley, P.4    Moss, D.5    Mylvaganam, S.6
  • 7
    • 0034651835 scopus 로고    scopus 로고
    • The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway
    • Toth E.A., and Yeates T.O. The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway. Structure Fold. Des. 8 (2000) 163-174
    • (2000) Structure Fold. Des. , vol.8 , pp. 163-174
    • Toth, E.A.1    Yeates, T.O.2
  • 8
    • 0030848314 scopus 로고    scopus 로고
    • Human argininosuccinate lyase: a structural basis for intragenic complementation
    • Turner M.A., Simpson A., McInnes R.R., and Howell P.L. Human argininosuccinate lyase: a structural basis for intragenic complementation. Proc. Natl Acad. Sci. USA 94 (1997) 9063-9068
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 9063-9068
    • Turner, M.A.1    Simpson, A.2    McInnes, R.R.3    Howell, P.L.4
  • 9
    • 4043057880 scopus 로고    scopus 로고
    • Crystal structure of 3-carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida, a fumarase class II type cycloisomerase: enzyme evolution in parallel pathways
    • Yang J., Wang Y., Woolridge E.M., Arora V., Petsko G.A., Kozarich J.W., and Ringe D. Crystal structure of 3-carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida, a fumarase class II type cycloisomerase: enzyme evolution in parallel pathways. Biochemistry 43 (2004) 10424-10434
    • (2004) Biochemistry , vol.43 , pp. 10424-10434
    • Yang, J.1    Wang, Y.2    Woolridge, E.M.3    Arora, V.4    Petsko, G.A.5    Kozarich, J.W.6    Ringe, D.7
  • 10
    • 0037414436 scopus 로고    scopus 로고
    • Crystal structure of thermostable aspartase from Bacillus sp. YM55-1: structure-based exploration of functional sites in the aspartase family
    • Fujii T., Sakai H., Kawata Y., and Hata Y. Crystal structure of thermostable aspartase from Bacillus sp. YM55-1: structure-based exploration of functional sites in the aspartase family. J. Mol. Biol. 328 (2003) 635-654
    • (2003) J. Mol. Biol. , vol.328 , pp. 635-654
    • Fujii, T.1    Sakai, H.2    Kawata, Y.3    Hata, Y.4
  • 11
    • 0033524224 scopus 로고    scopus 로고
    • His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of Bacillus subtilis
    • Lee T.T., Worby C., Bao Z.Q., Dixon J.E., and Colman R.F. His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of Bacillus subtilis. Biochemistry 38 (1999) 22-32
    • (1999) Biochemistry , vol.38 , pp. 22-32
    • Lee, T.T.1    Worby, C.2    Bao, Z.Q.3    Dixon, J.E.4    Colman, R.F.5
  • 12
    • 0037040187 scopus 로고    scopus 로고
    • Mutational analysis of duck delta 2 crystallin and the structure of an inactive mutant with bound substrate provide insight into the enzymatic mechanism of argininosuccinate lyase
    • Sampaleanu L.M., Yu B., and Howell P.L. Mutational analysis of duck delta 2 crystallin and the structure of an inactive mutant with bound substrate provide insight into the enzymatic mechanism of argininosuccinate lyase. J. Biol. Chem. 277 (2002) 4166-4175
    • (2002) J. Biol. Chem. , vol.277 , pp. 4166-4175
    • Sampaleanu, L.M.1    Yu, B.2    Howell, P.L.3
  • 13
    • 0028198853 scopus 로고
    • Mutagenic investigation of conserved functional amino acids in Escherichia coli l-aspartase
    • Saribas A.S., Schindler J.F., and Viola R.E. Mutagenic investigation of conserved functional amino acids in Escherichia coli l-aspartase. J. Biol. Chem. 269 (1994) 6313-6319
    • (1994) J. Biol. Chem. , vol.269 , pp. 6313-6319
    • Saribas, A.S.1    Schindler, J.F.2    Viola, R.E.3
  • 14
    • 0030938063 scopus 로고    scopus 로고
    • Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site
    • Weaver T., Lees M., and Banaszak L. Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site. Protein Sci. 6 (1997) 834-842
    • (1997) Protein Sci. , vol.6 , pp. 834-842
    • Weaver, T.1    Lees, M.2    Banaszak, L.3
  • 15
    • 0020804608 scopus 로고
    • Nitro analogs of substrates for adenylosuccinate synthetase and adenylosuccinate lyase
    • Porter D.J., Rudie N.G., and Bright H.J. Nitro analogs of substrates for adenylosuccinate synthetase and adenylosuccinate lyase. Arch. Biochem. Biophys. 225 (1983) 157-163
    • (1983) Arch. Biochem. Biophys. , vol.225 , pp. 157-163
    • Porter, D.J.1    Rudie, N.G.2    Bright, H.J.3
  • 16
    • 77956939611 scopus 로고
    • The enzymic elimination of ammonia
    • Boyer P.D. (Ed), Academic Press, New York
    • Hanson K.R., and Havir E.A. The enzymic elimination of ammonia. In: Boyer P.D. (Ed). The Enzymes. 3rd edit. vol. 7 (1972), Academic Press, New York 75-166
    • (1972) The Enzymes. 3rd edit. , vol.7 , pp. 75-166
    • Hanson, K.R.1    Havir, E.A.2
  • 17
    • 0014408541 scopus 로고
    • The kinetics of adenylosuccinate lyase
    • Bridger W.A., and Cohen L.H. The kinetics of adenylosuccinate lyase. J. Biol. Chem. 243 (1968) 644-650
    • (1968) J. Biol. Chem. , vol.243 , pp. 644-650
    • Bridger, W.A.1    Cohen, L.H.2
  • 18
    • 0023411218 scopus 로고
    • Purification of adenylosuccinate lyase from rat skeletal muscle by a novel affinity column. Stabilization of the enzyme, and effects of anions and fluoro analogues of the substrate
    • Casey P.J., and Lowenstein J.M. Purification of adenylosuccinate lyase from rat skeletal muscle by a novel affinity column. Stabilization of the enzyme, and effects of anions and fluoro analogues of the substrate. Biochem. J. 246 (1987) 263-269
    • (1987) Biochem. J. , vol.246 , pp. 263-269
    • Casey, P.J.1    Lowenstein, J.M.2
  • 19
    • 77956906954 scopus 로고
    • Argininosuccinases and adenylosuccinases
    • Boyer P.D. (Ed), Academic Press, New York
    • Ratner S. Argininosuccinases and adenylosuccinases. In: Boyer P.D. (Ed). The Enzymes. 3rd edit. vol. 7 (1972), Academic Press, New York 167-197
    • (1972) The Enzymes. 3rd edit. , vol.7 , pp. 167-197
    • Ratner, S.1
  • 20
    • 34250163723 scopus 로고
    • Biosynthesis of the purines. 28. Mechanism of action of adenylosuccinase
    • Miller R.W., and Buchanan J.M. Biosynthesis of the purines. 28. Mechanism of action of adenylosuccinase. J. Biol. Chem. 237 (1962) 491-496
    • (1962) J. Biol. Chem. , vol.237 , pp. 491-496
    • Miller, R.W.1    Buchanan, J.M.2
  • 21
    • 0032499536 scopus 로고    scopus 로고
    • Implication of His68 in the substrate site of Bacillus subtilis adenylosuccinate lyase by mutagenesis and affinity labeling with 2- [(4-bromo-2,3-dioxobutyl)thio]adenosine 5′-monophosphate
    • Lee T.T., Worby C., Bao Z.Q., Dixon J.E., and Colman R.F. Implication of His68 in the substrate site of Bacillus subtilis adenylosuccinate lyase by mutagenesis and affinity labeling with 2- [(4-bromo-2,3-dioxobutyl)thio]adenosine 5′-monophosphate. Biochemistry 37 (1998) 8481-8489
    • (1998) Biochemistry , vol.37 , pp. 8481-8489
    • Lee, T.T.1    Worby, C.2    Bao, Z.Q.3    Dixon, J.E.4    Colman, R.F.5
  • 22
    • 0030614461 scopus 로고    scopus 로고
    • Identification of His141 in the active site of Bacillus subtiliadenylosuccinate lyase by affinity labeling with 6-(4-bromo-2,3-dioxobutyl)thioadenosine 5′-monophosphate
    • Lee T.T., Worby C., Dixon J.E., and Colman R.F. Identification of His141 in the active site of Bacillus subtiliadenylosuccinate lyase by affinity labeling with 6-(4-bromo-2,3-dioxobutyl)thioadenosine 5′-monophosphate. J. Biol. Chem. 272 (1997) 458-465
    • (1997) J. Biol. Chem. , vol.272 , pp. 458-465
    • Lee, T.T.1    Worby, C.2    Dixon, J.E.3    Colman, R.F.4
  • 23
    • 0037133201 scopus 로고    scopus 로고
    • Three subunits contribute amino acids to the active site of tetrameric adenylosuccinate lyase: Lys268 and Glu275 are required
    • Brosius J.L., and Colman R.F. Three subunits contribute amino acids to the active site of tetrameric adenylosuccinate lyase: Lys268 and Glu275 are required. Biochemistry 41 (2002) 2217-2226
    • (2002) Biochemistry , vol.41 , pp. 2217-2226
    • Brosius, J.L.1    Colman, R.F.2
  • 24
    • 2942563993 scopus 로고    scopus 로고
    • Gln212, Asn270, and Arg301 are critical for catalysis by adenylosuccinate lyase from Bacillus subtilis
    • Segall M.L., and Colman R.F. Gln212, Asn270, and Arg301 are critical for catalysis by adenylosuccinate lyase from Bacillus subtilis. Biochemistry 43 (2004) 7391-7402
    • (2004) Biochemistry , vol.43 , pp. 7391-7402
    • Segall, M.L.1    Colman, R.F.2
  • 25
    • 0034619576 scopus 로고    scopus 로고
    • A key role in catalysis for His89 of adenylosuccinate lyase of Bacillus subtilis
    • Brosius J.L., and Colman R.F. A key role in catalysis for His89 of adenylosuccinate lyase of Bacillus subtilis. Biochemistry 39 (2000) 13336-13343
    • (2000) Biochemistry , vol.39 , pp. 13336-13343
    • Brosius, J.L.1    Colman, R.F.2
  • 26
    • 0033596716 scopus 로고    scopus 로고
    • Mutational analysis of amino acid residues involved in argininosuccinate lyase activity in duck delta II crystallin
    • Chakraborty A.R., Davidson A., and Howell P.L. Mutational analysis of amino acid residues involved in argininosuccinate lyase activity in duck delta II crystallin. Biochemistry 38 (1999) 2435-2443
    • (1999) Biochemistry , vol.38 , pp. 2435-2443
    • Chakraborty, A.R.1    Davidson, A.2    Howell, P.L.3
  • 27
    • 0030670929 scopus 로고    scopus 로고
    • Structural comparison of the enzymatically active and inactive forms of delta crystallin and the role of histidine 91
    • Abu-Abed M., Turner M.A., Vallee F., Simpson A., Slingsby C., and Howell P.L. Structural comparison of the enzymatically active and inactive forms of delta crystallin and the role of histidine 91. Biochemistry 36 (1997) 14012-14022
    • (1997) Biochemistry , vol.36 , pp. 14012-14022
    • Abu-Abed, M.1    Turner, M.A.2    Vallee, F.3    Simpson, A.4    Slingsby, C.5    Howell, P.L.6
  • 28
    • 0029073551 scopus 로고
    • Exploring the role of histidines in the catalytic activity of duck delta-crystallins using site-directed mutagenesis
    • Patejunas G., Barbosa P., Lacombe M., and O'Brien W.E. Exploring the role of histidines in the catalytic activity of duck delta-crystallins using site-directed mutagenesis. Exp. Eye Res. 61 (1995) 151-154
    • (1995) Exp. Eye Res. , vol.61 , pp. 151-154
    • Patejunas, G.1    Barbosa, P.2    Lacombe, M.3    O'Brien, W.E.4
  • 29
    • 0033596741 scopus 로고    scopus 로고
    • Crystal structure of an inactive duck delta II crystallin mutant with bound argininosuccinate
    • Vallee F., Turner M.A., Lindley P.L., and Howell P.L. Crystal structure of an inactive duck delta II crystallin mutant with bound argininosuccinate. Biochemistry 38 (1999) 2425-2434
    • (1999) Biochemistry , vol.38 , pp. 2425-2434
    • Vallee, F.1    Turner, M.A.2    Lindley, P.L.3    Howell, P.L.4
  • 30
    • 0029854921 scopus 로고    scopus 로고
    • Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli
    • Weaver T., and Banaszak L. Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli. Biochemistry 35 (1996) 13955-13965
    • (1996) Biochemistry , vol.35 , pp. 13955-13965
    • Weaver, T.1    Banaszak, L.2
  • 32
    • 0034636987 scopus 로고    scopus 로고
    • The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds
    • Toth E.A., Worby C., Dixon J.E., Goedken E.R., Marqusee S., and Yeates T.O. The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds. J. Mol. Biol. 301 (2000) 433-450
    • (2000) J. Mol. Biol. , vol.301 , pp. 433-450
    • Toth, E.A.1    Worby, C.2    Dixon, J.E.3    Goedken, E.R.4    Marqusee, S.5    Yeates, T.O.6
  • 33
    • 0035814902 scopus 로고    scopus 로고
    • Structural studies of duck delta 1 and delta 2 crystallin suggest conformational changes occur during catalysis
    • Sampaleanu L.M., Vallee F., Slingsby C., and Howell P.L. Structural studies of duck delta 1 and delta 2 crystallin suggest conformational changes occur during catalysis. Biochemistry 40 (2001) 2732-2742
    • (2001) Biochemistry , vol.40 , pp. 2732-2742
    • Sampaleanu, L.M.1    Vallee, F.2    Slingsby, C.3    Howell, P.L.4
  • 34
    • 21644485437 scopus 로고    scopus 로고
    • Structure determination and refinement at 2.44 Å resolution of argininosuccinate lyase from Escherichia coli
    • Bhaumik P., Koski M.K., Bergmann U., and Wierenga R.K. Structure determination and refinement at 2.44 Å resolution of argininosuccinate lyase from Escherichia coli. Acta Crystallog. sect. D 60 (2004) 1964-1970
    • (2004) Acta Crystallog. sect. D , vol.60 , pp. 1964-1970
    • Bhaumik, P.1    Koski, M.K.2    Bergmann, U.3    Wierenga, R.K.4
  • 35
    • 2942677105 scopus 로고    scopus 로고
    • The determinants of carboxyl pKa values in turkey ovomucoid third domain
    • Li H., Robertson A.D., and Jensen J.H. The determinants of carboxyl pKa values in turkey ovomucoid third domain. Proteins: Struct. Funct. Genet. 55 (2004) 689-704
    • (2004) Proteins: Struct. Funct. Genet. , vol.55 , pp. 689-704
    • Li, H.1    Robertson, A.D.2    Jensen, J.H.3
  • 36
    • 10344226653 scopus 로고    scopus 로고
    • Determinants of cysteine pKa values in creatine kinase and alpha1-antitrypsin
    • Naor M.M., and Jensen J.H. Determinants of cysteine pKa values in creatine kinase and alpha1-antitrypsin. Proteins: Struct. Funct. Genet. 57 (2004) 799-803
    • (2004) Proteins: Struct. Funct. Genet. , vol.57 , pp. 799-803
    • Naor, M.M.1    Jensen, J.H.2
  • 37
    • 0026738940 scopus 로고
    • Mutational analysis of active site residues in pig heart aconitase
    • Zheng L., Kennedy M.C., Beinert H., and Zalkin H. Mutational analysis of active site residues in pig heart aconitase. J. Biol. Chem. 267 (1992) 7895-7903
    • (1992) J. Biol. Chem. , vol.267 , pp. 7895-7903
    • Zheng, L.1    Kennedy, M.C.2    Beinert, H.3    Zalkin, H.4
  • 38
    • 33847323201 scopus 로고    scopus 로고
    • Important roles of hydroxylic amino acid residues in the function of Bacillus subtilis adenylosuccinate lyase
    • Segall M.L., Cashman M.A., and Colman R.F. Important roles of hydroxylic amino acid residues in the function of Bacillus subtilis adenylosuccinate lyase. Protein Sci. 16 (2007) 441-448
    • (2007) Protein Sci. , vol.16 , pp. 441-448
    • Segall, M.L.1    Cashman, M.A.2    Colman, R.F.3
  • 39
    • 0026436191 scopus 로고
    • Escherichia coli purB gene: cloning, nucleotide sequence, and regulation by purR
    • He B., Smith J.M., and Zalkin H. Escherichia coli purB gene: cloning, nucleotide sequence, and regulation by purR. J. Bacteriol. 174 (1992) 130-136
    • (1992) J. Bacteriol. , vol.174 , pp. 130-136
    • He, B.1    Smith, J.M.2    Zalkin, H.3
  • 40
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Carter C.W., and Sweet R.M. (Eds), Academic Press, New York
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. In: Carter C.W., and Sweet R.M. (Eds). Methods in Enzymology vol. 276A (1997), Academic Press, New York 307-326
    • (1997) Methods in Enzymology , vol.276 A , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 43
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125 (1999) 156-165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 44
    • 0030986177 scopus 로고    scopus 로고
    • Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement
    • Adams P.D., Pannu N.S., Read R.J., and Brunger A.T. Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement. Proc. Natl Acad. Sci. USA 94 (1997) 5018-5023
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5018-5023
    • Adams, P.D.1    Pannu, N.S.2    Read, R.J.3    Brunger, A.T.4
  • 45
    • 0032212015 scopus 로고    scopus 로고
    • Incorporation of prior phase information strengthens maximum-likelihood structure refinement
    • Pannu N.S., Murshudov G.N., Dodson E.J., and Read R.J. Incorporation of prior phase information strengthens maximum-likelihood structure refinement. Acta Crystallog. sect. D 54 (1998) 1285-1294
    • (1998) Acta Crystallog. sect. D , vol.54 , pp. 1285-1294
    • Pannu, N.S.1    Murshudov, G.N.2    Dodson, E.J.3    Read, R.J.4
  • 46
    • 0022325950 scopus 로고
    • Resolution of phase ambiguity in macromolecular crystallography
    • Wang B.C. Resolution of phase ambiguity in macromolecular crystallography. Methods Enzymol. 115 (1985) 90-112
    • (1985) Methods Enzymol. , vol.115 , pp. 90-112
    • Wang, B.C.1
  • 47
    • 0033213239 scopus 로고    scopus 로고
    • The finer things in X-ray diffraction data collection
    • Pflugrath J.W. The finer things in X-ray diffraction data collection. Acta Crystallog. sect. D 55 (1999) 1718-1725
    • (1999) Acta Crystallog. sect. D , vol.55 , pp. 1718-1725
    • Pflugrath, J.W.1
  • 48
    • 0001431519 scopus 로고
    • DREADD - data reduction and error analysis for single-crystal diffractometer data
    • Blessing R.H. DREADD - data reduction and error analysis for single-crystal diffractometer data. J. Appl. Crystallogr. 22 (1989) 396-397
    • (1989) J. Appl. Crystallogr. , vol.22 , pp. 396-397
    • Blessing, R.H.1
  • 49
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22 (1994) 4673-4680
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 50
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallog. sect. D 60 (2004) 2126-2132
    • (2004) Acta Crystallog. sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 51
    • 0015499956 scopus 로고
    • The purine nucleotide cycle. The production of ammonia from aspartate by extracts of rat skeletal muscle
    • Tornheim K., and Lowenstein J.M. The purine nucleotide cycle. The production of ammonia from aspartate by extracts of rat skeletal muscle. J. Biol. Chem. 247 (1972) 162-169
    • (1972) J. Biol. Chem. , vol.247 , pp. 162-169
    • Tornheim, K.1    Lowenstein, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.