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Volumn 290, Issue 22, 2015, Pages 14154-14165

Three-dimensional structure of a Kunitz-type inhibitor in complex with an elastase-like enzyme

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; BINS; COMPLEX NETWORKS; ENZYME INHIBITION; ENZYMES; SCAFFOLDS (BIOLOGY);

EID: 84930630956     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.647586     Document Type: Article
Times cited : (18)

References (65)
  • 1
  • 3
    • 0029446038 scopus 로고
    • Elastase in the prevention of arterial aging and the treatment of atherosclerosis
    • Ooyama, T., and Sakamato H. (1995) Elastase in the prevention of arterial aging and the treatment of atherosclerosis. Ciba Found. Symp. 192, 307-317
    • (1995) Ciba Found. Symp. , vol.192 , pp. 307-317
    • Ooyama, T.1    Sakamato, H.2
  • 4
    • 0029383641 scopus 로고
    • The pathogenesis of emphysema: The elastase:antielastase hypothesis 30 years later
    • Shapiro, S. D. (1995) The pathogenesis of emphysema: the elastase:antielastase hypothesis 30 years later. Proc. Assoc. Am. Physicians 107, 346-352
    • (1995) Proc. Assoc. Am. Physicians , vol.107 , pp. 346-352
    • Shapiro, S.D.1
  • 5
    • 78650096176 scopus 로고    scopus 로고
    • Neutrophil elastase, proteinase 3, and cathepsin G as therapeutic targets in human diseases
    • Korkmaz, B., Horwitz, M. S., Jenne, D. E., and Gauthier, F. (2010) Neutrophil elastase, proteinase 3, and cathepsin G as therapeutic targets in human diseases. Pharmacol. Rev. 62, 726-759
    • (2010) Pharmacol. Rev. , vol.62 , pp. 726-759
    • Korkmaz, B.1    Horwitz, M.S.2    Jenne, D.E.3    Gauthier, F.4
  • 6
    • 0024373709 scopus 로고
    • Novel inhibitors of human-leukocyte elastase and cathepsin G: Sequence variants of squash seed protease inhibitor with altered protease selectivity
    • McWherter, C. A., Walkenhorst, W. F., Campbell, E. J., and Glover, G. I. (1989) Novel inhibitors of human-leukocyte elastase and cathepsin G: sequence variants of squash seed protease inhibitor with altered protease selectivity. Biochemistry 28, 5708-5714
    • (1989) Biochemistry , vol.28 , pp. 5708-5714
    • McWherter, C.A.1    Walkenhorst, W.F.2    Campbell, E.J.3    Glover, G.I.4
  • 7
    • 12344305212 scopus 로고    scopus 로고
    • Potential role of inhibitors of neutrophil elastase in treating diseases of the airway
    • Chughtai, B., and O'Riordan, T. G. (2004) Potential role of inhibitors of neutrophil elastase in treating diseases of the airway. J. Aerosol Med. 17, 289-298
    • (2004) J. Aerosol Med. , vol.17 , pp. 289-298
    • Chughtai, B.1    O'Riordan, T.G.2
  • 9
    • 1342287837 scopus 로고    scopus 로고
    • Role of imbalance between neutrophil elastase and alpha 1-antitrypsin in cancer development and progression
    • Sun, Z., and Yang, P. (2004) Role of imbalance between neutrophil elastase and alpha 1-antitrypsin in cancer development and progression. Lancet Oncol. 5, 182-190
    • (2004) Lancet Oncol. , vol.5 , pp. 182-190
    • Sun, Z.1    Yang, P.2
  • 10
    • 0345708448 scopus 로고    scopus 로고
    • Neutrophil elastase cleaves PML-RARα and is important for the development of acute promyelocytic leukemia in mice
    • Lane, A. A., and Ley, T. J. (2003) Neutrophil elastase cleaves PML-RARα and is important for the development of acute promyelocytic leukemia in mice. Cell 115, 305-318
    • (2003) Cell , vol.115 , pp. 305-318
    • Lane, A.A.1    Ley, T.J.2
  • 11
    • 0024571818 scopus 로고
    • Human leukocyte and porcine pancreatic elastase X-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors
    • Bode, W., Meyer, E., Jr., and Powers, J. C. (1989) Human leukocyte and porcine pancreatic elastase X-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors. Biochemistry 28, 1951-1963
    • (1989) Biochemistry , vol.28 , pp. 1951-1963
    • Bode, W.1    Meyer, E.2    Powers, J.C.3
  • 13
    • 0022801412 scopus 로고
    • X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ocomucoid inhibitor
    • Bode, W., Wei, A. Z., Huber, R., Meyer, E., Travis, J., and Neumann, S. (1986) X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ocomucoid inhibitor. EMBO J. 5, 2453-2458
    • (1986) EMBO J. , vol.5 , pp. 2453-2458
    • Bode, W.1    Wei, A.Z.2    Huber, R.3    Meyer, E.4    Travis, J.5    Neumann, S.6
  • 14
    • 0029811088 scopus 로고    scopus 로고
    • Crystal structure of an elastase-specific inhibitor elafin complexed with porcine pancreatic elastase determined at 1.9 A resolution
    • Tsunemi, M., Matsuura, Y., Sakakibara, S., and Katsube, Y. (1996) Crystal structure of an elastase-specific inhibitor elafin complexed with porcine pancreatic elastase determined at 1.9 A resolution. Biochemistry 35, 11570-11576
    • (1996) Biochemistry , vol.35 , pp. 11570-11576
    • Tsunemi, M.1    Matsuura, Y.2    Sakakibara, S.3    Katsube, Y.4
  • 15
    • 0028773905 scopus 로고
    • The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase
    • Huang, K., Strynadka, N. C., Bernard, V. D., Peanasky, R. J., and James, M. N. (1994) The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase. Structure 2, 679-689
    • (1994) Structure , vol.2 , pp. 679-689
    • Huang, K.1    Strynadka, N.C.2    Bernard, V.D.3    Peanasky, R.J.4    James, M.N.5
  • 17
    • 85025382997 scopus 로고
    • Isolation from beef pancreas of crystalline trypsinogen, trypsin, a trypsin inhibitor, and an inhibitor-trypsin compound
    • Kunitz, M., and Northrop, J. H. (1936) Isolation from beef pancreas of crystalline trypsinogen, trypsin, a trypsin inhibitor, and an inhibitor-trypsin compound. J. Gen. Physiol. 19, 991-1007
    • (1936) J. Gen. Physiol. , vol.19 , pp. 991-1007
    • Kunitz, M.1    Northrop, J.H.2
  • 20
    • 0014211618 scopus 로고
    • On the size of the active site in proteases
    • I. Papain
    • Schechter, I., and Berger, A. (1967) On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 23
    • 0033485402 scopus 로고    scopus 로고
    • Selection of human elastase inhibitors from a conformationally constrained combinatorial peptide library
    • McBride, J. D., Freeman, H. N., and Leatherbarrow, R. J. (1999) Selection of human elastase inhibitors from a conformationally constrained combinatorial peptide library. Eur. J. Biochem. 266, 403-412
    • (1999) Eur. J. Biochem. , vol.266 , pp. 403-412
    • McBride, J.D.1    Freeman, H.N.2    Leatherbarrow, R.J.3
  • 24
    • 35848964031 scopus 로고    scopus 로고
    • Characterization and comparative 3D modeling of CmPI-II, a novel 'nonclassical' Kazal-type inhibitor from the marine snail Cenchritis muricatus (Mollusca)
    • González, Y., Pons, T., Gil, J., Besada, V., Alonso-del-Rivero, M., Tanaka, A. S., Araujo, M. S., and Chávez, M. A. (2007) Characterization and comparative 3D modeling of CmPI-II, a novel 'nonclassical' Kazal-type inhibitor from the marine snail Cenchritis muricatus (Mollusca). Biol. Chem. 388, 1183-1194
    • (2007) Biol. Chem. , vol.388 , pp. 1183-1194
    • González, Y.1    Pons, T.2    Gil, J.3    Besada, V.4    Alonso-del-Rivero, M.5    Tanaka, A.S.6    Araujo, M.S.7    Chávez, M.A.8
  • 26
    • 0029940321 scopus 로고    scopus 로고
    • Inhibition of human leukocyte and porcine pancreatic elastase by homologues of bovine pancreatic trypsin inhibitor
    • Kraunsoe, J. A., Claridge, T. D., and Lowe, G. (1996) Inhibition of human leukocyte and porcine pancreatic elastase by homologues of bovine pancreatic trypsin inhibitor. Biochemistry 35, 9090-9096
    • (1996) Biochemistry , vol.35 , pp. 9090-9096
    • Kraunsoe, J.A.1    Claridge, T.D.2    Lowe, G.3
  • 27
    • 0033612211 scopus 로고    scopus 로고
    • Interscaffolding additivity: Binding of P1 variants of bovine pancreatic trypsin inhibitor to four serine proteases
    • Krowarsch, D., Dadlez, M., Buczek, O., Krokoszynska, I., Smalas, A. O., and Otlewski, J. (1999) Interscaffolding additivity: binding of P1 variants of bovine pancreatic trypsin inhibitor to four serine proteases. J. Mol. Biol. 289, 175-186
    • (1999) J. Mol. Biol. , vol.289 , pp. 175-186
    • Krowarsch, D.1    Dadlez, M.2    Buczek, O.3    Krokoszynska, I.4    Smalas, A.O.5    Otlewski, J.6
  • 28
    • 0035905430 scopus 로고    scopus 로고
    • Selection of potent chymotrypsin and elastase inhibitors from M13 phage library of basic pancreatic trypsin inhibitor (BPTI)
    • Kiczak, L., Kasztura, M., Koscielska-Kasprzak, K., Dadlez, M., and Otlewski, J. (2001) Selection of potent chymotrypsin and elastase inhibitors from M13 phage library of basic pancreatic trypsin inhibitor (BPTI). Biochim. Biophys. Acta 1550, 153-163
    • (2001) Biochim. Biophys. Acta , vol.1550 , pp. 153-163
    • Kiczak, L.1    Kasztura, M.2    Koscielska-Kasprzak, K.3    Dadlez, M.4    Otlewski, J.5
  • 31
    • 80054909439 scopus 로고    scopus 로고
    • The P2' residue is a key determinant of mesotrypsin specificity, engineering a high affinity inhibitor with anticancer activity
    • Salameh, M. A., Soares, A. S., Hockla, A., Radisky, D. C., and Radisky, E. S. (2011) The P2' residue is a key determinant of mesotrypsin specificity, engineering a high affinity inhibitor with anticancer activity. Biochem. J. 440, 95-105
    • (2011) Biochem. J. , vol.440 , pp. 95-105
    • Salameh, M.A.1    Soares, A.S.2    Hockla, A.3    Radisky, D.C.4    Radisky, E.S.5
  • 32
    • 0030794907 scopus 로고    scopus 로고
    • Crystal structures of bovine chymotrypsin and trypsin complexed to the inhibitor domain of Alzheimer's amyloid β-protein precursor (APPI) and basic trypsin inhibitor (BPTI): Engineering of inhibitors with altered specificities
    • Scheidig, A. J., Hynes, T. R., Pelletier, L. A., Wells, J. A., and Kossiakoff, A. A. (1997) Crystal structures of bovine chymotrypsin and trypsin complexed to the inhibitor domain of Alzheimer's amyloid β-protein precursor (APPI) and basic trypsin inhibitor (BPTI): engineering of inhibitors with altered specificities. Protein Sci. 6, 1806-1824
    • (1997) Protein Sci. , vol.6 , pp. 1806-1824
    • Scheidig, A.J.1    Hynes, T.R.2    Pelletier, L.A.3    Wells, J.A.4    Kossiakoff, A.A.5
  • 33
    • 23044502564 scopus 로고    scopus 로고
    • Crystal structure of Kunitz domain 1 (KD1) of tissue factor pathway inhibitor-2 in complex with trypsin
    • Schmidt, A. E., Chand, H. S., Cascio, D., Kisiel, W., and Bajaj, S. P. (2005) Crystal structure of Kunitz domain 1 (KD1) of tissue factor pathway inhibitor-2 in complex with trypsin. J. Biol. Chem. 280, 27832-27838
    • (2005) J. Biol. Chem. , vol.280 , pp. 27832-27838
    • Schmidt, A.E.1    Chand, H.S.2    Cascio, D.3    Kisiel, W.4    Bajaj, S.P.5
  • 34
    • 0031698348 scopus 로고    scopus 로고
    • The crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitor
    • Helland, R., Leiros, I., Berglund, G. I., Willassen, N. P., and Smalås, A. O. (1998) The crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitor. Eur. J. Biochem. 256, 317-324
    • (1998) Eur. J. Biochem. , vol.256 , pp. 317-324
    • Helland, R.1    Leiros, I.2    Berglund, G.I.3    Willassen, N.P.4    Smalås, A.O.5
  • 36
    • 0027467611 scopus 로고
    • The NMR solution structure of a Kunitz-type proteinase inhibitor from the sea anemone Stichodactyla helianthus
    • Antuch, W., Berndt, K. D., Chávez, M. A., Delfín, J., and Wüthrich, K. (1993) The NMR solution structure of a Kunitz-type proteinase inhibitor from the sea anemone Stichodactyla helianthus. Eur. J. Biochem. 212, 675-684
    • (1993) Eur. J. Biochem. , vol.212 , pp. 675-684
    • Antuch, W.1    Berndt, K.D.2    Chávez, M.A.3    Delfín, J.4    Wüthrich, K.5
  • 37
    • 80053976963 scopus 로고    scopus 로고
    • Recombinant expression of ShPI-1A, a non-specific BPTI-Kunitz-type inhibitor, and its protection effect on proteolytic degradation of recombinant human miniproinsulin expressed in Pichia pastoris
    • Gil, D., García-Fernández, R., Alonso-del-Rivero, M., Lamazares, E., Pérez, M., Varas, L., Díaz, J., Chávez, M. A., González-González, Y., and Mansur, M. (2011) Recombinant expression of ShPI-1A, a non-specific BPTI-Kunitz-type inhibitor, and its protection effect on proteolytic degradation of recombinant human miniproinsulin expressed in Pichia pastoris. FEMS Yeast Res. 7, 575-586
    • (2011) FEMS Yeast Res. , vol.7 , pp. 575-586
    • Gil, D.1    García-Fernández, R.2    Alonso-del-Rivero, M.3    Lamazares, E.4    Pérez, M.5    Varas, L.6    Díaz, J.7    Chávez, M.A.8    González-González, Y.9    Mansur, M.10
  • 39
    • 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
  • 40
    • 0022445901 scopus 로고
    • Probing steric and hydrophobic effects on enzyme-substrate interactions by protein engineering
    • Estell, D. A., Graycar, T. P., Miller, J. V., Powers, D. B., Wells, J. A., Burnier, J. P., and Ng, P. G. (1986) Probing steric and hydrophobic effects on enzyme-substrate interactions by protein engineering. Science 233, 659-663
    • (1986) Science , vol.233 , pp. 659-663
    • Estell, D.A.1    Graycar, T.P.2    Miller, J.V.3    Powers, D.B.4    Wells, J.A.5    Burnier, J.P.6    Ng, P.G.7
  • 41
    • 50549163362 scopus 로고
    • Preparation and properties of two new chromogenic substrates of trypsin
    • Erlanger, B. F., Kokowsky, N., and Cohen, E. (1961) Preparation and properties of two new chromogenic substrates of trypsin. Arch. Biochem. Biophys. 95, 271-278
    • (1961) Arch. Biochem. Biophys. , vol.95 , pp. 271-278
    • Erlanger, B.F.1    Kokowsky, N.2    Cohen, E.3
  • 42
    • 0018747530 scopus 로고
    • Mapping the extended substrate binding site of cathepsin G and human leukocyte elastase: Studies with peptide substrates related to the α1-protease inhibitor reactive site
    • Nakajima, K., Powers, J. C., Ashe, B. M., and Zimmerman, M. (1979) Mapping the extended substrate binding site of cathepsin G and human leukocyte elastase: studies with peptide substrates related to the α1-protease inhibitor reactive site. J. Biol. Chem. 254, 4027-4032
    • (1979) J. Biol. Chem. , vol.254 , pp. 4027-4032
    • Nakajima, K.1    Powers, J.C.2    Ashe, B.M.3    Zimmerman, M.4
  • 44
    • 33644864110 scopus 로고
    • p-Nitrophenyl-p'-guanidinobenzoate HCl: A new active site titrant for trypsin
    • Chase, T., Jr., and Shaw, E. (1967) p-Nitrophenyl-p'-guanidinobenzoate HCl: a new active site titrant for trypsin. Biochem. Biophys. Res. Commun. 29, 508-514
    • (1967) Biochem. Biophys. Res. Commun. , vol.29 , pp. 508-514
    • Chase, T.1    Shaw, E.2
  • 45
    • 0029145029 scopus 로고
    • Estimating Ki values for tight binding inhibitors from dose-response plots
    • Copeland, R. A., Lombardo, D., Glannaras, J., and Decicco, C. P. (1995) Estimating Ki values for tight binding inhibitors from dose-response plots. Bioorg. Med. Chem. 5, 1947-1952
    • (1995) Bioorg. Med. Chem. , vol.5 , pp. 1947-1952
    • Copeland, R.A.1    Lombardo, D.2    Glannaras, J.3    Decicco, C.P.4
  • 46
    • 0029003409 scopus 로고
    • Theoretical and practical aspects of proteinase inhibition kinetics
    • Bieth, J. G. (1995) Theoretical and practical aspects of proteinase inhibition kinetics. Methods Enzymol. 248, 59-84
    • (1995) Methods Enzymol. , vol.248 , pp. 59-84
    • Bieth, J.G.1
  • 47
    • 80053063462 scopus 로고    scopus 로고
    • Erithacus Software Ltd., Horley, United Kingdom
    • Leatherbarrow, R. J. (2009) GraFit Version 7, Erithacus Software Ltd., Horley, United Kingdom
    • (2009) GraFit Version 7
    • Leatherbarrow, R.J.1
  • 48
    • 34347248436 scopus 로고    scopus 로고
    • Detection of non-covalent protein interactions by "intensity fading" MALDI-TOF mass spectrometry: Applications to proteases and protease inhibitors
    • Yanes, O., Villanueva, J., Querol, E., and Aviles, F. X. (2007) Detection of non-covalent protein interactions by "intensity fading" MALDI-TOF mass spectrometry: applications to proteases and protease inhibitors. Nat. Protoc. 2, 119-130
    • (2007) Nat. Protoc. , vol.2 , pp. 119-130
    • Yanes, O.1    Villanueva, J.2    Querol, E.3    Aviles, F.X.4
  • 50
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 55
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Lüthy, R., Bowie, J. U., and Eisenberg, D. (1992) Assessment of protein models with three-dimensional profiles. Nature 356, 83-85
    • (1992) Nature , vol.356 , pp. 83-85
    • Lüthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 57
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 58
    • 0025398721 scopus 로고
    • What if, a molecular modeling and drug design program
    • Vriend, G. (1990) WHAT IF, a molecular modeling and drug design program. J. Mol. Graph. 8, 52-56
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 59
    • 22444436454 scopus 로고    scopus 로고
    • The limit of accuracy of protein modeling: Influence of crystal packing on protein structure
    • Eyal, E., Gerzon, S., Potapov, V., Edelman, M., and Sobolev, V. (2005) The limit of accuracy of protein modeling: influence of crystal packing on protein structure. J. Mol. Biol. 351, 431-442
    • (2005) J. Mol. Biol. , vol.351 , pp. 431-442
    • Eyal, E.1    Gerzon, S.2    Potapov, V.3    Edelman, M.4    Sobolev, V.5
  • 62
    • 0030005908 scopus 로고    scopus 로고
    • A removable spacer peptide in a α-factor-leader/insulin precursor fusion protein improves processing and concomitant yield of the insulin precursor in Saccharomyces cerevisiae
    • Kjeldsen, T., Brandt, J., Andersen, A. S., Egel-Mitani, M., Hach, M., Pettersson, A. F., and Vad, K. (1996) A removable spacer peptide in a α-factor-leader/insulin precursor fusion protein improves processing and concomitant yield of the insulin precursor in Saccharomyces cerevisiae. Gene 170, 107-112
    • (1996) Gene , vol.170 , pp. 107-112
    • Kjeldsen, T.1    Brandt, J.2    Andersen, A.S.3    Egel-Mitani, M.4    Hach, M.5    Pettersson, A.F.6    Vad, K.7
  • 63
    • 0021459593 scopus 로고
    • The isoinhibitors of chymotrypsin/elastase from Ascaris lumbricoides: Isolation by affinity chromatography and association with the enzymes
    • Peanasky, R. J., Bentz, Y., Paulson, B., Graham, D. L., and Babin, D. R. (1984) The isoinhibitors of chymotrypsin/elastase from Ascaris lumbricoides: isolation by affinity chromatography and association with the enzymes. Arch. Biochem. Biophys. 232, 127-134
    • (1984) Arch. Biochem. Biophys. , vol.232 , pp. 127-134
    • Peanasky, R.J.1    Bentz, Y.2    Paulson, B.3    Graham, D.L.4    Babin, D.R.5
  • 64
    • 3042565155 scopus 로고    scopus 로고
    • Kinetics of the inhibition of neutrophil proteinases by recombinant elafin and pre-elafin (trappin-2) expressed in Pichia pastoris
    • Zani, M. L., Nobar, S. M., Lacour, S. A., Lemoine, S., Boudier, C., Bieth, J. G., and Moreau, T. (2004) Kinetics of the inhibition of neutrophil proteinases by recombinant elafin and pre-elafin (trappin-2) expressed in Pichia pastoris. Eur. J. Biochem. 271, 2370-2378
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2370-2378
    • Zani, M.L.1    Nobar, S.M.2    Lacour, S.A.3    Lemoine, S.4    Boudier, C.5    Bieth, J.G.6    Moreau, T.7
  • 65
    • 0031826511 scopus 로고    scopus 로고
    • Variability of the canonical loop conformations in serine proteinases inhibitors and other proteins
    • Apostoluk, W., and Otlewski, J. (1998) Variability of the canonical loop conformations in serine proteinases inhibitors and other proteins. Proteins Struct. Funct. Genet. 32, 459-474
    • (1998) Proteins Struct. Funct. Genet. , vol.32 , pp. 459-474
    • Apostoluk, W.1    Otlewski, J.2


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