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Volumn 21, Issue 9, 2003, Pages 1063-1068

Engineering of a macromolecular scaffold to develop specific protease inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; MACROMOLECULES;

EID: 0042861481     PISSN: 10870156     EISSN: None     Source Type: Journal    
DOI: 10.1038/nbt860     Document Type: Article
Times cited : (55)

References (49)
  • 1
    • 0003115709 scopus 로고    scopus 로고
    • Introduction: Family S1 of trypsin
    • (eds. Barrett, A.J., Rawlings, N.D. & Woessner, J.F.) (Academic Press, London, UK)
    • Rawlings, N.D. Introduction: family S1 of trypsin. in Handbook of Proteolytic Enzymes (eds. Barrett, A.J., Rawlings, N.D. & Woessner, J.F.) 5-12 (Academic Press, London, UK, 1998).
    • (1998) Handbook of Proteolytic Enzymes , pp. 5-12
    • Rawlings, N.D.1
  • 3
    • 0037298739 scopus 로고    scopus 로고
    • Quantification of membrane type serine protease 1 (MT-SP1) in transformed and normal cells
    • Bhatt, A.S. et al. Quantification of membrane type serine protease 1 (MT-SP1) in transformed and normal cells. Biol. Chem. 384, 257-266 (2003).
    • (2003) Biol. Chem. , vol.384 , pp. 257-266
    • Bhatt, A.S.1
  • 4
    • 0035846933 scopus 로고    scopus 로고
    • Type II transmembrane serine proteases. Insights into an emerging class of cell surface proteolytic enzymes
    • Hooper, J.D., Clements, J.A., Quigley, J.P. & Antalis, T.M. Type II transmembrane serine proteases. Insights into an emerging class of cell surface proteolytic enzymes. J. Biol. Chem. 276, 857-860 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 857-860
    • Hooper, J.D.1    Clements, J.A.2    Quigley, J.P.3    Antalis, T.M.4
  • 5
    • 0036661263 scopus 로고    scopus 로고
    • Human tissue kallikreins: A new enzymatic cascade pathway?
    • Yousef, G.M. & Diamandis, E.P. Human tissue kallikreins: a new enzymatic cascade pathway? Biol. Chem. 383, 1045-1057 (2002).
    • (2002) Biol. Chem. , vol.383 , pp. 1045-1057
    • Yousef, G.M.1    Diamandis, E.P.2
  • 6
    • 0033613123 scopus 로고    scopus 로고
    • Reverse biochemistry: Use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue
    • Takeuchi, T., Shuman, M.A. & Craik, C.S. Reverse biochemistry: use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue. Proc. Natl. Acad. Sci. USA 96, 11054-11061 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11054-11061
    • Takeuchi, T.1    Shuman, M.A.2    Craik, C.S.3
  • 7
    • 0033603574 scopus 로고    scopus 로고
    • Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity
    • Lin, C.Y., Anders, J., Johnson, M., Sang, Q.A. & Dickson, R.B. Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity. J. Biol. Chem. 274, 18231-18236 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 18231-18236
    • Lin, C.Y.1    Anders, J.2    Johnson, M.3    Sang, Q.A.4    Dickson, R.B.5
  • 8
    • 0032923230 scopus 로고    scopus 로고
    • Cloning and chromosomal mapping of a gene isolated from thymic stromal cells encoding a new mouse type II membrane serine protease, epithin, containing four LDL receptor modules and two CUB domains
    • Kim, M.G. et al. Cloning and chromosomal mapping of a gene isolated from thymic stromal cells encoding a new mouse type II membrane serine protease, epithin, containing four LDL receptor modules and two CUB domains. Immunogenetics 49, 420-428 (1999).
    • (1999) Immunogenetics , vol.49 , pp. 420-428
    • Kim, M.G.1
  • 9
    • 0036554846 scopus 로고    scopus 로고
    • Expression of the serine protease matriptase and its inhibitor HAI-1 in epithelial ovarian cancer: Correlation with clinical outcome and tumor clinicopathological parameters
    • Oberst, M.D. et al. Expression of the serine protease matriptase and its inhibitor HAI-1 in epithelial ovarian cancer: correlation with clinical outcome and tumor clinicopathological parameters. Clin. Cancer Res. 8, 1101-1107 (2002).
    • (2002) Clin. Cancer Res. , vol.8 , pp. 1101-1107
    • Oberst, M.D.1
  • 10
    • 0037374303 scopus 로고    scopus 로고
    • Tissue microarray analysis of hepatocyte growth factor/Met pathway components reveals a role for Met, matriptase, and hepatocyte growth factor activator inhibitor 1 in the progression of node-negative breast cancer
    • Kang, J.Y. et al. Tissue microarray analysis of hepatocyte growth factor/Met pathway components reveals a role for Met, matriptase, and hepatocyte growth factor activator inhibitor 1 in the progression of node-negative breast cancer. Cancer Res. 63, 1101-1105 (2003).
    • (2003) Cancer Res. , vol.63 , pp. 1101-1105
    • Kang, J.Y.1
  • 11
    • 0035939903 scopus 로고    scopus 로고
    • Delineation of prognostic biomarkers in prostate cancer
    • Dhanasekaran, S.M. et al. Delineation of prognostic biomarkers in prostate cancer. Nature 412, 822-826 (2001).
    • (2001) Nature , vol.412 , pp. 822-826
    • Dhanasekaran, S.M.1
  • 12
    • 0025849053 scopus 로고
    • Measurement of prostate-specific antigen in serum as a screening test for prostate cancer
    • Catalona, W.J. et al. Measurement of prostate-specific antigen in serum as a screening test for prostate cancer. N. Engl. J. Med. 324, 1156-1161 (1991).
    • (1991) N. Engl. J. Med. , vol.324 , pp. 1156-1161
    • Catalona, W.J.1
  • 13
    • 18644361962 scopus 로고    scopus 로고
    • Immunofluorometric quantitation and histochemical localisation of kallikrein 6 protein in ovarian cancer tissue: A new independent unfavourable prognostic biomarker
    • Hoffman, B.R. et al. Immunofluorometric quantitation and histochemical localisation of kallikrein 6 protein in ovarian cancer tissue: a new independent unfavourable prognostic biomarker. Br. J. Cancer 87, 763-771 (2002).
    • (2002) Br. J. Cancer , vol.87 , pp. 763-771
    • Hoffman, B.R.1
  • 14
    • 0037161955 scopus 로고    scopus 로고
    • Matriptase/MT-SP1 is required for postnatal survival, epidermal barrier function, hair follicle development, and thymic homeostasis
    • List, K. et al. Matriptase/MT-SP1 is required for postnatal survival, epidermal barrier function, hair follicle development, and thymic homeostasis. Oncogene 21, 3765-3779 (2002).
    • (2002) Oncogene , vol.21 , pp. 3765-3779
    • List, K.1
  • 15
    • 0029083438 scopus 로고
    • Granzyme A-deficient mice retain potent cell-mediated cytotoxicity
    • Ebnet, K. et al. Granzyme A-deficient mice retain potent cell-mediated cytotoxicity. EMBO J. 14, 4230-4239 (1995).
    • (1995) EMBO J. , vol.14 , pp. 4230-4239
    • Ebnet, K.1
  • 16
    • 0033017497 scopus 로고    scopus 로고
    • Small, noncovalent serine protease inhibitors
    • Sanderson, P.E. Small, noncovalent serine protease inhibitors. Med. Res. Rev. 19, 179-197 (1999).
    • (1999) Med. Res. Rev. , vol.19 , pp. 179-197
    • Sanderson, P.E.1
  • 17
    • 0034628448 scopus 로고    scopus 로고
    • Protease inhibitors: Current status and future prospects
    • Leung, D., Abbenante, G. & Fairlie, D.P. Protease inhibitors: current status and future prospects. J. Med. Chem. 43, 305-341 (2000).
    • (2000) J. Med. Chem. , vol.43 , pp. 305-341
    • Leung, D.1    Abbenante, G.2    Fairlie, D.P.3
  • 18
    • 0027300523 scopus 로고
    • Crystal structures of rat anionic trypsin complexed with the protein inhibitors APPI and BPTI
    • Perona, J.J., Tsu, C.A., Craik, C.S. & Fletterick, R.J. Crystal structures of rat anionic trypsin complexed with the protein inhibitors APPI and BPTI. J. Mol. Biol. 230, 919-933 (1993).
    • (1993) J. Mol. Biol. , vol.230 , pp. 919-933
    • Perona, J.J.1    Tsu, C.A.2    Craik, C.S.3    Fletterick, R.J.4
  • 19
    • 0021112585 scopus 로고
    • Purification from Escherichia coli of a periplasmic protein that is a potent inhibitor of pancreatic proteases
    • Chung, C.H., Ives, H.E., Almeda, S. & Goldberg, A.L. Purification from Escherichia coli of a periplasmic protein that is a potent inhibitor of pancreatic proteases. J. Biol. Chem. 258, 11032-11038 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 11032-11038
    • Chung, C.H.1    Ives, H.E.2    Almeda, S.3    Goldberg, A.L.4
  • 20
    • 0034674167 scopus 로고    scopus 로고
    • Compromise and accommodation in ecotin, a dimeric macromolecular inhibitor of serine proteases
    • Gillmor, S.A., Takeuchi, T., Yang, S.Q., Craik, C.S. & Fletterick, R.J. Compromise and accommodation in ecotin, a dimeric macromolecular inhibitor of serine proteases. J. Mol. Biol. 299, 993-1003 (2000).
    • (2000) J. Mol. Biol. , vol.299 , pp. 993-1003
    • Gillmor, S.A.1    Takeuchi, T.2    Yang, S.Q.3    Craik, C.S.4    Fletterick, R.J.5
  • 21
    • 0028266885 scopus 로고
    • Macromolecular chelation as an improved mechanism of protease inhibition: Structure of the ecotin-trypsin complex
    • McGrath, M.E., Erpel, T., Bystroff, C. & Fletterick, R.J. Macromolecular chelation as an improved mechanism of protease inhibition: structure of the ecotin-trypsin complex. EMBO J. 13, 1502-1507 (1994).
    • (1994) EMBO J. , vol.13 , pp. 1502-1507
    • McGrath, M.E.1    Erpel, T.2    Bystroff, C.3    Fletterick, R.J.4
  • 22
    • 0035964276 scopus 로고    scopus 로고
    • Crystal structure of thrombin-ecotin reveals conformational changes and extended interactions
    • Wang, S.X., Esmon, C.T. & Fletterick, R.J. Crystal structure of thrombin-ecotin reveals conformational changes and extended interactions. Biochemistry 40, 10038-10046 (2001).
    • (2001) Biochemistry , vol.40 , pp. 10038-10046
    • Wang, S.X.1    Esmon, C.T.2    Fletterick, R.J.3
  • 23
  • 24
    • 0028269445 scopus 로고
    • Ecotin is a potent anticoagulant and reversible tight-binding inhibitor of Factor Xa
    • Seymour, J.L. et al. Ecotin is a potent anticoagulant and reversible tight-binding inhibitor of Factor Xa. Biochemistry 33, 3949-3958 (1994).
    • (1994) Biochemistry , vol.33 , pp. 3949-3958
    • Seymour, J.L.1
  • 25
    • 0029025751 scopus 로고
    • Ecotin is a potent inhibitor of the contact system proteases Factor XIIa and plasma kallikrein
    • Ulmer, J.S., Lindquist, R.N., Dennis, M.S. & Lazarus, R.A. Ecotin is a potent inhibitor of the contact system proteases Factor XIIa and plasma kallikrein. FEBS Lett. 365, 159-163 (1995).
    • (1995) FEBS Lett. , vol.365 , pp. 159-163
    • Ulmer, J.S.1    Lindquist, R.N.2    Dennis, M.S.3    Lazarus, R.A.4
  • 26
    • 0030830360 scopus 로고    scopus 로고
    • Contact system: A vascular biology modulator with anticoagulant, profibrinolytic, antiadhesive, and proinflammatory attributes
    • Colman, R.W. & Schmaier, A.H. Contact system: a vascular biology modulator with anticoagulant, profibrinolytic, antiadhesive, and proinflammatory attributes. Blood 90, 3819-3843 (1997).
    • (1997) Blood , vol.90 , pp. 3819-3843
    • Colman, R.W.1    Schmaier, A.H.2
  • 27
    • 0035095955 scopus 로고    scopus 로고
    • A plasma kallikrein-dependent plasminogen cascade required for adipocyte differentiation
    • Selvarajan, S., Lund, L.R., Takeuchi, T., Craik, C.S. & Werb, Z. A plasma kallikrein-dependent plasminogen cascade required for adipocyte differentiation. Nat. Cell Biol. 3, 267-275 (2001).
    • (2001) Nat. Cell Biol. , vol.3 , pp. 267-275
    • Selvarajan, S.1    Lund, L.R.2    Takeuchi, T.3    Craik, C.S.4    Werb, Z.5
  • 28
    • 0028921732 scopus 로고
    • Inhibition of plasma kallikrein prevents peptidoglycan-induced arthritis in the Lewis rat
    • Dela Cadena, R.A. et al. Inhibition of plasma kallikrein prevents peptidoglycan-induced arthritis in the Lewis rat. FASEB J. 9, 446-452 (1995).
    • (1995) FASEB J. , vol.9 , pp. 446-452
    • Dela Cadena, R.A.1
  • 29
    • 0031930846 scopus 로고    scopus 로고
    • Specific inhibition of plasma kallikrein modulates chronic granulomatous intestinal and systemic inflammation in genetically susceptible rats
    • Stadnicki, A. et al. Specific inhibition of plasma kallikrein modulates chronic granulomatous intestinal and systemic inflammation in genetically susceptible rats. FASEB J. 12, 325-333 (1998).
    • (1998) FASEB J. , vol.12 , pp. 325-333
    • Stadnicki, A.1
  • 30
    • 0028841350 scopus 로고
    • Potent and selective Kunitz domain inhibitors of plasma kallikrein designed by phage display
    • Dennis, M.S., Herzka, A. & Lazarus, R.A. Potent and selective Kunitz domain inhibitors of plasma kallikrein designed by phage display. J. Biol. Chem. 270, 25411-25417 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 25411-25417
    • Dennis, M.S.1    Herzka, A.2    Lazarus, R.A.3
  • 31
    • 0029894775 scopus 로고    scopus 로고
    • Iterative optimization of high-affinity protease inhibitors using phage display. 2. Plasma kallikrein and thrombin
    • Markland, W., Ley, A.C. & Ladner, R.C. Iterative optimization of high-affinity protease inhibitors using phage display. 2. Plasma kallikrein and thrombin. Biochemistry 35, 8058-8067 (1996).
    • (1996) Biochemistry , vol.35 , pp. 8058-8067
    • Markland, W.1    Ley, A.C.2    Ladner, R.C.3
  • 32
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer, W.P. Rapid evolution of a protein in vitro by DNA shuffling. Nature 370, 389-391 (1994).
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.1
  • 33
    • 0036901312 scopus 로고    scopus 로고
    • Synthetic shuffling expands functional protein diversity by allowing amino acids to recombine independently
    • Ness, J.E. et al. Synthetic shuffling expands functional protein diversity by allowing amino acids to recombine independently. Nat. Biotechnol. 20, 1251-1255 (2002).
    • (2002) Nat. Biotechnol. , vol.20 , pp. 1251-1255
    • Ness, J.E.1
  • 34
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan, A.A. & Thorn, K.S. Anatomy of hot spots in protein interfaces. J. Mol. Biol. 280, 1-9 (1998).
    • (1998) J. Mol. Biol. , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 35
    • 0032546736 scopus 로고    scopus 로고
    • Engineering bidentate macromolecular inhibitors for trypsin and urokinase-type plasminogen activator
    • Yang, S.Q. & Craik, C.S. Engineering bidentate macromolecular inhibitors for trypsin and urokinase-type plasminogen activator. J. Mol. Biol. 279, 1001-1011 (1998).
    • (1998) J. Mol. Biol. , vol.279 , pp. 1001-1011
    • Yang, S.Q.1    Craik, C.S.2
  • 36
    • 0037135561 scopus 로고    scopus 로고
    • Computer-assisted mutagenesis of ecotin to engineer its secondary binding site for urokinase inhibition
    • Laboissiere, M.C. et al. Computer-assisted mutagenesis of ecotin to engineer its secondary binding site for urokinase inhibition. J. Biol. Chem. 277, 26623-26631 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 26623-26631
    • Laboissiere, M.C.1
  • 37
    • 0038089976 scopus 로고    scopus 로고
    • Selection of chymotrypsin inhibitors from a conformationally-constrained combinatorial peptide library
    • McBride, J.D., Freeman, N., Domingo, G.J. & Leatherbarrow, R.J. Selection of chymotrypsin inhibitors from a conformationally-constrained combinatorial peptide library. J. Mol. Biol. 259, 819-827 (1996).
    • (1996) J. Mol. Biol. , vol.259 , pp. 819-827
    • McBride, J.D.1    Freeman, N.2    Domingo, G.J.3    Leatherbarrow, R.J.4
  • 38
    • 0028085530 scopus 로고
    • Kunitz domain inhibitors of tissue factor-Factor VIIa. I. Potent inhibitors selected from libraries by phage display
    • Dennis M.S. & Lazarus R.A. Kunitz domain inhibitors of tissue factor-Factor VIIa. I. Potent inhibitors selected from libraries by phage display. J. Biol. Chem. 269, 22129-22136 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 22129-22136
    • Dennis, M.S.1    Lazarus, R.A.2
  • 39
    • 0032546757 scopus 로고    scopus 로고
    • Ecotin: A serine protease inhibitor with two distinct and interacting binding sites
    • Yang, S.Q., Wang, C.I., Gillmor, S.A. Fletterick, R.J. & Craik C.S. Ecotin: a serine protease inhibitor with two distinct and interacting binding sites. J. Mol. Biol. 279, 945-957 (1998).
    • (1998) J. Mol. Biol. , vol.279 , pp. 945-957
    • Yang, S.Q.1    Wang, C.I.2    Gillmor, S.A.3    Fletterick, R.J.4    Craik, C.S.5
  • 40
    • 0031915891 scopus 로고    scopus 로고
    • Error analysis of chemically synthesized polynucleotides
    • Hecker, K.H. & Rill, R.L. Error analysis of chemically synthesized polynucleotides. Biotechniques 24, 256-260 (1998).
    • (1998) Biotechniques , vol.24 , pp. 256-260
    • Hecker, K.H.1    Rill, R.L.2
  • 41
    • 0023043187 scopus 로고
    • Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats
    • Chung, D.W., Fujikawa, K., McMullen, B.A. & Davie, E.W. Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats. Biochemistry 25, 2410-2417 (1986).
    • (1986) Biochemistry , vol.25 , pp. 2410-2417
    • Chung, D.W.1    Fujikawa, K.2    McMullen, B.A.3    Davie, E.W.4
  • 42
    • 0033528281 scopus 로고    scopus 로고
    • Effects of recombinant hirudin (lepirudin) compared with heparin on death, myocardial infarction, refractory angina, and revascularisation procedures in patients with acute myocardial ischaemia without ST elevation: A randomised trial
    • OASIS investigators. Effects of recombinant hirudin (lepirudin) compared with heparin on death, myocardial infarction, refractory angina, and revascularisation procedures in patients with acute myocardial ischaemia without ST elevation: a randomised trial. Lancet 353, 429-438 (1999).
    • (1999) Lancet , vol.353 , pp. 429-438
  • 43
    • 0029014045 scopus 로고
    • Ancylostoma caninum anticoagulant peptide: A hookworm-derived inhibitor of human coagulation Factor Xa
    • Cappello, M., Vlasuk, G.P., Bergum, P.W., Huang, S. & Hotez, P.J. Ancylostoma caninum anticoagulant peptide: a hookworm-derived inhibitor of human coagulation Factor Xa. Proc. Natl. Acad. Sci. USA 92, 6152-6156 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6152-6156
    • Cappello, M.1    Vlasuk, G.P.2    Bergum, P.W.3    Huang, S.4    Hotez, P.J.5
  • 44
    • 0034663308 scopus 로고    scopus 로고
    • Recombinant staphylokinase variants with reduced antigenicity due to elimination of B-lymphocyte epitopes
    • Laroche, Y. et al. Recombinant staphylokinase variants with reduced antigenicity due to elimination of B-lymphocyte epitopes. Blood 96, 1425-1432 (2000).
    • (2000) Blood , vol.96 , pp. 1425-1432
    • Laroche, Y.1
  • 45
    • 0025838021 scopus 로고
    • Assembly of combinatorial antibody libraries on phage surfaces: The gene III site
    • Barbas, C.F., Kang, A.S., Lerner, R.A. & Benkovic, S.J. Assembly of combinatorial antibody libraries on phage surfaces: the gene III site. Proc. Natl. Acad. Sci. USA 88, 7978-7982 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7978-7982
    • Barbas, C.F.1    Kang, A.S.2    Lerner, R.A.3    Benkovic, S.J.4
  • 46
    • 0034283566 scopus 로고    scopus 로고
    • High-density mutagenesis by combined DNA shuffling and phage display to assign essential amino acid residues in protein-protein interactions: Application to study structure-function of plasminogen activation inhibitor 1 (PAI-I)
    • Stoop, A.A., Jespers, L., Lasters, I., Eldering, E. & Pannekoek, H. High-density mutagenesis by combined DNA shuffling and phage display to assign essential amino acid residues in protein-protein interactions: application to study structure-function of plasminogen activation inhibitor 1 (PAI-I). J. Mol. Biol. 301, 1135-1147 (2000).
    • (2000) J. Mol. Biol. , vol.301 , pp. 1135-1147
    • Stoop, A.A.1    Jespers, L.2    Lasters, I.3    Eldering, E.4    Pannekoek, H.5
  • 47
    • 0014454095 scopus 로고
    • Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors
    • Morrison, J.F. Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors. Biochim. Biophys. Acta 185, 269-286 (1969).
    • (1969) Biochim. Biophys. Acta , vol.185 , pp. 269-286
    • Morrison, J.F.1
  • 48
    • 0026244229 scopus 로고
    • MolScript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. MolScript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 49
    • 0023043178 scopus 로고
    • Aminoacid sequence of human Factor XI, a blood coagulation factor with four tandem repeats that are highly homologous with plasma prekallikrein
    • Fujikawa, K., Chung, D.W., Hendrickson L.E. & Davie, E.W. Aminoacid sequence of human Factor XI, a blood coagulation factor with four tandem repeats that are highly homologous with plasma prekallikrein. Biochemistry 25, 2417-2424 (1986).
    • (1986) Biochemistry , vol.25 , pp. 2417-2424
    • Fujikawa, K.1    Chung, D.W.2    Hendrickson, L.E.3    Davie, E.W.4


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