메뉴 건너뛰기




Volumn 112, Issue 11, 2003, Pages 1732-1740

The molecular basis for adhesion-mediated suppression of reactive oxygen species generation by human neutrophils

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATASE; INTEGRIN; OXIDIZING AGENT; PAK PROTEIN; PROTEIN; PROTEIN KINASE SYK; PROTEIN P47; PROTEIN P67; PROTEIN TYROSINE PHOSPHATASE; RAC2 PROTEIN; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; UNCLASSIFIED DRUG; VAV1 PROTEIN;

EID: 0346690398     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI19108     Document Type: Article
Times cited : (73)

References (47)
  • 1
    • 0025324376 scopus 로고
    • The human neutrophil respiratory burst oxidase
    • Clark, R.A. 1990. The human neutrophil respiratory burst oxidase. J. Infect. Dis. 161:1140-1147.
    • (1990) J. Infect. Dis. , vol.161 , pp. 1140-1147
    • Clark, R.A.1
  • 2
    • 0028556421 scopus 로고
    • Neutrophils, host defense, and inflammation: A double-edged sword
    • Smith, J.A. 1994. Neutrophils, host defense, and inflammation: a double-edged sword. J. Leukoc. Biol. 56:672-686.
    • (1994) J. Leukoc. Biol. , vol.56 , pp. 672-686
    • Smith, J.A.1
  • 3
    • 0023484511 scopus 로고
    • Neutrophil activation on biological surfaces. Massive secretion of hydrogen peroxide in response to products of macrophages and lymphocytes
    • Nathan, C.F. 1987. Neutrophil activation on biological surfaces. Massive secretion of hydrogen peroxide in response to products of macrophages and lymphocytes. J. Clin. Invest. 80:1550-1560.
    • (1987) J. Clin. Invest. , vol.80 , pp. 1550-1560
    • Nathan, C.F.1
  • 4
    • 0024595405 scopus 로고
    • Respiratory burst in adherent human neutrophils: Triggering by colony-stimulating factors CSF-GM and CSF-G
    • Nathan, C.F. 1989. Respiratory burst in adherent human neutrophils: triggering by colony-stimulating factors CSF-GM and CSF-G. Blood. 73:301-306.
    • (1989) Blood , vol.73 , pp. 301-306
    • Nathan, C.F.1
  • 5
    • 0024444326 scopus 로고
    • Cytokine-induced respiratory burst of human neutrophils: Dependence on extracellular matrix proteins and CD11/CD18 integrins
    • Nathan, C., et al. 1989. Cytokine-induced respiratory burst of human neutrophils: dependence on extracellular matrix proteins and CD11/CD18 integrins. J. Cell Biol. 109:1341-1349.
    • (1989) J. Cell Biol. , vol.109 , pp. 1341-1349
    • Nathan, C.1
  • 6
    • 0025219115 scopus 로고
    • Mac-1 (CD11b/CD18) mediates adherence-dependent hydrogen peroxide production by human and canine neutrophils
    • Shappell, S.B., et al. 1990. Mac-1 (CD11b/CD18) mediates adherence-dependent hydrogen peroxide production by human and canine neutrophils. J. Immunol. 144:2702-2711.
    • (1990) J. Immunol. , vol.144 , pp. 2702-2711
    • Shappell, S.B.1
  • 7
    • 0029609732 scopus 로고
    • Cross-linking of CD18 primes human neutrophils for activation of the respiratory burst in response to specific stimuli: Implications for adhesion-dependent physiological responses in neutrophils
    • Liles, W.C., Ledbetter, J.A., Waltersdorph, A.W., and Klebanoff, S.J. 1995. Cross-linking of CD18 primes human neutrophils for activation of the respiratory burst in response to specific stimuli: implications for adhesion-dependent physiological responses in neutrophils. J. Leukoc. Biol. 58:690-697.
    • (1995) J. Leukoc. Biol. , vol.58 , pp. 690-697
    • Liles, W.C.1    Ledbetter, J.A.2    Waltersdorph, A.W.3    Klebanoff, S.J.4
  • 8
    • 0030588684 scopus 로고    scopus 로고
    • Mechanisms of stimulation of the respiratory burst by TNF in nonadherent neutrophils: Its independence of lipidic transmembrane signaling and dependence on protein tyrosine phosphorylation and cytoskeleton
    • Dusi, S., Della Bianca, V., Donini, M., Nadalini, K.A., and Rossi, F. 1996. Mechanisms of stimulation of the respiratory burst by TNF in nonadherent neutrophils: its independence of lipidic transmembrane signaling and dependence on protein tyrosine phosphorylation and cytoskeleton. J. Immunol. 157:4615-4623.
    • (1996) J. Immunol. , vol.157 , pp. 4615-4623
    • Dusi, S.1    Della Bianca, V.2    Donini, M.3    Nadalini, K.A.4    Rossi, F.5
  • 10
    • 0036710445 scopus 로고    scopus 로고
    • The superoxide-generating NADPH oxidase: Structural aspects and activation mechanism
    • Vignais, P.V. 2002. The superoxide-generating NADPH oxidase: structural aspects and activation mechanism. Cell. Mol. Life Sci. 59:1428-1459.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1428-1459
    • Vignais, P.V.1
  • 11
    • 0029080863 scopus 로고
    • Dissociation of Rac translocation from p47phox/p67phox movements in human neutrophils by tyrosine kinase inhibitors
    • Dorseuil, O., Quinn, M.T., and Bokoch, G.M. 1995. Dissociation of Rac translocation from p47phox/p67phox movements in human neutrophils by tyrosine kinase inhibitors. J. Leukoc. Biol. 58:108-113.
    • (1995) J. Leukoc. Biol. , vol.58 , pp. 108-113
    • Dorseuil, O.1    Quinn, M.T.2    Bokoch, G.M.3
  • 12
    • 0028151013 scopus 로고
    • Rac translocates independently of the neutrophil NADPH oxidase components p47phox and p67phox. Evidence for its interaction with flavocytochrome b558
    • Heyworth, P.G., Bohl, B.P., Bokoch, G.M., and Curnutte, J.T. 1994. Rac translocates independently of the neutrophil NADPH oxidase components p47phox and p67phox. Evidence for its interaction with flavocytochrome b558. J. Biol. Chem. 269:30749-30752.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30749-30752
    • Heyworth, P.G.1    Bohl, B.P.2    Bokoch, G.M.3    Curnutte, J.T.4
  • 13
    • 0033609785 scopus 로고    scopus 로고
    • Tetratricopeptide repeat (TPR) motifs of p67(phox) participate in interaction with the small GTPase Rac and activation of the phagocyte NADPH oxidase
    • Koga, H., et al. 1999. Tetratricopeptide repeat (TPR) motifs of p67(phox) participate in interaction with the small GTPase Rac and activation of the phagocyte NADPH oxidase. J. Biol. Chem. 274:25051-25060.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25051-25060
    • Koga, H.1
  • 14
    • 0033635228 scopus 로고    scopus 로고
    • Structure of the TPR domain of p67phox in complex with Rac
    • Lapouge, K., et al. 2000. Structure of the TPR domain of p67phox in complex with Rac. GTP. Mol. Cell. 6:899-907.
    • (2000) GTP. Mol. Cell , vol.6 , pp. 899-907
    • Lapouge, K.1
  • 15
    • 0035293023 scopus 로고    scopus 로고
    • Molecular basis for Rac2 regulation of phagocyte NADPH oxidase
    • Diebold, B.A., and Bokoch, G.M. 2001. Molecular basis for Rac2 regulation of phagocyte NADPH oxidase. Nat. Immunol. 2:211-215.
    • (2001) Nat. Immunol. , vol.2 , pp. 211-215
    • Diebold, B.A.1    Bokoch, G.M.2
  • 16
    • 0020642791 scopus 로고
    • Assay of H2O2 production by macrophages and neutrophils with homovanillic acid and horse-radish peroxidase
    • Ruch, W., Cooper, P.H., and Baggiolini, M. 1983. Assay of H2O2 production by macrophages and neutrophils with homovanillic acid and horse-radish peroxidase. J. Immunol. Methods. 63:347-357.
    • (1983) J. Immunol. Methods , vol.63 , pp. 347-357
    • Ruch, W.1    Cooper, P.H.2    Baggiolini, M.3
  • 17
    • 0036898598 scopus 로고    scopus 로고
    • Spatial and temporal analysis of Rac activation during live neutrophil chemotaxis
    • Gardiner, E.M., et al. 2002. Spatial and temporal analysis of Rac activation during live neutrophil chemotaxis. Curr. Biol. 12:2029-2034.
    • (2002) Curr. Biol. , vol.12 , pp. 2029-2034
    • Gardiner, E.M.1
  • 18
    • 0033531955 scopus 로고    scopus 로고
    • Characterization of rac and cdc42 activation in chemoattractant-stimulated human neutrophils using a novel assay for active GTPases
    • Benard, V., Bohl, B.P., and Bokoch, G.M. 1999. Characterization of rac and cdc42 activation in chemoattractant-stimulated human neutrophils using a novel assay for active GTPases. J. Biol. Chem. 274:13198-13204.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13198-13204
    • Benard, V.1    Bohl, B.P.2    Bokoch, G.M.3
  • 19
    • 0027520431 scopus 로고
    • Translocation of Rac correlates with NADPH oxidase activation. Evidence for equimolar translocation of oxidase components
    • Quinn, M.T., Evans, T., Loetterle, L.R., Jesaitis, A.J., and Bokoch, G.M. 1993. Translocation of Rac correlates with NADPH oxidase activation. Evidence for equimolar translocation of oxidase components. J. Biol. Chem. 268:20983-20987.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20983-20987
    • Quinn, M.T.1    Evans, T.2    Loetterle, L.R.3    Jesaitis, A.J.4    Bokoch, G.M.5
  • 20
    • 0029780095 scopus 로고    scopus 로고
    • The renaturable 69- and 63-kDa protein kinases that undergo rapid activation in chemoattractant-stimulated guinea pig neutrophils are p21-activated kinases
    • Ding, J. Knaus, U.G., Lian, J.P., Bokoch, G.M., and Badwey, J.A. 1996. The renaturable 69- and 63-kDa protein kinases that undergo rapid activation in chemoattractant-stimulated guinea pig neutrophils are p21-activated kinases. J. Biol. Chem. 271:24869-24873.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24869-24873
    • Ding, J.1    Knaus, U.G.2    Lian, J.P.3    Bokoch, G.M.4    Badwey, J.A.5
  • 21
    • 0030772657 scopus 로고    scopus 로고
    • Localization of p21-activated kinase 1 (PAK1) to pinocytic vesicles and cortical actin structures in stimulated cells
    • Dharmawardhane, S., Sanders, L.C., Martin, S.S., Daniels, R.H., and Bokoch, G.M. 1997. Localization of p21-activated kinase 1 (PAK1) to pinocytic vesicles and cortical actin structures in stimulated cells. J. Cell Biol. 138:1265-1278.
    • (1997) J. Cell Biol. , vol.138 , pp. 1265-1278
    • Dharmawardhane, S.1    Sanders, L.C.2    Martin, S.S.3    Daniels, R.H.4    Bokoch, G.M.5
  • 22
    • 0028081350 scopus 로고
    • Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins
    • Bokoch, G.M., Bohl, B.P., and Chuang, T.H. 1994. Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins. J. Biol. Chem. 269:31674-31679.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31674-31679
    • Bokoch, G.M.1    Bohl, B.P.2    Chuang, T.H.3
  • 23
    • 0027467339 scopus 로고
    • Requirement for posttranslational processing of Rac GTP-binding proteins for activation of human neutrophil NADPH oxidase
    • Heyworth, P.G., et al. 1993. Requirement for posttranslational processing of Rac GTP-binding proteins for activation of human neutrophil NADPH oxidase. Mol. Biol. Cell. 4:261-269.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 261-269
    • Heyworth, P.G.1
  • 24
    • 0026542401 scopus 로고
    • Generation of signals activating neutrophil functions by leukocyte integrins: LFA-1 and gp150/95, but not CR3, are able to stimulate the respiratory burst of human neutrophils
    • Berton, G., Laudanna, C., Sorio, C., and Rossi, F. 1992. Generation of signals activating neutrophil functions by leukocyte integrins: LFA-1 and gp150/95, but not CR3, are able to stimulate the respiratory burst of human neutrophils. J. Cell Biol. 116:1007-1017.
    • (1992) J. Cell Biol. , vol.116 , pp. 1007-1017
    • Berton, G.1    Laudanna, C.2    Sorio, C.3    Rossi, F.4
  • 25
    • 0030008394 scopus 로고    scopus 로고
    • Deficiency of Src family kinases p59/61hck and p58c-fgr results in defective adhesion-dependent neutrophil functions
    • Lowell, C.A., Fumagalli, L., and Berton, G. 1996. Deficiency of Src family kinases p59/61hck and p58c-fgr results in defective adhesion-dependent neutrophil functions. J. Cell Biol. 133:895-910.
    • (1996) J. Cell Biol. , vol.133 , pp. 895-910
    • Lowell, C.A.1    Fumagalli, L.2    Berton, G.3
  • 26
    • 0025092134 scopus 로고
    • Inhibitors of the leukocyte superoxide generating oxidase: Mechanisms of action and methods for their elucidation
    • Cross, A.R. 1990. Inhibitors of the leukocyte superoxide generating oxidase: mechanisms of action and methods for their elucidation. Free Radic. Biol. Med. 8:71-93.
    • (1990) Free Radic. Biol. Med. , vol.8 , pp. 71-93
    • Cross, A.R.1
  • 27
    • 0026520888 scopus 로고
    • Isoprenoid metabolism is required for stimulation of the respiratory burst oxidase of HL-60 cells
    • Bokoch, G.M., and Prossnitz, V. 1992. Isoprenoid metabolism is required for stimulation of the respiratory burst oxidase of HL-60 cells. J. Clin. Invest. 89:402-408.
    • (1992) J. Clin. Invest. , vol.89 , pp. 402-408
    • Bokoch, G.M.1    Prossnitz, V.2
  • 28
    • 0037166293 scopus 로고    scopus 로고
    • Rac activation induces NADPH oxidase activity in transgenic COSphox cells, and the level of superoxide production is exchange factor-dependent
    • Price, M.O., Atkinson, S.J., Knaus, U.G., and Dinauer, M.C. 2002. Rac activation induces NADPH oxidase activity in transgenic COSphox cells, and the level of superoxide production is exchange factor-dependent. J. Biol. Chem. 277:19220-19228.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19220-19228
    • Price, M.O.1    Atkinson, S.J.2    Knaus, U.G.3    Dinauer, M.C.4
  • 29
    • 0037155727 scopus 로고    scopus 로고
    • P-Rex1, a PtdIns(3,4,5)P3- and Gbetagamma-regulated guanine-nucleotide exchange factor for Rac
    • Welch, H.C., et al. 2002. P-Rex1, a PtdIns(3,4,5)P3- and Gbetagamma-regulated guanine-nucleotide exchange factor for Rac. Cell. 108:809-821.
    • (2002) Cell , vol.108 , pp. 809-821
    • Welch, H.C.1
  • 30
    • 0032481142 scopus 로고    scopus 로고
    • Identification of a novel integrin signaling pathway involving the kinase Syk and the guanine nucleotide exchange factor Vav1
    • Miranti, C.K., Leng, L., Maschberger, P., Brugge, J.S., and Shattil, S.J. 1998. Identification of a novel integrin signaling pathway involving the kinase Syk and the guanine nucleotide exchange factor Vav1. Curr. Biol. 8:1289-1299.
    • (1998) Curr. Biol. , vol.8 , pp. 1289-1299
    • Miranti, C.K.1    Leng, L.2    Maschberger, P.3    Brugge, J.S.4    Shattil, S.J.5
  • 31
    • 0033847105 scopus 로고    scopus 로고
    • Vav family proteins couple to diverse cell surface receptors
    • Moores, S.L., et al. 2000. Vav family proteins couple to diverse cell surface receptors. Mol. Cell. Biol. 20:6364-6373.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6364-6373
    • Moores, S.L.1
  • 32
    • 0034269240 scopus 로고    scopus 로고
    • Structural basis for relief of autoinhibition of the Dbl homology domain of proto-oncogene Vav by tyrosine phosphorylation
    • Aghazadeh, B., Lowry, W.E., Huang, X.Y., and Rosen, M.K. 2000. Structural basis for relief of autoinhibition of the Dbl homology domain of proto-oncogene Vav by tyrosine phosphorylation. Cell. 102:625-633.
    • (2000) Cell , vol.102 , pp. 625-633
    • Aghazadeh, B.1    Lowry, W.E.2    Huang, X.Y.3    Rosen, M.K.4
  • 33
    • 0021927439 scopus 로고
    • Antiadhesive properties of biological surfaces are protective against stimulated granulocytes
    • Fehr, J., Moser, R., Leppert, D., and Groscurth, P. 1985. Antiadhesive properties of biological surfaces are protective against stimulated granulocytes. J. Clin. Invest. 76:535-542.
    • (1985) J. Clin. Invest. , vol.76 , pp. 535-542
    • Fehr, J.1    Moser, R.2    Leppert, D.3    Groscurth, P.4
  • 34
    • 0037108109 scopus 로고    scopus 로고
    • Current molecular models for NADPH oxidase regulation by Rac GTPase
    • Bokoch, G.M., and Diebold, B.A. 2002. Current molecular models for NADPH oxidase regulation by Rac GTPase. Blood. 100:2692-2696.
    • (2002) Blood , vol.100 , pp. 2692-2696
    • Bokoch, G.M.1    Diebold, B.A.2
  • 35
    • 0034256024 scopus 로고    scopus 로고
    • Signaling networks linking integrins and rho family GTPases
    • Schwartz, M.A., and Shattil, S.J. 2000. Signaling networks linking integrins and rho family GTPases. Trends Biochem. Sci. 25:388-391.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 388-391
    • Schwartz, M.A.1    Shattil, S.J.2
  • 36
    • 0027442667 scopus 로고
    • Biologically active lipids are regulators of Rac. GDI complexation
    • Chuang, T.H., Bohl, B.P., and Bokoch, G.M. 1993. Biologically active lipids are regulators of Rac. GDI complexation. J. Biol. Chem. 268:26206-26211.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26206-26211
    • Chuang, T.H.1    Bohl, B.P.2    Bokoch, G.M.3
  • 37
    • 0029164237 scopus 로고
    • Integrin transmembrane signaling and cytoskeletal control
    • Yamada, K.M., and Miyamoto, S. 1995. Integrin transmembrane signaling and cytoskeletal control. Curr. Opin. Cell Biol. 7:681-689.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 681-689
    • Yamada, K.M.1    Miyamoto, S.2
  • 38
    • 0032572557 scopus 로고    scopus 로고
    • Integrin-mediated signals regulated by members of the rho family of GTPases
    • Clark, E.A., King, W.G., Brugge, J.S., Symons, M., and Hynes, R.O. 1998., Integrin-mediated signals regulated by members of the rho family of GTPases. J. Cell Biol. 142:573-586.
    • (1998) J. Cell Biol. , vol.142 , pp. 573-586
    • Clark, E.A.1    King, W.G.2    Brugge, J.S.3    Symons, M.4    Hynes, R.O.5
  • 39
    • 0031844821 scopus 로고    scopus 로고
    • Activation of Rac and Cdc42 by integrins mediates cell spreading
    • Price, L.S., Leng, J., Schwartz, M.A., and Bokoch, G.M. 1998. Activation of Rac and Cdc42 by integrins mediates cell spreading. Mol. Biol. Cell. 9:1863-1871.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1863-1871
    • Price, L.S.1    Leng, J.2    Schwartz, M.A.3    Bokoch, G.M.4
  • 40
    • 0033081753 scopus 로고    scopus 로고
    • Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton
    • Ren, X.D., Kiosses, W.B., and Schwartz, M.A. 1999. Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 18:578-585.
    • (1999) EMBO J. , vol.18 , pp. 578-585
    • Ren, X.D.1    Kiosses, W.B.2    Schwartz, M.A.3
  • 41
    • 0038175548 scopus 로고    scopus 로고
    • Overexpression of WISP-1 down-regulated motility and invasion of lung cancer cells through inhibition of Rac activation
    • Soon, L.L., et al. 2003. Overexpression of WISP-1 down-regulated motility and invasion of lung cancer cells through inhibition of Rac activation. J. Biol. Chem. 278:11465-11470.
    • (2003) J. Biol. Chem. , vol.278 , pp. 11465-11470
    • Soon, L.L.1
  • 42
    • 0037929688 scopus 로고    scopus 로고
    • Down-regulation of Rac activity during beta 2 integrin-mediated adhesion of human neutrophils
    • Dib, K., et al. 2003. Down-regulation of Rac activity during beta 2 integrin-mediated adhesion of human neutrophils. J. Biol. Chem. 278:24181-24188.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24181-24188
    • Dib, K.1
  • 43
    • 0037443465 scopus 로고    scopus 로고
    • Proline-rich tyrosine kinase 2 and rac activation by chemokine and integrin receptors controls NK cell transendothelial migration
    • Gismondi, A., et al. 2003. Proline-rich tyrosine kinase 2 and rac activation by chemokine and integrin receptors controls NK cell transendothelial migration. J. Immunol. 170:3065-3073.
    • (2003) J. Immunol. , vol.170 , pp. 3065-3073
    • Gismondi, A.1
  • 44
    • 0031022433 scopus 로고    scopus 로고
    • Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate
    • Huyer, G., et al. 1997. Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. J. Biol. Chem. 272:843-851.
    • (1997) J. Biol. Chem. , vol.272 , pp. 843-851
    • Huyer, G.1
  • 45
    • 0032476646 scopus 로고    scopus 로고
    • Impaired integrin-mediated adhesion and signaling in fibroblasts expressing a dominant-negative mutant PTP1B
    • Arregui, C.O., Balsamo, J., and Lilien, J. 1998. Impaired integrin-mediated adhesion and signaling in fibroblasts expressing a dominant-negative mutant PTP1B. J. Cell Biol. 143:861-873.
    • (1998) J. Cell Biol. , vol.143 , pp. 861-873
    • Arregui, C.O.1    Balsamo, J.2    Lilien, J.3
  • 46
    • 0037113097 scopus 로고    scopus 로고
    • PTP-PEST controls motility through regulation of Rac1
    • Sastry, S.K., Lyons, P.D., Schaller, M.D., and Burridge, K. 2002. PTP-PEST controls motility through regulation of Rac1. J. Cell Sci. 115:4305-4316.
    • (2002) J. Cell Sci. , vol.115 , pp. 4305-4316
    • Sastry, S.K.1    Lyons, P.D.2    Schaller, M.D.3    Burridge, K.4
  • 47
    • 0028231065 scopus 로고
    • Adhesion molecules and inflammatory injury
    • Albelda, S.M., Smith, C.W., and Ward, P.A. 1994. Adhesion molecules and inflammatory injury. FASEB J. 8:504-512.
    • (1994) FASEB J. , vol.8 , pp. 504-512
    • Albelda, S.M.1    Smith, C.W.2    Ward, P.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.