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Volumn 19, Issue 7, 1999, Pages 5061-5072

Domain swapping used to investigate the mechanism of protein kinase B regulation by 3-phosphoinositide-dependent protein kinase 1 and Ser473 kinase

Author keywords

[No Author keywords available]

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; PHORBOL 13 ACETATE 12 MYRISTATE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOPEPTIDE; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN KINASE; PROTEIN KINASE B; PROTEIN KINASE C; SERINE; THREONINE;

EID: 0033043389     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.19.7.5061     Document Type: Article
Times cited : (102)

References (58)
  • 2
    • 0031127305 scopus 로고    scopus 로고
    • Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα
    • Alessi, D. R., S. R. James, C. P. Downes, A. B. Holmes, P. R. J. Gaffney, C. Reese, and P. Cohen. 1997. Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα. Curr. Biol. 7:261-269.
    • (1997) Curr. Biol. , vol.7 , pp. 261-269
    • Alessi, D.R.1    James, S.R.2    Downes, C.P.3    Holmes, A.B.4    Gaffney, P.R.J.5    Reese, C.6    Cohen, P.7
  • 4
    • 0024394549 scopus 로고
    • Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile-acid biosynthetic enzyme
    • Andersson, S., D. N. Davie, H. Dahlbäck, H. Jörnvall, and D. W. Russell. 1989. Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile-acid biosynthetic enzyme. J. Biol. Chem. 264:8222-8229.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8222-8229
    • Andersson, S.1    Davie, D.N.2    Dahlbäck, H.3    Jörnvall, H.4    Russell, D.W.5
  • 5
    • 0029942186 scopus 로고    scopus 로고
    • Activation and phosphorylation of a pleckstrin homology domain-containing protein-kinase (RAC-PK/PKB) promoted by serum and protein-phosphatase inhibitors
    • Andjelković, M., T. Jakubowicz, P. Cron, X.-F. Ming, J. H. Han, and B. A. Hemmings. 1996. Activation and phosphorylation of a pleckstrin homology domain-containing protein-kinase (RAC-PK/PKB) promoted by serum and protein-phosphatase inhibitors. Proc. Natl. Acad. Sci. USA 93:5699-5704.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5699-5704
    • Andjelković, M.1    Jakubowicz, T.2    Cron, P.3    Ming, X.-F.4    Han, J.H.5    Hemmings, B.A.6
  • 8
    • 0029856725 scopus 로고    scopus 로고
    • cAMP counter-regulates insulin-mediated protein phosphatase 2A inactivation in rat skeletal muscle cells
    • Begum, N., and L. Ragolia. 1996. cAMP counter-regulates insulin-mediated protein phosphatase 2A inactivation in rat skeletal muscle cells. J. Biol. Chem. 271:31166-31171.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31166-31171
    • Begum, N.1    Ragolia, L.2
  • 9
    • 0026095665 scopus 로고
    • A retroviral oncogene, akt, encoding a serine threonine kinase containing an SH2-like region
    • Bellacosa, A., J. R. Testa, S. P. Staal, and P. N. Tsichlis. 1991. A retroviral oncogene, akt, encoding a serine threonine kinase containing an SH2-like region. Science 254:274-277.
    • (1991) Science , vol.254 , pp. 274-277
    • Bellacosa, A.1    Testa, J.R.2    Staal, S.P.3    Tsichlis, P.N.4
  • 10
    • 0033515625 scopus 로고    scopus 로고
    • A human protein kinase Bγ with regulatory phosphorylation sites in the activation loop and in the C-terminal hydrophobic domain
    • Brodbeck, D., P. Cron, and B. A. Hemmings. 1999. A human protein kinase Bγ with regulatory phosphorylation sites in the activation loop and in the C-terminal hydrophobic domain. J. Biol. Chem. 274:9133-9136.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9133-9136
    • Brodbeck, D.1    Cron, P.2    Hemmings, B.A.3
  • 12
    • 0029160069 scopus 로고
    • Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
    • Burgering, B. M. T., and P. J. Coffer. 1995. Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature 376:599-602.
    • (1995) Nature , vol.376 , pp. 599-602
    • Burgering, B.M.T.1    Coffer, P.J.2
  • 13
    • 0023711798 scopus 로고
    • Calcium phosphate mediated gene transfer: A highly efficient transfection system for stably transforming cells with plasmid DNA
    • Chen, C., and H. Okayama. 1988. Calcium phosphate mediated gene transfer: a highly efficient transfection system for stably transforming cells with plasmid DNA. BioTechniques 6:632-638.
    • (1988) BioTechniques , vol.6 , pp. 632-638
    • Chen, C.1    Okayama, H.2
  • 14
    • 0033056079 scopus 로고    scopus 로고
    • Osmotic shock inhibits insulin signaling by maintaining Akt/protein kinase B in an inactive dephosphorylated state
    • Chen, D., R. V. Fucini, A. L. Olson, B. A. Hemmings, and J. E. Pessin. 1999. Osmotic shock inhibits insulin signaling by maintaining Akt/protein kinase B in an inactive dephosphorylated state. Mol. Cell. Biol. 19:4684-4694.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4684-4694
    • Chen, D.1    Fucini, R.V.2    Olson, A.L.3    Hemmings, B.A.4    Pessin, J.E.5
  • 15
    • 0032544011 scopus 로고    scopus 로고
    • Phosphorylation and activation of cAMP-dependent protein kinase by phosphoinositide-dependent protein kinase
    • Cheng, X., M. Yuliang, M. Moore, B. A. Hemmings, and S. S. Tailor. 1998. Phosphorylation and activation of cAMP-dependent protein kinase by phosphoinositide-dependent protein kinase. Proc. Natl. Acad. Sci. USA 95:9849-9854.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9849-9854
    • Cheng, X.1    Yuliang, M.2    Moore, M.3    Hemmings, B.A.4    Tailor, S.S.5
  • 16
    • 0026006501 scopus 로고
    • Molecular-cloning and characterization of a novel putative protein-serine kinase related to the cAMP-dependent and protein-kinase-C families
    • Coffer, P. J., and J. R. Woodgett. 1991. Molecular-cloning and characterization of a novel putative protein-serine kinase related to the cAMP-dependent and protein-kinase-C families. Eur. J. Biochem. 201:475-481.
    • (1991) Eur. J. Biochem. , vol.201 , pp. 475-481
    • Coffer, P.J.1    Woodgett, J.R.2
  • 17
    • 0029587224 scopus 로고
    • Inhibition of glycogen-synthase kinase-3 by insulin mediated by protein-kinase-B
    • Cross, D. A. E., D. R. Alessi, P. Cohen, M. Andjelković, and B. A. Hemmings. 1995. Inhibition of glycogen-synthase kinase-3 by insulin mediated by protein-kinase-B. Nature 378:785-789.
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.E.1    Alessi, D.R.2    Cohen, P.3    Andjelković, M.4    Hemmings, B.A.5
  • 18
    • 0032530482 scopus 로고    scopus 로고
    • Phosphoinositide-2-OH-kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase
    • Delcommene, M., C. Tan, V. Gray, L. Rue, J. Woodgett, and S. Dedhar. 1998. Phosphoinositide-2-OH-kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase. Proc. Natl. Acad. Sci. USA 95:11211-11216.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11211-11216
    • Delcommene, M.1    Tan, C.2    Gray, V.3    Rue, L.4    Woodgett, J.5    Dedhar, S.6
  • 20
    • 0032053709 scopus 로고    scopus 로고
    • Mechanisms and consequences of activation of protein kinase B/Akt
    • Downward, J. 1998. Mechanisms and consequences of activation of protein kinase B/Akt. Curr. Opin. Cell Biol. 10:262-267.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 262-267
    • Downward, J.1
  • 22
    • 0032973572 scopus 로고    scopus 로고
    • Protein kinase B localization and activation differentially affect S6 kinase activity and eukaryotic transcription initiation factor 4E-binding protein 1 phosphorylation
    • Dufner, A., M. Andjelković, B. M. T. Burgering, B. A. Hemmings, and G. Thomas. Protein kinase B localization and activation differentially affect S6 kinase activity and eukaryotic transcription initiation factor 4E-binding protein 1 phosphorylation. Mol. Cell. Biol. 19:4525-4534.
    • Mol. Cell. Biol. , vol.19 , pp. 4525-4534
    • Dufner, A.1    Andjelković, M.2    Burgering, B.M.T.3    Hemmings, B.A.4    Thomas, G.5
  • 23
    • 0022494971 scopus 로고
    • Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose
    • Ellis, L., E. Clauser, D. O. Morgan, M. Edery, R. A. Roth, and W. J. Rutter. 1986. Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose. Cell 45:721-732.
    • (1986) Cell , vol.45 , pp. 721-732
    • Ellis, L.1    Clauser, E.2    Morgan, D.O.3    Edery, M.4    Roth, R.A.5    Rutter, W.J.6
  • 24
    • 0032518666 scopus 로고    scopus 로고
    • Activation of phospholipase Cγ by PI 3-kinase-induced PH domain-mediated membrane targeting
    • Falasca, M., S. K. Logan, V. P. Lehto, G. Baccante, M. A. Lemmon, and J. Schlessinger. 1998. Activation of phospholipase Cγ by PI 3-kinase-induced PH domain-mediated membrane targeting. EMBO J. 17:414-422.
    • (1998) EMBO J. , vol.17 , pp. 414-422
    • Falasca, M.1    Logan, S.K.2    Lehto, V.P.3    Baccante, G.4    Lemmon, M.A.5    Schlessinger, J.6
  • 25
    • 0029079275 scopus 로고
    • The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
    • Franke, T. F., S.-I. Yang, T. O. Chan, K. Datta, A. Kazlauskas, D. Morrison, D. R. Kaplan, and P. N. Tsichlis. 1995. The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell 81:727-736.
    • (1995) Cell , vol.81 , pp. 727-736
    • Franke, T.F.1    Yang, S.-I.2    Chan, T.O.3    Datta, K.4    Kazlauskas, A.5    Morrison, D.6    Kaplan, D.R.7    Tsichlis, P.N.8
  • 26
    • 0030991386 scopus 로고    scopus 로고
    • High affinity binding of inositol phosphates and phosphoinositides to the pleckstrin homology domain of RAC/protein kinase B and their influence on kinase activity
    • Frech, M., M. Andjelković, E. Ingley, K. K. Reddy, J. R. Falck, and B. A. Hemmings. 1997. High affinity binding of inositol phosphates and phosphoinositides to the pleckstrin homology domain of RAC/protein kinase B and their influence on kinase activity. J. Biol. Chem. 272:8474-8481.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8474-8481
    • Frech, M.1    Andjelković, M.2    Ingley, E.3    Reddy, K.K.4    Falck, J.R.5    Hemmings, B.A.6
  • 27
    • 85038151338 scopus 로고    scopus 로고
    • Mechanism of protein kinase B activation by insulin/IGF1 revealed by specific inhibitors of phosphoinositide 3-kinase - Significance for diabetes and cancer
    • in press
    • Galetić, I., M. Andjelković, R. Meier, D. Brodbeck, J. Park, and B. A. Hemmings. Mechanism of protein kinase B activation by insulin/IGF1 revealed by specific inhibitors of phosphoinositide 3-kinase - significance for diabetes and cancer. Pharmacol. Ther., in press.
    • Pharmacol. Ther.
    • Galetić, I.1    Andjelković, M.2    Meier, R.3    Brodbeck, D.4    Park, J.5    Hemmings, B.A.6
  • 28
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Harlow, E., and D. Lane. 1988. Antibodies: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 29
  • 30
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin, C. H. 1995. Dimerization of cell surface receptors in signal transduction. Cell 80:213-223.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 31
    • 0030993451 scopus 로고    scopus 로고
    • PH domains - A universal membrane adaptor
    • Hemmings, B. A. 1997. PH domains - a universal membrane adaptor. Science 275:1889.
    • (1997) Science , vol.275 , pp. 1889
    • Hemmings, B.A.1
  • 32
    • 0031053360 scopus 로고    scopus 로고
    • Akt signaling: Linking membrane events to life and death decisions
    • Hemmings, B. A. 1997. Akt signaling: linking membrane events to life and death decisions. Science 275:628-630.
    • (1997) Science , vol.275 , pp. 628-630
    • Hemmings, B.A.1
  • 33
    • 0030847535 scopus 로고    scopus 로고
    • 3 gets its message across
    • 3 gets its message across. Science 277:534.
    • (1997) Science , vol.277 , pp. 534
    • Hemmings, B.A.1
  • 34
    • 0020694766 scopus 로고
    • Relationship between mezerein-mediated biological responses and phorbol ester receptor occupancy
    • Jaken, S., M. A. Shupnik, P. M. Blumberg, and A. H. Tashjian, Jr. 1983. Relationship between mezerein-mediated biological responses and phorbol ester receptor occupancy. Cancer Res. 43:11-14.
    • (1983) Cancer Res. , vol.43 , pp. 11-14
    • Jaken, S.1    Shupnik, M.A.2    Blumberg, P.M.3    Tashjian A.H., Jr.4
  • 35
    • 0029993517 scopus 로고    scopus 로고
    • Specific binding of the AKT-1 protein kinase to phosphatidyl-inositol 3,4,5-trisphosphate without subsequent activation
    • James, S. R., C. P. Downes, R. Gigg, S. J. A. Grove, A. B. Holmes, and D. R. Alessi. 1996. Specific binding of the AKT-1 protein kinase to phosphatidyl-inositol 3,4,5-trisphosphate without subsequent activation. Biochem. J. 315: 709-713.
    • (1996) Biochem. J. , vol.315 , pp. 709-713
    • James, S.R.1    Downes, C.P.2    Gigg, R.3    Grove, S.J.A.4    Holmes, A.B.5    Alessi, D.R.6
  • 36
    • 0025882091 scopus 로고
    • Molecular cloning and identification of a serine threonine protein-kinase of the second messenger subfamily
    • Jones, P. F., T. Jakubowicz, F. J. Pitossi, F. Maurer, and B. A. Hemmings. 1991. Molecular cloning and identification of a serine threonine protein-kinase of the second messenger subfamily. Proc. Natl. Acad. Sci. USA 88: 4171-4175.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4171-4175
    • Jones, P.F.1    Jakubowicz, T.2    Pitossi, F.J.3    Maurer, F.4    Hemmings, B.A.5
  • 37
    • 0026270993 scopus 로고
    • Molecular cloning of a second form of rac protein kinase
    • Jones, P. F., T. Jakubowicz, and B. A. Hemmings. 1991. Molecular cloning of a second form of rac protein kinase. Cell Regul. 2:1001-1009.
    • (1991) Cell Regul. , vol.2 , pp. 1001-1009
    • Jones, P.F.1    Jakubowicz, T.2    Hemmings, B.A.3
  • 40
    • 0029908016 scopus 로고    scopus 로고
    • Expression of a constitutive active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation
    • Kohn, A. D., S. A. Summers, M. Birnbaum, and R. A. Roth. 1996. Expression of a constitutive active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation. J. Biol. Chem. 271: 31372-31378.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31372-31378
    • Kohn, A.D.1    Summers, S.A.2    Birnbaum, M.3    Roth, R.A.4
  • 42
    • 0028799420 scopus 로고
    • Molecular-cloning and characterization of a new member of the RAC protein-kinase family - Association of the pleckstrin homology domain of 3 types of RAC protein-kinase with protein-kinase-C subspecies and beta-gamma-subunits of G-proteins
    • Konishi, H., S. Kuroda, M. Tanaka, H. Matsuzaki, Y. Ono, K. Kameyama, T. Haga, and U. Kikkawa. 1995. Molecular-cloning and characterization of a new member of the RAC protein-kinase family - association of the pleckstrin homology domain of 3 types of RAC protein-kinase with protein-kinase-C subspecies and beta-gamma-subunits of G-proteins. Biochem. Biophys. Res. Commun. 216:526-534.
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 526-534
    • Konishi, H.1    Kuroda, S.2    Tanaka, M.3    Matsuzaki, H.4    Ono, Y.5    Kameyama, K.6    Haga, T.7    Kikkawa, U.8
  • 43
    • 0032566691 scopus 로고    scopus 로고
    • Characterization of a PKC activation loop kinase
    • Le Good, A. J., W. H. Ziegler, D. Alessi, and P. J. Parker. 1998. Characterization of a PKC activation loop kinase. Science 281:2042-2045.
    • (1998) Science , vol.281 , pp. 2042-2045
    • Le Good, A.J.1    Ziegler, W.H.2    Alessi, D.3    Parker, P.J.4
  • 44
    • 0029939448 scopus 로고    scopus 로고
    • PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surface
    • Lemmon, M. A., K. M. Ferguson, and J. Schlessinger. 1996. PH domains: diverse sequences with a common fold recruit signaling molecules to the cell surface. Cell 85:621-624.
    • (1996) Cell , vol.85 , pp. 621-624
    • Lemmon, M.A.1    Ferguson, K.M.2    Schlessinger, J.3
  • 45
    • 0030727172 scopus 로고    scopus 로고
    • Mitogenic activation, phosphorylation, and nuclear translocation of protein kinase Bβ
    • Meier, R., D. R. Alessi, P. Cron, M. Andjelković, and B. A. Hemmings. 1997. Mitogenic activation, phosphorylation, and nuclear translocation of protein kinase Bβ. J. Biol. Chem. 272:30491-30497.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30491-30497
    • Meier, R.1    Alessi, D.R.2    Cron, P.3    Andjelković, M.4    Hemmings, B.A.5
  • 46
    • 0032535490 scopus 로고    scopus 로고
    • Inactivation and dephosphorylation of protein kinase Bα (PKBα) promoted by hyperosmotic stress
    • Meier, R., M. Thelen, and B. A. Hemmings. 1998. Inactivation and dephosphorylation of protein kinase Bα (PKBα) promoted by hyperosmotic stress. EMBO J. 17:7294-7303.
    • (1998) EMBO J. , vol.17 , pp. 7294-7303
    • Meier, R.1    Thelen, M.2    Hemmings, B.A.3
  • 47
    • 0030987070 scopus 로고    scopus 로고
    • Regulation of protein kinase C
    • Newton, A. 1997. Regulation of protein kinase C. Curr. Opin. Cell Biol. 9: 161-167.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 161-167
    • Newton, A.1
  • 49
    • 0028306807 scopus 로고
    • Differential inhibition of protein kinase C izozymes by UCN-01, a staurosporine analogue
    • Seynaeve, C. M., M. G. Kazanietz, P. M. Blumberg, E. A. Sausville, and P. J. Worland. 1994. Differential inhibition of protein kinase C izozymes by UCN-01, a staurosporine analogue. Mol. Pharmacol. 45:1207-1214.
    • (1994) Mol. Pharmacol. , vol.45 , pp. 1207-1214
    • Seynaeve, C.M.1    Kazanietz, M.G.2    Blumberg, P.M.3    Sausville, E.A.4    Worland, P.J.5
  • 52
    • 0030992837 scopus 로고    scopus 로고
    • Signalling through the lipid products of phosphoinositide-3-OH kinase
    • Toker, A., and L. Cantley. 1997. Signalling through the lipid products of phosphoinositide-3-OH kinase. Nature 387:673-676.
    • (1997) Nature , vol.387 , pp. 673-676
    • Toker, A.1    Cantley, L.2
  • 55
    • 0028877293 scopus 로고
    • Rejection antigen peptides on BALB/c RL♂1 leukemia recognized by cytotoxic T lymphocytes: Derivation from the normally untranslated 5′ region of the c-Akt proto-oncogene activated by log terminal repeat
    • Wada, H., M. Matsuo, A. Uenaka, N. Shimbara, K. Shimizu, and E. Nakayama. 1995. Rejection antigen peptides on BALB/c RL♂1 leukemia recognized by cytotoxic T lymphocytes: derivation from the normally untranslated 5′ region of the c-Akt proto-oncogene activated by log terminal repeat. Cancer Res. 55:4780-4783.
    • (1995) Cancer Res. , vol.55 , pp. 4780-4783
    • Wada, H.1    Matsuo, M.2    Uenaka, A.3    Shimbara, N.4    Shimizu, K.5    Nakayama, E.6
  • 56
    • 0032055131 scopus 로고    scopus 로고
    • Activation of protein kinase Bβ and γ isoforms by insulin in vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro: Comparison with protein kinase Bα
    • Walker, K. S., M. Deak, A. Paterson, K. Hudson, P. Cohen, and D. R. Alessi. 1998. Activation of protein kinase Bβ and γ isoforms by insulin in vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro: comparison with protein kinase Bα. Biochem. J. 331:299-308.
    • (1998) Biochem. J. , vol.331 , pp. 299-308
    • Walker, K.S.1    Deak, M.2    Paterson, A.3    Hudson, K.4    Cohen, P.5    Alessi, D.R.6
  • 57
    • 0028979464 scopus 로고
    • Crystal structure of the Cys2 activator-binding domain of protein kinase Cδ in complex with phorbol ester
    • Zhang, G., M. G. Kazanietz, P. M. Blumberg, and J. H. Hurley. 1995. Crystal structure of the Cys2 activator-binding domain of protein kinase Cδ in complex with phorbol ester. Cell 81:917-924.
    • (1995) Cell , vol.81 , pp. 917-924
    • Zhang, G.1    Kazanietz, M.G.2    Blumberg, P.M.3    Hurley, J.H.4


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