메뉴 건너뛰기




Volumn 71, Issue 5, 1998, Pages 2123-2131

Alzheimer's β-amyloid peptide 1-42 induces a phagocytic response in murine microglia

Author keywords

Acetylated low density lipoproteins; Microglia; Microspheres; Phagocytosis; Zymosan; Amyloid

Indexed keywords

AMYLOID BETA PROTEIN;

EID: 0031753157     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1998.71052123.x     Document Type: Article
Times cited : (99)

References (59)
  • 1
    • 0030038809 scopus 로고    scopus 로고
    • Scavenging of Alzheimer's amyloid beta-protein by microglia in culture
    • Ard M. D., Cole G. M., Wei J., Mehrle A. P., and Fratkin J. D. (1996) Scavenging of Alzheimer's amyloid beta-protein by microglia in culture. J. Neurosci. Res. 43, 190-202.
    • (1996) J. Neurosci. Res. , vol.43 , pp. 190-202
    • Ard, M.D.1    Cole, G.M.2    Wei, J.3    Mehrle, A.P.4    Fratkin, J.D.5
  • 2
    • 0030037586 scopus 로고    scopus 로고
    • Beta-amyloid peptide secretion by a microglial cell line is induced by beta-amyloid-(25-35) and lipopolysaccharide
    • Bitting L., Naidu A., Cordell B., and Murphy G. M. (1996) Beta-amyloid peptide secretion by a microglial cell line is induced by beta-amyloid-(25-35) and lipopolysaccharide. J. Biol. Chem. 271, 16084-16089.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16084-16089
    • Bitting, L.1    Naidu, A.2    Cordell, B.3    Murphy, G.M.4
  • 3
    • 0025233694 scopus 로고
    • Immortalization of murine microglial cells by a v-raf/ v-myc carrying retrovirus
    • Blasi E., Barluzzi R., Bocchini V., Mazzolla R., and Bistoni F. (1990) Immortalization of murine microglial cells by a v-raf/ v-myc carrying retrovirus. J. Neuroimmunol. 27, 229-237.
    • (1990) J. Neuroimmunol. , vol.27 , pp. 229-237
    • Blasi, E.1    Barluzzi, R.2    Bocchini, V.3    Mazzolla, R.4    Bistoni, F.5
  • 4
    • 0030793528 scopus 로고    scopus 로고
    • Activation of nuclear factor-κB by β-amyloid peptides and interferon-γ in murine microglia
    • Bonaiuto C., McDonald P. P., Rossi F., and Cassatella M. A. (1997) Activation of nuclear factor-κB by β-amyloid peptides and interferon-γ in murine microglia. J. Neuroimmunol. 77, 51-56.
    • (1997) J. Neuroimmunol. , vol.77 , pp. 51-56
    • Bonaiuto, C.1    McDonald, P.P.2    Rossi, F.3    Cassatella, M.A.4
  • 5
    • 0027158642 scopus 로고
    • Association cortex, cerebellum, and serum concentrations of C1q and factor B in Alzheimer's disease
    • Brachova L., Lue L. F., Schultz J., El Rashidy T., and Rogers J. (1993) Association cortex, cerebellum, and serum concentrations of C1q and factor B in Alzheimer's disease. Mol. Brain Rex. 18, 329-334.
    • (1993) Mol. Brain Rex. , vol.18 , pp. 329-334
    • Brachova, L.1    Lue, L.F.2    Schultz, J.3    El Rashidy, T.4    Rogers, J.5
  • 7
    • 0030725311 scopus 로고    scopus 로고
    • Perlecan binds to the β-amyloid proteins (Aβ) of Alzheimer's disease, accelerates Aβ fibril formation, and maintains Aβ fibril stability
    • Castillo G. M., Ngo C., Cummings J., Wight T. N., and Snow A. D. (1997) Perlecan binds to the β-amyloid proteins (Aβ) of Alzheimer's disease, accelerates Aβ fibril formation, and maintains Aβ fibril stability. J. Neurochem. 69, 2452-2465.
    • (1997) J. Neurochem. , vol.69 , pp. 2452-2465
    • Castillo, G.M.1    Ngo, C.2    Cummings, J.3    Wight, T.N.4    Snow, A.D.5
  • 8
    • 0030250758 scopus 로고    scopus 로고
    • Neuroglial-mediated immunoinflammatory responses in Alzheimer's disease: Complement activation and therapeutic approaches
    • Chen S., Frederickson R. C. A., and Brunden K. R. (1996) Neuroglial-mediated immunoinflammatory responses in Alzheimer's disease: complement activation and therapeutic approaches. Neurobiol. Aging 17, 781-787.
    • (1996) Neurobiol. Aging , vol.17 , pp. 781-787
    • Chen, S.1    Frederickson, R.C.A.2    Brunden, K.R.3
  • 10
    • 0030464914 scopus 로고    scopus 로고
    • β-Amyloid deposition and other measures of neuropathology predict cognitive status in Alzheimer's disease
    • Cummings B. J., Pike C. J., Shankle R., and Cotman C. W. (1996) β-Amyloid deposition and other measures of neuropathology predict cognitive status in Alzheimer's disease. Neurobiol. Aging 17, 921-933.
    • (1996) Neurobiol. Aging , vol.17 , pp. 921-933
    • Cummings, B.J.1    Pike, C.J.2    Shankle, R.3    Cotman, C.W.4
  • 11
    • 0026802893 scopus 로고
    • Zymosan induces selective release of arachidonic acid from rabbit alveolar macrophages via stimulation of a beta-glucan receptor
    • Daum T. and Rohrbach M. S. (1992) Zymosan induces selective release of arachidonic acid from rabbit alveolar macrophages via stimulation of a beta-glucan receptor. FEBS Lett. 309, 119-122.
    • (1992) FEBS Lett. , vol.309 , pp. 119-122
    • Daum, T.1    Rohrbach, M.S.2
  • 12
    • 0027099863 scopus 로고
    • The amyloid beta protein of Alzheimer's disease is chemotactic for mononuclear phagocytes
    • Davis J. B., McMurray H. F., and Schubert D. (1992) The amyloid beta protein of Alzheimer's disease is chemotactic for mononuclear phagocytes. Biochem. Biophys. Res. Commun. 189, 1096-1100.
    • (1992) Biochem. Biophys. Res. Commun. , vol.189 , pp. 1096-1100
    • Davis, J.B.1    McMurray, H.F.2    Schubert, D.3
  • 16
    • 0030250886 scopus 로고    scopus 로고
    • Evolutionary perspectives on amyloid and inflammatory features of Alzheimer's disease
    • Finch C. E. and Marchalonis J. J. (1996) Evolutionary perspectives on amyloid and inflammatory features of Alzheimer's disease. Neurobiol. Aging 17, 809-815.
    • (1996) Neurobiol. Aging , vol.17 , pp. 809-815
    • Finch, C.E.1    Marchalonis, J.J.2
  • 17
    • 0026783591 scopus 로고
    • Ultrastructure of the microglia that phagocytose amyloid and the microglia that produce β-amyloid fibrils
    • Frackowiak J., Wisniewski H. M., Wegiel J., Merz G. S., Iqbal I., and Wang K. C. (1992) Ultrastructure of the microglia that phagocytose amyloid and the microglia that produce β-amyloid fibrils. Acta Neuropathol. 84, 225-233.
    • (1992) Acta Neuropathol. , vol.84 , pp. 225-233
    • Frackowiak, J.1    Wisniewski, H.M.2    Wegiel, J.3    Merz, G.S.4    Iqbal, I.5    Wang, K.C.6
  • 19
    • 0027978247 scopus 로고
    • New opportunities in AD research - Roles of immunoinflammatory responses and glia
    • Frederickson R. C. A. and Brunden K. R. (1994) New opportunities in AD research - roles of immunoinflammatory responses and glia. Alzheimer Dis. Assoc. Disord. 8, 159-164.
    • (1994) Alzheimer Dis. Assoc. Disord. , vol.8 , pp. 159-164
    • Frederickson, R.C.A.1    Brunden, K.R.2
  • 20
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner G. G. and Wong C. W. (1984) Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120, 885-890.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 21
    • 0029087650 scopus 로고
    • Microglial release of nitric oxide by the synergistic action of β-amyloid and IFN-γ
    • Goodwin J. L., Uemura E., and Cunnick J. E. (1995) Microglial release of nitric oxide by the synergistic action of β-amyloid and IFN-γ. Brain Res. 692, 207-214.
    • (1995) Brain Res. , vol.692 , pp. 207-214
    • Goodwin, J.L.1    Uemura, E.2    Cunnick, J.E.3
  • 22
    • 0000662562 scopus 로고
    • On a new series of bodies in which nitrogen is substituted for hydrogen
    • Griess J. P. (1864) On a new series of bodies in which nitrogen is substituted for hydrogen. Philos. Trans. R. Soc. Lond. 154, 667-731.
    • (1864) Philos. Trans. R. Soc. Lond. , vol.154 , pp. 667-731
    • Griess, J.P.1
  • 23
    • 0028926976 scopus 로고
    • Interleukin-1 expression in different plaque types in Alzheimer's disease: Significance in plaque evolution
    • Griffin W. S. T., Sheng J. G., Roberts G. W., and Mrak R. E. (1995) Interleukin-1 expression in different plaque types in Alzheimer's disease: significance in plaque evolution. J. Neuropathol. Exp. Neurol. 54, 276-281.
    • (1995) J. Neuropathol. Exp. Neurol. , vol.54 , pp. 276-281
    • Griffin, W.S.T.1    Sheng, J.G.2    Roberts, G.W.3    Mrak, R.E.4
  • 24
    • 0027333557 scopus 로고
    • Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptide
    • Haass C. and Selkoe D. J. (1993) Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptide. Cell 75, 1039-1042.
    • (1993) Cell , vol.75 , pp. 1039-1042
    • Haass, C.1    Selkoe, D.J.2
  • 25
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer's disease
    • Hardy J. and Allsop D. (1991) Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol. Sci. 12, 383-388.
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 26
    • 0028587152 scopus 로고
    • Regional differences in reactive gliosis induced by substrate-bound beta-amyloid
    • Hoke A., Canning D. R., Malemud C. J., and Silver J. (1994) Regional differences in reactive gliosis induced by substrate-bound beta-amyloid. Exp. Neurol. 130, 56-66.
    • (1994) Exp. Neurol. , vol.130 , pp. 56-66
    • Hoke, A.1    Canning, D.R.2    Malemud, C.J.3    Silver, J.4
  • 27
    • 0021262101 scopus 로고
    • Immuno-electron-microscopic localization of complements in amyloid fibrils of senile plaques
    • Ishii T. and Haga S. (1984) Immuno-electron-microscopic localization of complements in amyloid fibrils of senile plaques. Acta Neuropathol. 63, 296-300.
    • (1984) Acta Neuropathol. , vol.63 , pp. 296-300
    • Ishii, T.1    Haga, S.2
  • 28
    • 0031056029 scopus 로고    scopus 로고
    • Interaction of Alzheimer β-amyloid peptide with the human monocytic cell line THP-1 results in a protein kinase C-dependent secretion of tumor necrosis factor-α
    • Klegaris A., Walker D. G., and McGeer P. L. (1997) Interaction of Alzheimer β-amyloid peptide with the human monocytic cell line THP-1 results in a protein kinase C-dependent secretion of tumor necrosis factor-α. Brain Res. 747, 114-121.
    • (1997) Brain Res. , vol.747 , pp. 114-121
    • Klegaris, A.1    Walker, D.G.2    McGeer, P.L.3
  • 30
    • 0027502784 scopus 로고
    • Thioflavin T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine H. (1993) Thioflavin T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2, 404-410.
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • Levine, H.1
  • 31
    • 0030153520 scopus 로고    scopus 로고
    • Beta-amyloid induces increased release of interleukin-1 beta from lipopolysaccharide-activated human monocytes
    • Lorton D., Kocsis J. M., King L., Madden K., and Brunden K. R. (1996) Beta-amyloid induces increased release of interleukin-1 beta from lipopolysaccharide-activated human monocytes. J. Neuroimmunol. 67, 21-29.
    • (1996) J. Neuroimmunol. , vol.67 , pp. 21-29
    • Lorton, D.1    Kocsis, J.M.2    King, L.3    Madden, K.4    Brunden, K.R.5
  • 32
    • 1842293994 scopus 로고    scopus 로고
    • High affinity saturable uptake of oxidized low density lipoprotein by macrophages from mice lacking the scavenger receptor class a type I/II
    • Lougheed M., Lum C. M., Ling W., Suzuki H., Kodama T., and Steinbrecher U. (1997) High affinity saturable uptake of oxidized low density lipoprotein by macrophages from mice lacking the scavenger receptor class A type I/II. J. Biol. Chem. 272, 12938-12944.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12938-12944
    • Lougheed, M.1    Lum, C.M.2    Ling, W.3    Suzuki, H.4    Kodama, T.5    Steinbrecher, U.6
  • 33
    • 0028787874 scopus 로고
    • Role of microglia in senile plaque formation
    • Mackenzie I. R. A., Hao C., and Munoz D. G. (1995) Role of microglia in senile plaque formation. Neurobiol. Aging 16, 797-804.
    • (1995) Neurobiol. Aging , vol.16 , pp. 797-804
    • Mackenzie, I.R.A.1    Hao, C.2    Munoz, D.G.3
  • 34
    • 0030013534 scopus 로고    scopus 로고
    • Amyloid protein dependent nitric oxide production from microglial cells and neurotoxicity
    • Masayuki I., Sunamoto M., Ohnishi K., and Ichimori Y. (1996) β-Amyloid protein dependent nitric oxide production from microglial cells and neurotoxicity. Brain Res. 720, 93-100.
    • (1996) Brain Res. , vol.720 , pp. 93-100
    • Masayuki, I.1    Sunamoto, M.2    Ohnishi, K.3    Ichimori, Y.4
  • 36
    • 0030961544 scopus 로고    scopus 로고
    • Amyloid fibrils activate tyrosine kinase-dependent signaling and superoxide production in microglia
    • McDonald D. R., Brunden K. R., and Landreth G. E. (1997) Amyloid fibrils activate tyrosine kinase-dependent signaling and superoxide production in microglia. J. Neurosci. 17, 2284-2294.
    • (1997) J. Neurosci. , vol.17 , pp. 2284-2294
    • McDonald, D.R.1    Brunden, K.R.2    Landreth, G.E.3
  • 37
    • 0032526423 scopus 로고    scopus 로고
    • Amyloid fibrils activate parallel mitogen-activated protein kinase pathways in microglia and THP-1 monocytes
    • McDonald D. R., Bamberger M. E., Combs C. K., and Landreth G. E. (1998) β-Amyloid fibrils activate parallel mitogen-activated protein kinase pathways in microglia and THP-1 monocytes. J. Neurosci. 18, 4451-4460.
    • (1998) J. Neurosci. , vol.18 , pp. 4451-4460
    • McDonald, D.R.1    Bamberger, M.E.2    Combs, C.K.3    Landreth, G.E.4
  • 40
    • 0030248270 scopus 로고    scopus 로고
    • Microglial cells internalize aggregates of the Alzheimer's disease amyloid β-protein via a scavenger receptor
    • Paresce D. M., Ghosh R. N., and Maxfield F. R. (1996) Microglial cells internalize aggregates of the Alzheimer's disease amyloid β-protein via a scavenger receptor. Neuron 17, 553-565.
    • (1996) Neuron , vol.17 , pp. 553-565
    • Paresce, D.M.1    Ghosh, R.N.2    Maxfield, F.R.3
  • 41
    • 0030664076 scopus 로고    scopus 로고
    • Slow degradation of aggregates of the Alzheimer's disease amyloid β-protein by microglial cells
    • Paresce D. M., Chung H., and Maxfield F. R. (1997) Slow degradation of aggregates of the Alzheimer's disease amyloid β-protein by microglial cells. J. Cell Biol. 272, 29390-29397.
    • (1997) J. Cell Biol. , vol.272 , pp. 29390-29397
    • Paresce, D.M.1    Chung, H.2    Maxfield, F.R.3
  • 42
    • 1842367306 scopus 로고    scopus 로고
    • Degradation of amyloid β-protein by a metalloprotease secreted by microglia and other neural and non-neural cells
    • Qiu W. Q., Ye Z., Kholodenko D., Seubert P., and Selkoe D. J. (1997) Degradation of amyloid β-protein by a metalloprotease secreted by microglia and other neural and non-neural cells. J. Biol. Chem. 272, 6641-6646.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6641-6646
    • Qiu, W.Q.1    Ye, Z.2    Kholodenko, D.3    Seubert, P.4    Selkoe, D.J.5
  • 45
  • 47
    • 0027066985 scopus 로고
    • Regulation and subcellular location of nitrogen oxide synthases in RAW264.7 macrophages
    • Schmidt H. H. H. W., Warner T. D., Nakane M., Forstermann U., and Murad F. (1992) Regulation and subcellular location of nitrogen oxide synthases in RAW264.7 macrophages. Mol. Pharmacol. 41, 615-624.
    • (1992) Mol. Pharmacol. , vol.41 , pp. 615-624
    • Schmidt, H.H.H.W.1    Warner, T.D.2    Nakane, M.3    Forstermann, U.4    Murad, F.5
  • 49
    • 0030669656 scopus 로고    scopus 로고
    • Amyloid peptide induces tumor necrosis factor-α and nitric oxide production in murine macrophage cultures
    • Shalit F., Sredni B., Rosenblatt-Bin H., Kazimirsky G., Brodie C., and Huberman M. (1997) β-Amyloid peptide induces tumor necrosis factor-α and nitric oxide production in murine macrophage cultures. Neuroreport 8, 3577-3580.
    • (1997) Neuroreport , vol.8 , pp. 3577-3580
    • Shalit, F.1    Sredni, B.2    Rosenblatt-Bin, H.3    Kazimirsky, G.4    Brodie, C.5    Huberman, M.6
  • 50
    • 0028173033 scopus 로고
    • S100β protein expression in Alzheimer's disease: Potential role in the pathogenesis of neuritic plaques
    • Sheng J. G., Mrak R. E., and Griffin W. S. T. (1994) S100β protein expression in Alzheimer's disease: potential role in the pathogenesis of neuritic plaques. J. Neurosci. Res. 39, 398-404.
    • (1994) J. Neurosci. Res. , vol.39 , pp. 398-404
    • Sheng, J.G.1    Mrak, R.E.2    Griffin, W.S.T.3
  • 51
    • 0007692414 scopus 로고    scopus 로고
    • In vivo and in vitro evidence supporting a role for the inflammatory cytokine interleukin-1 as a driving force in Alzheimer pathogenesis
    • Sheng J. G., Ito K., Skinner R. D., Mrak R. E., Rovnaghi C. R., Van Eldik L. J., and Griffin W. S. T. (1996) In vivo and in vitro evidence supporting a role for the inflammatory cytokine interleukin-1 as a driving force in Alzheimer pathogenesis. Neurobiol. Aging 17, 761-766.
    • (1996) Neurobiol. Aging , vol.17 , pp. 761-766
    • Sheng, J.G.1    Ito, K.2    Skinner, R.D.3    Mrak, R.E.4    Rovnaghi, C.R.5    Van Eldik, L.J.6    Griffin, W.S.T.7
  • 52
    • 0030757323 scopus 로고    scopus 로고
    • Neuritic plaque evolution in Alzheimer's disease is accompanied by transition of activated microglia from primed to enlarged to phagocytic forms
    • Sheng J. G., Mrak R. E., and Griffin W. S. T. (1997) Neuritic plaque evolution in Alzheimer's disease is accompanied by transition of activated microglia from primed to enlarged to phagocytic forms. Acta Neuropathol. 94, 1-5.
    • (1997) Acta Neuropathol. , vol.94 , pp. 1-5
    • Sheng, J.G.1    Mrak, R.E.2    Griffin, W.S.T.3
  • 53
    • 0028362886 scopus 로고
    • Heparan sulfate proteoglycan in diffuse plaques of hippocampus but not in cerebellum of Alzheimer's disease brain
    • Snow A. D., Sekiguchi R., Nochlin D., Kalaria R. N., and Kimata K. (1994) Heparan sulfate proteoglycan in diffuse plaques of hippocampus but not in cerebellum of Alzheimer's disease brain. Am. J. Pathol. 144, 337-347.
    • (1994) Am. J. Pathol. , vol.144 , pp. 337-347
    • Snow, A.D.1    Sekiguchi, R.2    Nochlin, D.3    Kalaria, R.N.4    Kimata, K.5
  • 54
    • 0020068143 scopus 로고
    • Phagocytosis: Flow cytometric quantitation with fluorescent microspheres
    • Steinkamp J. A., Wilson J. S., Saunders G. C., and Stewart C. C. (1982) Phagocytosis: flow cytometric quantitation with fluorescent microspheres. Science 215, 64-66.
    • (1982) Science , vol.215 , pp. 64-66
    • Steinkamp, J.A.1    Wilson, J.S.2    Saunders, G.C.3    Stewart, C.C.4
  • 55
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid β protein secreted by familial amyloid β protein precursor (βAPP717) mutants
    • Suzuki N., Cheung T. T., Cai X. D., Odaka A., Otvos L. J., Eckman C., Golde T. E., and Younkin S. G. (1994) An increased percentage of long amyloid β protein secreted by familial amyloid β protein precursor (βAPP717) mutants. Science 264, 1336-1340.
    • (1994) Science , vol.264 , pp. 1336-1340
    • Suzuki, N.1    Cheung, T.T.2    Cai, X.D.3    Odaka, A.4    Otvos, L.J.5    Eckman, C.6    Golde, T.E.7    Younkin, S.G.8
  • 56
    • 0004818738 scopus 로고
    • High-affinity receptor-mediated uptake and degradation of glucose-modified proteins: A potential mechanism for the removal of senescent macromolecules
    • Vlassara H., Brownlee M., and Cerami A. (1985) High-affinity receptor-mediated uptake and degradation of glucose-modified proteins: a potential mechanism for the removal of senescent macromolecules. Proc. Natl. Acad. Sci. USA 82, 5588-5592.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 5588-5592
    • Vlassara, H.1    Brownlee, M.2    Cerami, A.3
  • 57
    • 0031583918 scopus 로고    scopus 로고
    • Microglial phagocytosis is modulated by pro- And anti-inflammatory cytokines
    • von Zahn J., Moller T., Kettenmann H., and Nolte C. (1997) Microglial phagocytosis is modulated by pro-and anti-inflammatory cytokines. Neuroreport 8, 3851-3856.
    • (1997) Neuroreport , vol.8 , pp. 3851-3856
    • Von Zahn, J.1    Moller, T.2    Kettenmann, H.3    Nolte, C.4
  • 59
    • 0024339121 scopus 로고
    • The ultrastructural localization of sulfated proteoglycans is identical in the amyloids of Alzheimer's disease and AA, AL, senile cardiac and medullary carcinoma-associated amyloidosis
    • Young I. D., Willmer J. P., and Kisilevsky R. (1989) The ultrastructural localization of sulfated proteoglycans is identical in the amyloids of Alzheimer's disease and AA, AL, senile cardiac and medullary carcinoma-associated amyloidosis. Acta Neuropathol. (Berl.) 78, 202-209.
    • (1989) Acta Neuropathol. (Berl.) , vol.78 , pp. 202-209
    • Young, I.D.1    Willmer, J.P.2    Kisilevsky, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.