메뉴 건너뛰기




Volumn 36, Issue 4, 2004, Pages 223-231

MMP and ADAM in rheumatoid arthritis

Author keywords

A disintegrin and metalloproteinase; Extracellular matrix; Matrix metalloproteinase; Rheumatoid arthritis; Tissue inhibitor of metalloproteinases

Indexed keywords

MATRIX METALLOPROTEINASE; TISSUE INHIBITOR OF METALLOPROTEINASE; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME;

EID: 11144297635     PISSN: 0916572X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (1)

References (49)
  • 2
    • 0030037395 scopus 로고    scopus 로고
    • Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme
    • Knauper, V., Will, H., Lopez-Otin, C., Smith, B., Atkinson, S.J., Stanton, H., Hembry, R.M., and Murphy, G. (1996) Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme. J. Biol. Chem. 271, 17124-17131
    • (1996) J. Biol. Chem. , vol.271 , pp. 17124-17131
    • Knauper, V.1    Will, H.2    Lopez-Otin, C.3    Smith, B.4    Atkinson, S.J.5    Stanton, H.6    Hembry, R.M.7    Murphy, G.8
  • 3
    • 0025616093 scopus 로고
    • Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties
    • Okada, Y., Morodomi, T., Enghild, J.J., Suzuki, K., Yasui, A., Nakanishi, I., Salvesen, G., and Nagase, H. (1990) Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties. Eur. J. Biochem. 194, 721-730
    • (1990) Eur. J. Biochem. , vol.194 , pp. 721-730
    • Okada, Y.1    Morodomi, T.2    Enghild, J.J.3    Suzuki, K.4    Yasui, A.5    Nakanishi, I.6    Salvesen, G.7    Nagase, H.8
  • 4
    • 0026795140 scopus 로고
    • Matrix metalloproteinase 9 (92-kDa gelatinase/type IV collagenase) from HT 1080 human fibrosarcoma cells. Purification and activation of the precursor and enzymic properties
    • Okada, Y., Gonoji, Y., Naka, K., Tomita, K., Nakanishi, I., Iwata, K., Yamashita, K., and Hayakawa, T. (1992) Matrix metalloproteinase 9 (92-kDa gelatinase/type IV collagenase) from HT 1080 human fibrosarcoma cells. Purification and activation of the precursor and enzymic properties. J. Biol. Chem. 267, 21712-21719
    • (1992) J. Biol. Chem. , vol.267 , pp. 21712-21719
    • Okada, Y.1    Gonoji, Y.2    Naka, K.3    Tomita, K.4    Nakanishi, I.5    Iwata, K.6    Yamashita, K.7    Hayakawa, T.8
  • 5
    • 0023024460 scopus 로고
    • A metalloproteinase from human rheumatoid synovial fibroblasts that digests connective tissue matrix components. Purification and characterization
    • Okada, Y., Nagase, H., and Harris, E.D., Jr. (1986) A metalloproteinase from human rheumatoid synovial fibroblasts that digests connective tissue matrix components. Purification and characterization. J. Biol. Chem. 261, 14245-14255
    • (1986) J. Biol. Chem. , vol.261 , pp. 14245-14255
    • Okada, Y.1    Nagase, H.2    Harris Jr., E.D.3
  • 6
    • 0030957218 scopus 로고    scopus 로고
    • Activation mechanisms of matrix metalloproteinases
    • Nagase, H. (1997) Activation mechanisms of matrix metalloproteinases. Biol. Chem. 378, 151-160
    • (1997) Biol. Chem. , vol.378 , pp. 151-160
    • Nagase, H.1
  • 7
    • 0032053550 scopus 로고    scopus 로고
    • Activation of the precursor of human stromelysin 2 and its interactions with other matrix metalloproteinases
    • Nakamura, H., Fujii, Y., Ohuchi, E., Yamamoto, E., and Okada, Y. (1998) Activation of the precursor of human stromelysin 2 and its interactions with other matrix metalloproteinases. Eur. J. Biochem. 253, 67-75
    • (1998) Eur. J. Biochem. , vol.253 , pp. 67-75
    • Nakamura, H.1    Fujii, Y.2    Ohuchi, E.3    Yamamoto, E.4    Okada, Y.5
  • 8
    • 0028913443 scopus 로고
    • Matrix metalloproteinase 7 (matrilysin) from human rectal carcinoma cells. Activation of the precursor, interaction with other matrix metalloproteinases and enzymic properties
    • Imai, K., Yokohama, Y., Nakanishi, I., Ohuchi, E., Fujii, Y., Nakai, N., and Okada, Y. (1995) Matrix metalloproteinase 7 (matrilysin) from human rectal carcinoma cells. Activation of the precursor, interaction with other matrix metalloproteinases and enzymic properties. J. Biol. Chem. 270, 6691-6697
    • (1995) J. Biol. Chem. , vol.270 , pp. 6691-6697
    • Imai, K.1    Yokohama, Y.2    Nakanishi, I.3    Ohuchi, E.4    Fujii, Y.5    Nakai, N.6    Okada, Y.7
  • 9
    • 0034617262 scopus 로고    scopus 로고
    • Identification and characterization of human endometase (Matrix metalloproteinase-26) from endometrial tumor
    • Park, H.I., Ni, J., Gerkema, F.E., Liu, D., Belozerov, V.E., and Sang, Q.X. (2000) Identification and characterization of human endometase (Matrix metalloproteinase-26) from endometrial tumor. J. Biol. Chem. 275, 20540-20544
    • (2000) J. Biol. Chem. , vol.275 , pp. 20540-20544
    • Park, H.I.1    Ni, J.2    Gerkema, F.E.3    Liu, D.4    Belozerov, V.E.5    Sang, Q.X.6
  • 10
    • 0036109679 scopus 로고    scopus 로고
    • MT-MMPs play pivotal roles in cancer dissemination
    • Yana, I. and Seiki, M. (2002) MT-MMPs play pivotal roles in cancer dissemination. Clin. Exp. Metastasis. 19, 209-215
    • (2002) Clin. Exp. Metastasis , vol.19 , pp. 209-215
    • Yana, I.1    Seiki, M.2
  • 11
    • 0031025218 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromoleclules
    • Ohuchi, E., Imai, K., Fujii, Y., Sato, H., Seiki, M., and Okada, Y. (1997) Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromoleclules. J. Biol. Chem. 272, 2446-2451
    • (1997) J. Biol. Chem. , vol.272 , pp. 2446-2451
    • Ohuchi, E.1    Imai, K.2    Fujii, Y.3    Sato, H.4    Seiki, M.5    Okada, Y.6
  • 12
    • 6844250127 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases
    • d'Ortho, M.P., Will, H., Atkinson, S., Butler, G., Messent, A., Gavrilovic, J., Smith, B., Timpl, R., Zardi, L., and Murphy, G. (1997) Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases. Eur. J. Biochem. 250, 751-757
    • (1997) Eur. J. Biochem. , vol.250 , pp. 751-757
    • D'Ortho, M.P.1    Will, H.2    Atkinson, S.3    Butler, G.4    Messent, A.5    Gavrilovic, J.6    Smith, B.7    Timpl, R.8    Zardi, L.9    Murphy, G.10
  • 13
    • 0033564010 scopus 로고    scopus 로고
    • Characterization of a truncated recombinant form of human membrane type 3 matrix metalloproteinase
    • Shimada, T., Nakamura, H., Ohuchi, E., Fujii, Y., Murakami, Y., Sato, H., Seiki, M., and Okada, Y. (1999) Characterization of a truncated recombinant form of human membrane type 3 matrix metalloproteinase. Eur. J. Biochem. 262, 907-914
    • (1999) Eur. J. Biochem. , vol.262 , pp. 907-914
    • Shimada, T.1    Nakamura, H.2    Ohuchi, E.3    Fujii, Y.4    Murakami, Y.5    Sato, H.6    Seiki, M.7    Okada, Y.8
  • 16
    • 0036133646 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha converting enzyme
    • Black, R.A. (2002) Tumor necrosis factor-alpha converting enzyme. Int. J. Biochem. Cell. Biol. 34, 1-5
    • (2002) Int. J. Biochem. Cell. Biol. , vol.34 , pp. 1-5
    • Black, R.A.1
  • 18
    • 0142211236 scopus 로고    scopus 로고
    • Processing and localization of ADAMTS-1 and proteolytic cleavage of versican during cumulus matrix expansion and ovulation
    • Russell, D.L., Doyle, K.M., Ochsner, S.A., Sandy, J.D., and Richards, J.S. (2003) Processing and localization of ADAMTS-1 and proteolytic cleavage of versican during cumulus matrix expansion and ovulation. J. Biol. Chem. 278, 42330-42339
    • (2003) J. Biol. Chem. , vol.278 , pp. 42330-42339
    • Russell, D.L.1    Doyle, K.M.2    Ochsner, S.A.3    Sandy, J.D.4    Richards, J.S.5
  • 24
    • 0023805619 scopus 로고
    • The precursor of a metalloendopeptidase from human rheumatoid synovial fibroblasts. Purification and mechanisms of activation by endopeptidases and 4-aminophenylmercuric acetate
    • Okada, Y., Harris, E.D., Jr., and Nagase, H. (1988) The precursor of a metalloendopeptidase from human rheumatoid synovial fibroblasts. Purification and mechanisms of activation by endopeptidases and 4-aminophenylmercuric acetate. Biochem. J. 254, 731-741
    • (1988) Biochem. J. , vol.254 , pp. 731-741
    • Okada, Y.1    Harris Jr., E.D.2    Nagase, H.3
  • 25
    • 0035801473 scopus 로고    scopus 로고
    • Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion
    • Itoh, Y., Takamura, A., Ito, N., Maru, Y., Sato, H., Suenaga, N., Aoki, T., and Seiki, M. (2001) Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion. Embo. J. 20, 4782-4793
    • (2001) Embo. J. , vol.20 , pp. 4782-4793
    • Itoh, Y.1    Takamura, A.2    Ito, N.3    Maru, Y.4    Sato, H.5    Suenaga, N.6    Aoki, T.7    Seiki, M.8
  • 26
    • 0034652586 scopus 로고    scopus 로고
    • EMMPRIN (CD147), an inducer of matrix metalloproteinase synthesis, also binds interstitial collagenase to the tumor cell surface
    • Guo, H., Li, R., Zucker, S., and Toole, B.P. (2000) EMMPRIN (CD147), an inducer of matrix metalloproteinase synthesis, also binds interstitial collagenase to the tumor cell surface. Cancer Res. 60, 888-891
    • (2000) Cancer Res. , vol.60 , pp. 888-891
    • Guo, H.1    Li, R.2    Zucker, S.3    Toole, B.P.4
  • 28
    • 0036468005 scopus 로고    scopus 로고
    • CD44 anchors the assembly of matrilysin/ MMP-7 with heparin-binding epidermal growth factor precursor and Erb B4 and regulates female reproductive organ remodeling
    • Yu, W.H., Woessner, J.F., Jr., McNeish, J.D., and Stamenkovic, I. (2002) CD44 anchors the assembly of matrilysin/ MMP-7 with heparin-binding epidermal growth factor precursor and Erb B4 and regulates female reproductive organ remodeling. Genes. Dev. 16, 307-323
    • (2002) Genes. Dev. , vol.16 , pp. 307-323
    • Yu, W.H.1    Woessner Jr., J.F.2    McNeish, J.D.3    Stamenkovic, I.4
  • 29
    • 0034650486 scopus 로고    scopus 로고
    • Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis
    • Yu, Q. and Stamenkovic, I. (2000) Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes, Dev. 14, 163-176
    • (2000) Genes. Dev. , vol.14 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2
  • 30
    • 0030717692 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases: Structure, regulation and biological functions
    • Gomez, D.E., Alonso, D.F., Yoshiji, H., and Thorgeirsson, U.P. (1997) Tissue inhibitors of metalloproteinases: structure, regulation and biological functions. Eur. J. Cell. Biol. 74, 111-122
    • (1997) Eur. J. Cell. Biol. , vol.74 , pp. 111-122
    • Gomez, D.E.1    Alonso, D.F.2    Yoshiji, H.3    Thorgeirsson, U.P.4
  • 31
    • 0034615550 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases: Evolution, structure and function
    • Brew, K., Dinakarpandian, D., and Nagase, H. (2000) Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochim. Biophys. Acta 1477, 267-283
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 267-283
    • Brew, K.1    Dinakarpandian, D.2    Nagase, H.3
  • 32
    • 0036800192 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors: Biological actions and therapeutic opportunities
    • Baker, A.H., Edwards, D.R., and Murphy, G. (2002) Metalloproteinase inhibitors: biological actions and therapeutic opportunities. J. Cell Sci. 115, 3719-3727
    • (2002) J. Cell Sci. , vol.115 , pp. 3719-3727
    • Baker, A.H.1    Edwards, D.R.2    Murphy, G.3
  • 33
    • 0036775766 scopus 로고    scopus 로고
    • The cell surface: The stage for matrix metalloproteinase regulation of migration
    • Seiki, M. (2002) The cell surface: The stage for matrix metalloproteinase regulation of migration. Curr. Opin. Cell. Biol. 14, 624-632
    • (2002) Curr. Opin. Cell. Biol. , vol.14 , pp. 624-632
    • Seiki, M.1
  • 34
    • 0034332481 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha induces a metalloprotease-disintegrin, ADAM8 (CD156): Implications for neuron-glia interactions during neurodegeneration
    • Schlomann, U., Rathke-Hartlieb, S., Yamamoto, S., Jockusch, H., and Bartsch, J.W. (2000) Tumor necrosis factor alpha induces a metalloprotease- disintegrin, ADAM8 (CD156): Implications for neuron-glia interactions during neurodegeneration. J. Neurosci. 20, 7964-7971
    • (2000) J. Neurosci. , vol.20 , pp. 7964-7971
    • Schlomann, U.1    Rathke-Hartlieb, S.2    Yamamoto, S.3    Jockusch, H.4    Bartsch, J.W.5
  • 35
    • 0038374867 scopus 로고    scopus 로고
    • ADAM12 in human liver cancers: TGF-beta-regulated expression in stellate cells is associated with matrix remodeling
    • Le Pabic, H., Bonnier, D., Wewer, U.M., Coutand, A., Musso, O., Baffet, G., Clement, B., and Theret, N. (2003) ADAM12 in human liver cancers: TGF-beta-regulated expression in stellate cells is associated with matrix remodeling. Hepatology 37, 1056-1066
    • (2003) Hepatology , vol.37 , pp. 1056-1066
    • Le Pabic, H.1    Bonnier, D.2    Wewer, U.M.3    Coutand, A.4    Musso, O.5    Baffet, G.6    Clement, B.7    Theret, N.8
  • 36
    • 3042849113 scopus 로고    scopus 로고
    • Tumour necrosis factor-alpha stimulates expression of TNF-alpha converting enzyme in endothelial cells
    • Bzowska, M., Jura, N., Lassak, A., Black, R.A., and Bereta, J. (2004) Tumour necrosis factor-alpha stimulates expression of TNF-alpha converting enzyme in endothelial cells. Eur. J. Biochem. 271, 2808-2820
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2808-2820
    • Bzowska, M.1    Jura, N.2    Lassak, A.3    Black, R.A.4    Bereta, J.5
  • 38
    • 0842308119 scopus 로고    scopus 로고
    • ADAM28 is activated by MMP-7 (matrilysin-1) and cleaves insulin-like growth factor binding protein-3
    • Mochizuki, S., Shimoda, M., Shiomi, T., Fujii, Y., and Okada, Y. (2004) ADAM28 is activated by MMP-7 (matrilysin-1) and cleaves insulin-like growth factor binding protein-3. Biochem. Biophys. Res. Commun. 315, 79-84
    • (2004) Biochem. Biophys. Res. Commun. , vol.315 , pp. 79-84
    • Mochizuki, S.1    Shimoda, M.2    Shiomi, T.3    Fujii, Y.4    Okada, Y.5
  • 39
    • 0035853456 scopus 로고    scopus 로고
    • Inhibition of ADAMTS4 (aggrecanase-1) by tissue inhibitors of metalloproteinases (TIMP-1, 2, 3 and 4)
    • Hashimoto, G., Aoki, T., Nakamura, H., Tanzawa, K., and Okada, Y. (2001) Inhibition of ADAMTS4 (aggrecanase-1) by tissue inhibitors of metalloproteinases (TIMP-1, 2, 3 and 4). FEBS Lett. 494, 192-195
    • (2001) FEBS Lett. , vol.494 , pp. 192-195
    • Hashimoto, G.1    Aoki, T.2    Nakamura, H.3    Tanzawa, K.4    Okada, Y.5
  • 40
    • 3543004686 scopus 로고    scopus 로고
    • ADAMTS4 (aggrecanase-1) interaction with the COOH-terminal domain of fibronectin inhibits proteolysis of aggrecan
    • Hashimoto, G., Shimoda, M., and Okada, Y. (2004) ADAMTS4 (aggrecanase-1) interaction with the COOH-terminal domain of fibronectin inhibits proteolysis of aggrecan. J. Biol. Chem. 279, 32483-32491
    • (2004) J. Biol. Chem. , vol.279 , pp. 32483-32491
    • Hashimoto, G.1    Shimoda, M.2    Okada, Y.3
  • 41
    • 0024473876 scopus 로고
    • Immunolocalization of matrix metalloproteinase 3 (stromelysin) in rheumatoid synovioblasts (B cells): Correlation with rheumatoid arthritis
    • Okada, Y., Takeuchi, N., Tomita, K., Nakanishi, I., and Nagase, H. (1989) Immunolocalization of matrix metalloproteinase 3 (stromelysin) in rheumatoid synovioblasts (B cells): correlation with rheumatoid arthritis. Ann. Rheum. Dis. 48, 645-653
    • (1989) Ann. Rheum. Dis. , vol.48 , pp. 645-653
    • Okada, Y.1    Takeuchi, N.2    Tomita, K.3    Nakanishi, I.4    Nagase, H.5
  • 42
    • 0025039296 scopus 로고
    • Immunohistochemical demonstration of collagenase and tissue inhibitor of metalloproteinases (TIMP) in synovial lining cells of rheumatoid synovium
    • Okada, Y., Gonoji, Y., Nakanishi, I., Nagase, H., and Hayakawa, T. (1990) Immunohistochemical demonstration of collagenase and tissue inhibitor of metalloproteinases (TIMP) in synovial lining cells of rheumatoid synovium. Virchows Arch. B Cell. Pathol. Incl. Mol. Pathol. 59, 305-312
    • (1990) Virchows Arch. B Cell. Pathol. Incl. Mol. Pathol. , vol.59 , pp. 305-312
    • Okada, Y.1    Gonoji, Y.2    Nakanishi, I.3    Nagase, H.4    Hayakawa, T.5
  • 43
    • 0029790101 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase 9 (96-kd gelatinase B) in human rheumatoid arthritis
    • Ahrens, D., Koch, A.E., Pope, R.M., Stein-Picarella, M., and Niedbala, M.J. (1996) Expression of matrix metalloproteinase 9 (96-kd gelatinase B) in human rheumatoid arthritis. Arthritis. Rheum. 39, 1576-1587
    • (1996) Arthritis. Rheum. , vol.39 , pp. 1576-1587
    • Ahrens, D.1    Koch, A.E.2    Pope, R.M.3    Stein-Picarella, M.4    Niedbala, M.J.5
  • 45
    • 0033851494 scopus 로고    scopus 로고
    • Production of tissue inhibitor of metalloproteinases 3 is selectively enhanced by calcium pentosan polysulfate in human rheumatoid synovial fibroblasts
    • Takizawa, M., Ohuchi, E., Yamanaka, H., Nakamura, H., Ikeda, E., Ghosh, P., and Okada, Y. (2000) Production of tissue inhibitor of metalloproteinases 3 is selectively enhanced by calcium pentosan polysulfate in human rheumatoid synovial fibroblasts. Arthritis. Rheum. 43, 812-820
    • (2000) Arthritis. Rheum. , vol.43 , pp. 812-820
    • Takizawa, M.1    Ohuchi, E.2    Yamanaka, H.3    Nakamura, H.4    Ikeda, E.5    Ghosh, P.6    Okada, Y.7
  • 46
    • 0008741084 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases in synovial fluids from patients with rheumatoid arthritis or osteoarthritis
    • Yoshihara, Y., Nakamura, H., Obata, K., Yamada, H., Hayakawa, T., Fujikawa, K., and Okada, Y. (2000) Matrix metalloproteinases and tissue inhibitors of metalloproteinases in synovial fluids from patients with rheumatoid arthritis or osteoarthritis. Ann. Rheum. Dis. 59, 455-461
    • (2000) Ann. Rheum. Dis. , vol.59 , pp. 455-461
    • Yoshihara, Y.1    Nakamura, H.2    Obata, K.3    Yamada, H.4    Hayakawa, T.5    Fujikawa, K.6    Okada, Y.7
  • 47
    • 0035462010 scopus 로고    scopus 로고
    • Highly enhanced expression of the disintegrin metalloproteinase MDC15 (metargidin) in rheumatoid synovial tissue
    • Böhm, B.B., Aigner, T., Blobel, C.P., Kalden, J.R., and Burkhardt, H. (2001) Highly enhanced expression of the disintegrin metalloproteinase MDC15 (metargidin) in rheumatoid synovial tissue. Arthritis. Rheum. 44, 2046-2054
    • (2001) Arthritis. Rheum. , vol.44 , pp. 2046-2054
    • Böhm, B.B.1    Aigner, T.2    Blobel, C.P.3    Kalden, J.R.4    Burkhardt, H.5
  • 48
    • 0034903680 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha (TNF-alpha) converting enzyme contributes to production of TNF-alpha in synovial tissues from patients with rheumatoid arthritis
    • Ohta, S., Harigai, M., Tanaka, M., Kawaguchi, Y., Sugiura, T., Takagi, K., Fukasawa, C., Hara, M., and Kamatani, N. (2001) Tumor necrosis factor-alpha (TNF-alpha) converting enzyme contributes to production of TNF-alpha in synovial tissues from patients with rheumatoid arthritis. J. Rheumatol. 28, 1756-1763
    • (2001) J. Rheumatol. , vol.28 , pp. 1756-1763
    • Ohta, S.1    Harigai, M.2    Tanaka, M.3    Kawaguchi, Y.4    Sugiura, T.5    Takagi, K.6    Fukasawa, C.7    Hara, M.8    Kamatani, N.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.