메뉴 건너뛰기




Volumn 11, Issue 5, 1997, Pages 355-364

Mammalian membrane metallopeptidases: NEP, ECE, KELL, and PEX

Author keywords

atherosclerosis; cardiovascular system; endothelial cells; hypertension; regulatory peptides

Indexed keywords

ENDOTHELIN 1; ENDOTHELIN CONVERTING ENZYME; MEMBRANE METALLOENDOPEPTIDASE; METALLOPROTEINASE;

EID: 0030899822     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.11.5.9141502     Document Type: Review
Times cited : (389)

References (56)
  • 1
    • 0024538318 scopus 로고
    • Neutral endopeptidase 24.11 (enkephalinase) and related regulators of peptide hormones
    • Erdös, E. G., and Skidgel, R. A. (1989) Neutral endopeptidase 24.11 (enkephalinase) and related regulators of peptide hormones. FASEB J. 3, 145-151
    • (1989) FASEB J. , vol.3 , pp. 145-151
    • Erdös, E.G.1    Skidgel, R.A.2
  • 2
    • 0027475050 scopus 로고
    • Neutral endopeptidase 24.11. Structure, inhibition, and experimental and clinical pharmacology
    • Roques, B. P., Noble, F., Daugé, V., Fournié-Zaluski, M. C., and Beaumont, A. (1993) Neutral endopeptidase 24.11. Structure, inhibition, and experimental and clinical pharmacology. Pharmacol. Rev. 45, 87-146
    • (1993) Pharmacol. Rev. , vol.45 , pp. 87-146
    • Roques, B.P.1    Noble, F.2    Daugé, V.3    Fournié-Zaluski, M.C.4    Beaumont, A.5
  • 3
    • 0015973588 scopus 로고
    • The purification and specificity of a neutral endopeptidase from rabbit kidney brush border
    • Kerr, M. A., and Kenny, A. J. (1974) The purification and specificity of a neutral endopeptidase from rabbit kidney brush border. Biochem. J. 137, 477-488
    • (1974) Biochem. J. , vol.137 , pp. 477-488
    • Kerr, M.A.1    Kenny, A.J.2
  • 4
    • 0025863753 scopus 로고
    • A highly sensitive elisa for endopeptidase-24.11, the common acute lymphoblastic leukaemia antigen (CALLA, CD-10), applicable to material of porcine and human origin
    • Howell, S., Murray, H., Turner, A. J., and Kenny, A. J. (1991) A highly sensitive elisa for endopeptidase-24.11, the common acute lymphoblastic leukaemia antigen (CALLA, CD-10), applicable to material of porcine and human origin. Biochem. J. 278, 417-421
    • (1991) Biochem. J. , vol.278 , pp. 417-421
    • Howell, S.1    Murray, H.2    Turner, A.J.3    Kenny, A.J.4
  • 5
    • 0021007899 scopus 로고
    • Purification of endopeptidase-24.11 ("enkephalinase") from pig brain by immunoadsorbent chromatography
    • Relton, J. M., Gee, N. S., Matsas, R., Turner, A. J., and Kenny, A. J. (1983) Purification of endopeptidase-24.11 ("enkephalinase") from pig brain by immunoadsorbent chromatography. Biochem. J. 215, 519-523
    • (1983) Biochem. J. , vol.215 , pp. 519-523
    • Relton, J.M.1    Gee, N.S.2    Matsas, R.3    Turner, A.J.4    Kenny, A.J.5
  • 6
    • 0010374240 scopus 로고
    • Substance P and [Leu]enkephalin are hydrolysed by an enzyme in pig caudate synaptic membranes that is identical with the endopeptidase of kidney microvilli
    • Matsas, R., Fulcher, I. S., Kenny, A. J., and Turner, A. J. (1983) Substance P and [Leu]enkephalin are hydrolysed by an enzyme in pig caudate synaptic membranes that is identical with the endopeptidase of kidney microvilli. Proc. Natl. Acad. Sci. USA 80, 3111-3115
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 3111-3115
    • Matsas, R.1    Fulcher, I.S.2    Kenny, A.J.3    Turner, A.J.4
  • 7
    • 0025986666 scopus 로고
    • CD10(CALLA)/neutral endopeptidase 24.11 modulates inflammatory peptide-induced changes in neutrophil morphology, migration and adhesion proteins and is itself regulated by neutrophil activation
    • Shipp, M. A., Stefano, G. B., Switzer, S. N., Griffin, S. N., and Reinherz, E. L. (1991) CD10(CALLA)/neutral endopeptidase 24.11 modulates inflammatory peptide-induced changes in neutrophil morphology, migration and adhesion proteins and is itself regulated by neutrophil activation. Blood 78, 1834-1841
    • (1991) Blood , vol.78 , pp. 1834-1841
    • Shipp, M.A.1    Stefano, G.B.2    Switzer, S.N.3    Griffin, S.N.4    Reinherz, E.L.5
  • 9
    • 0027941838 scopus 로고
    • Families of zinc metallopeptidases
    • Hooper, N. M. (1994) Families of zinc metallopeptidases. FEBS Lett. 354, 1-6
    • (1994) FEBS Lett. , vol.354 , pp. 1-6
    • Hooper, N.M.1
  • 11
    • 0027244148 scopus 로고
    • Hematopoietic differentiation antigens that are membrane-associated enzymes: Cutting is the key!
    • Shipp, M. A., and Look, A. T. (1993) Hematopoietic differentiation antigens that are membrane-associated enzymes: Cutting is the key! Blood 82, 1052-1070
    • (1993) Blood , vol.82 , pp. 1052-1070
    • Shipp, M.A.1    Look, A.T.2
  • 12
    • 0004187426 scopus 로고
    • Organization of the gene encoding common acute lymphoblastic leukemia antigen (neutral endopeptidase 24.11): Multiple miniexons and separate 5-prime untranslated regions
    • D'Adamio, L., Shipp, M. A., Masteller, E. L., and Reinherz, E. L. (1989) Organization of the gene encoding common acute lymphoblastic leukemia antigen (neutral endopeptidase 24.11): multiple miniexons and separate 5-prime untranslated regions. Proc. Natl. Acad. Sci. USA 86, 7103-7107
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7103-7107
    • D'Adamio, L.1    Shipp, M.A.2    Masteller, E.L.3    Reinherz, E.L.4
  • 13
    • 0024586783 scopus 로고
    • The common acute lymphoblastic leukemia antigen maps to chromosomal region 3(q21-q27)
    • Barker, P. E., Shipp, M. A., D'Adamio, L., Masteller, E. L., and Reinherz, E. L. (1989) The common acute lymphoblastic leukemia antigen maps to chromosomal region 3(q21-q27). J. Immunol. 142, 283-287
    • (1989) J. Immunol. , vol.142 , pp. 283-287
    • Barker, P.E.1    Shipp, M.A.2    D'Adamio, L.3    Masteller, E.L.4    Reinherz, E.L.5
  • 14
    • 0028906255 scopus 로고
    • Tissue-specific expression of rat neutral endopeptidase (neprilysin) mRNAs
    • Li, C., Booze, R. M., and Hersh, L. B. (1995) Tissue-specific expression of rat neutral endopeptidase (neprilysin) mRNAs. J. Biol. Chem. 270, 5723-5728
    • (1995) J. Biol. Chem. , vol.270 , pp. 5723-5728
    • Li, C.1    Booze, R.M.2    Hersh, L.B.3
  • 15
    • 0028324121 scopus 로고
    • Aspartate-residue 650 is crucial for catalytic activity of neutral endopeptidase 24.11
    • Le Moual, H., Dion, N., Roques, B. P., Crine, P., and Boileau, G. (1994) Aspartate-residue 650 is crucial for catalytic activity of neutral endopeptidase 24.11. Eur. J. Biochem. 221, 475-480
    • (1994) Eur. J. Biochem. , vol.221 , pp. 475-480
    • Le Moual, H.1    Dion, N.2    Roques, B.P.3    Crine, P.4    Boileau, G.5
  • 16
    • 0027456271 scopus 로고
    • Kinetic evidence that His-711 of neutral endopeptidase 24.11 is involved in stabilization of the transition state
    • Dion, N., Le Moual, H., Crine, P., and Boileau, G. (1993) Kinetic evidence that His-711 of neutral endopeptidase 24.11 is involved in stabilization of the transition state. FEBS Lett. 318, 301-304
    • (1993) FEBS Lett. , vol.318 , pp. 301-304
    • Dion, N.1    Le Moual, H.2    Crine, P.3    Boileau, G.4
  • 17
    • 0028972611 scopus 로고
    • Evidence that Asn542 of neprilysin (EC 3.4.24.11) is involved in binding of the P2′ residue of substrates and inhibitors
    • Dion, N., Le Moual, H., Fournié-Zaluski, M. C., Roques, B. P., Crine, P., and Boileau, G. (1995) Evidence that Asn542 of neprilysin (EC 3.4.24.11) is involved in binding of the P2′ residue of substrates and inhibitors. Biochem. J. 311, 623-627
    • (1995) Biochem. J. , vol.311 , pp. 623-627
    • Dion, N.1    Le Moual, H.2    Fournié-Zaluski, M.C.3    Roques, B.P.4    Crine, P.5    Boileau, G.6
  • 18
    • 0027474862 scopus 로고
    • Cloning and sequencing of the gene for a Lactococcal endopeptidase, an enzyme with sequence similarity to mammalian enkephalinase
    • Mierau, I., Tan, P. S. T., Haandrikman, A. J., Kok, J., Leenhouts, K. J., Konings, W. N., and Venema, G. (1993) Cloning and sequencing of the gene for a Lactococcal endopeptidase, an enzyme with sequence similarity to mammalian enkephalinase. J. Bacteriol. 175, 2087-2096
    • (1993) J. Bacteriol. , vol.175 , pp. 2087-2096
    • Mierau, I.1    Tan, P.S.T.2    Haandrikman, A.J.3    Kok, J.4    Leenhouts, K.J.5    Konings, W.N.6    Venema, G.7
  • 20
    • 0029091082 scopus 로고
    • Endothelin receptors and calcium signalling
    • Pollock, D. M., Keith, T. L., and Highsmith, R. F. (1995) Endothelin receptors and calcium signalling. FASEB J. 9, 1196-1204
    • (1995) FASEB J. , vol.9 , pp. 1196-1204
    • Pollock, D.M.1    Keith, T.L.2    Highsmith, R.F.3
  • 22
    • 0030032386 scopus 로고    scopus 로고
    • Molecular pharmacology of endothelin converting enzymes
    • Turner, A. J., and Murphy, L. J. (1996) Molecular pharmacology of endothelin converting enzymes. Biochem. Pharmacol. 51, 91-102
    • (1996) Biochem. Pharmacol. , vol.51 , pp. 91-102
    • Turner, A.J.1    Murphy, L.J.2
  • 23
    • 0027454492 scopus 로고
    • Purification and characterization of endothelin-converting enzyme from rat lung
    • Takahashi, M., Matsushita, Y., Iijima, Y., and Tanzawa, K. (1993) Purification and characterization of endothelin-converting enzyme from rat lung. J. Biol. Chem. 268, 21394-21398
    • (1993) J. Biol. Chem. , vol.268 , pp. 21394-21398
    • Takahashi, M.1    Matsushita, Y.2    Iijima, Y.3    Tanzawa, K.4
  • 24
    • 0027992642 scopus 로고
    • ECE-1: A membrane-bound metalloprotease that catalyzes the proteolytic activation of big endothelin-1
    • Xu, D., Emoto, N., Giaid, A., Slaughter, C., Kaw, S., deWit, D., and Yanagisawa, M. (1994) ECE-1: A membrane-bound metalloprotease that catalyzes the proteolytic activation of big endothelin-1. Cell 78, 473-485
    • (1994) Cell , vol.78 , pp. 473-485
    • Xu, D.1    Emoto, N.2    Giaid, A.3    Slaughter, C.4    Kaw, S.5    DeWit, D.6    Yanagisawa, M.7
  • 25
    • 0027452151 scopus 로고
    • Purification and characterization of a phosphoramidon-sensitive endothelin-converting enzyme in porcine aortic endothelium
    • Ohnaka, K., Takayanagi, R., Nishikawa, M., Haji, M., and Nawata, H. (1993) Purification and characterization of a phosphoramidon-sensitive endothelin-converting enzyme in porcine aortic endothelium. J. Biol. Chem. 268, 26759-26766
    • (1993) J. Biol. Chem. , vol.268 , pp. 26759-26766
    • Ohnaka, K.1    Takayanagi, R.2    Nishikawa, M.3    Haji, M.4    Nawata, H.5
  • 27
    • 0028261084 scopus 로고
    • Cloning and functional expression of endothelin-converting enzyme from rat endothelial cells
    • Shimada, K., Takahashi, M., and Tanzawa, K. (1994) Cloning and functional expression of endothelin-converting enzyme from rat endothelial cells. J. Biol. Chem. 269, 18275-18278
    • (1994) J. Biol. Chem. , vol.269 , pp. 18275-18278
    • Shimada, K.1    Takahashi, M.2    Tanzawa, K.3
  • 29
    • 0028923422 scopus 로고
    • Cloning and sequencing of a human endothelin converting enzyme in renal adenocarcinoma (ACHN) cells producing endothelin-2
    • Yorimitsu, K., Moroi, K., Inagaki, N., Saito, T., Madsuda, Y., Masaki, T., Seino, S., and Kimura, S. (1995) Cloning and sequencing of a human endothelin converting enzyme in renal adenocarcinoma (ACHN) cells producing endothelin-2. Biochem. Biophys. Res. Commun. 208, 721-727
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 721-727
    • Yorimitsu, K.1    Moroi, K.2    Inagaki, N.3    Saito, T.4    Madsuda, Y.5    Masaki, T.6    Seino, S.7    Kimura, S.8
  • 30
    • 0029997473 scopus 로고    scopus 로고
    • 412 with a similar catalytic mechanism and a distinct substrate binding mechanism compared with neutral endopeptidase-24.11
    • 412 with a similar catalytic mechanism and a distinct substrate binding mechanism compared with neutral endopeptidase-24.11. Biochem. J. 315, 863-867
    • (1996) Biochem. J. , vol.315 , pp. 863-867
    • Shimada, K.1    Takahashi, M.2    Turner, A.J.3    Tanzawa, K.4
  • 33
    • 0029149716 scopus 로고
    • Identification and characterization of two isoforms of an endothelin converting enzyme-1
    • Shimada, K., Takahashi, M., Ikeda, M., and Tanzawa, K. (1995) Identification and characterization of two isoforms of an endothelin converting enzyme-1. FEBS Lett. 371, 140-144
    • (1995) FEBS Lett. , vol.371 , pp. 140-144
    • Shimada, K.1    Takahashi, M.2    Ikeda, M.3    Tanzawa, K.4
  • 34
    • 0029585975 scopus 로고
    • Organisation of the gene encoding the human endothelin-converting enzyme (ECE-1)
    • Valdenaire, O., Rohrbacher, E., and Mattei, M.-G. (1995). Organisation of the gene encoding the human endothelin-converting enzyme (ECE-1). J. Biol. Chem. 270, 29794-29798
    • (1995) J. Biol. Chem. , vol.270 , pp. 29794-29798
    • Valdenaire, O.1    Rohrbacher, E.2    Mattei, M.-G.3
  • 37
    • 0029017876 scopus 로고
    • Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon-sensitive metalloprotease with acidic pH optimum
    • Emoto, N., and Yanagisawa, M. (1995) Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon-sensitive metalloprotease with acidic pH optimum. J. Biol. Chem. 270, 15262-15268
    • (1995) J. Biol. Chem. , vol.270 , pp. 15262-15268
    • Emoto, N.1    Yanagisawa, M.2
  • 38
    • 0031031038 scopus 로고    scopus 로고
    • Expression of endothelin-converting enzyme in both neuroblastoma and glial cell lines and its localization in rat hippocampus
    • Barnes, K., Walkden, B. J., Wilkinson, T. C., and Turner, A. J. (1997) Expression of endothelin-converting enzyme in both neuroblastoma and glial cell lines and its localization in rat hippocampus. J. Neurochem. 68, 570-577
    • (1997) J. Neurochem. , vol.68 , pp. 570-577
    • Barnes, K.1    Walkden, B.J.2    Wilkinson, T.C.3    Turner, A.J.4
  • 39
    • 0029887148 scopus 로고    scopus 로고
    • Metallopeptidase inhibitors induce an up-regulation of endothelin-converting enzyme and its redistribution from the plasma membrane to an intracellular compartment
    • Barnes, K., Shimada, K., Takahashi, M., Tanzawa, K., and Turner, A. J. (1996) Metallopeptidase inhibitors induce an up-regulation of endothelin-converting enzyme and its redistribution from the plasma membrane to an intracellular compartment. J. Cell Sci. 109, 919-928
    • (1996) J. Cell Sci. , vol.109 , pp. 919-928
    • Barnes, K.1    Shimada, K.2    Takahashi, M.3    Tanzawa, K.4    Turner, A.J.5
  • 40
    • 0029022823 scopus 로고
    • Identification of endothelin-1 and big endothelin-1 in secretory vesicles isolated from bovine aortic endothelial cells
    • Harrison, V. J., Barnes, K., Turner, A. J., Wood, E., Corder, R., and Vane, J. R. (1995) Identification of endothelin-1 and big endothelin-1 in secretory vesicles isolated from bovine aortic endothelial cells. Proc. Natl. Acad. Sci. USA 92, 6344-6348
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6344-6348
    • Harrison, V.J.1    Barnes, K.2    Turner, A.J.3    Wood, E.4    Corder, R.5    Vane, J.R.6
  • 41
    • 0027963329 scopus 로고
    • Generation by the phosphoramidon-sensitive peptidases, endopeptidase-24.11 and thermolysin, of endothelin-1 and C-terminal fragment from big endothelin-1. Br
    • Murphy, L. J., Corder, R., Mallet, A. I., and Turner, A. J. (1994) Generation by the phosphoramidon-sensitive peptidases, endopeptidase-24.11 and thermolysin, of endothelin-1 and C-terminal fragment from big endothelin-1. Br. J. Pharmacol. 113, 137-142
    • (1994) J. Pharmacol. , vol.113 , pp. 137-142
    • Murphy, L.J.1    Corder, R.2    Mallet, A.I.3    Turner, A.J.4
  • 42
    • 0025779323 scopus 로고
    • Molecular cloning and primary structure of Kell blood group protein
    • Lee, S., Zambas, E. D., Marsh, W. L., and Redman, C. M. (1991) Molecular cloning and primary structure of Kell blood group protein. Proc. Natl. Acad. Sci. USA 88, 6353-6357
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6353-6357
    • Lee, S.1    Zambas, E.D.2    Marsh, W.L.3    Redman, C.M.4
  • 43
    • 0028946052 scopus 로고
    • Organisation of the gene encoding the human Kell blood group protein
    • Lee, S., Zambas, E., Green, E. D., and Redman, C. (1995) Organisation of the gene encoding the human Kell blood group protein. Blood 85, 1364-1370
    • (1995) Blood , vol.85 , pp. 1364-1370
    • Lee, S.1    Zambas, E.2    Green, E.D.3    Redman, C.4
  • 44
    • 0029160578 scopus 로고
    • A gene (PEX) with homologies to endopeptidases is mutated in patients with X-linked hypophosphatemic rickets
    • The HYP Consortium (1995) A gene (PEX) with homologies to endopeptidases is mutated in patients with X-linked hypophosphatemic rickets. Nature Genet. 11 130-136
    • (1995) Nature Genet. , vol.11 , pp. 130-136
  • 45
    • 0027513914 scopus 로고
    • Membrane peptidases on human osteoblast-like cells in culture: Hydrolysis of calcitonin and hormonal regulation of endopeptidase-24.11
    • Howell, S., Caswell, A. M., Kenny, A. J., and Turner, A. J. (1993) Membrane peptidases on human osteoblast-like cells in culture: hydrolysis of calcitonin and hormonal regulation of endopeptidase-24.11. Biochem. J. 290, 159-164
    • (1993) Biochem. J. , vol.290 , pp. 159-164
    • Howell, S.1    Caswell, A.M.2    Kenny, A.J.3    Turner, A.J.4
  • 46
    • 0028958066 scopus 로고
    • Expression of membrane-bound peptidases (CD10 and CD26) on human articular chondrocytes. Possible role of neuropeptidases in the pathogenesis of osteoarthritis
    • Lapadula, G., Iannone, F., Zuccaro, C., Covelli, M., Patella, V., Lobianco, G., and Pipitone, V. (1995) Expression of membrane-bound peptidases (CD10 and CD26) on human articular chondrocytes. Possible role of neuropeptidases in the pathogenesis of osteoarthritis. Clin. Exp. Rheumatol. 13, 143-148
    • (1995) Clin. Exp. Rheumatol. , vol.13 , pp. 143-148
    • Lapadula, G.1    Iannone, F.2    Zuccaro, C.3    Covelli, M.4    Patella, V.5    Lobianco, G.6    Pipitone, V.7
  • 49
    • 0028609612 scopus 로고
    • Interaction of endothelin-3 with endothelin-B receptor is essential for development of epidermal melanocytes and enteric neurons
    • Baynash, A. G., Hosoda, K., Giaid, A., Richardson, J. A., Emoto, N., Hammer, R. E., and Yanagisawa M. (1994) Interaction of endothelin-3 with endothelin-B receptor is essential for development of epidermal melanocytes and enteric neurons. Cell 79, 1277-1285
    • (1994) Cell , vol.79 , pp. 1277-1285
    • Baynash, A.G.1    Hosoda, K.2    Giaid, A.3    Richardson, J.A.4    Emoto, N.5    Hammer, R.E.6    Yanagisawa, M.7
  • 51
    • 0028034161 scopus 로고
    • Distribution of, and a putative role for, the cell-surface neutral metalloendopeptidases during craniofacial development
    • Spencer-Dene, B., Thorogood, P., Nair, S., Kenny, A. J., Harris, M., and Henderson, B. (1994) Distribution of, and a putative role for, the cell-surface neutral metalloendopeptidases during craniofacial development. Development 120, 3213-3216
    • (1994) Development , vol.120 , pp. 3213-3216
    • Spencer-Dene, B.1    Thorogood, P.2    Nair, S.3    Kenny, A.J.4    Harris, M.5    Henderson, B.6
  • 52
    • 0025374430 scopus 로고
    • Neutral endopeptidase-24.11 inhibitors: From analgesics to antihypertensives
    • Roques, B. P., and Beaumont, A. (1993) Neutral endopeptidase-24.11 inhibitors: from analgesics to antihypertensives. Trends Pharmacol. Sci. 11, 245-249
    • (1993) Trends Pharmacol. Sci. , vol.11 , pp. 245-249
    • Roques, B.P.1    Beaumont, A.2
  • 54
    • 0030053873 scopus 로고    scopus 로고
    • Expression of endothelin-1, endothelin-3, endothelin-converting enzyme, and endothelin-A and endothelin-B receptor mRNA after angioplasty-induced neointimal formation in the rat
    • Wang, X., Douglas, S. A., Louden, C., Vickery-Clark, L. M., Feuerstein, G. Z., and Ohlstein, E. H. (1996) Expression of endothelin-1, endothelin-3, endothelin-converting enzyme, and endothelin-A and endothelin-B receptor mRNA after angioplasty-induced neointimal formation in the rat. Circ. Res. 78, 322-328
    • (1996) Circ. Res. , vol.78 , pp. 322-328
    • Wang, X.1    Douglas, S.A.2    Louden, C.3    Vickery-Clark, L.M.4    Feuerstein, G.Z.5    Ohlstein, E.H.6
  • 56
    • 0028825317 scopus 로고
    • WS75624 a and B, new endothelin converting enzyme inhibitors isolated from Saccharothrix sp. no. 75624
    • Tsurumi, Y., Ueda, H., Hayashi, K., Takase, S., Nishikawa, M., Kiyoto, S., and Okuhara, M. (1995) WS75624 A and B, new endothelin converting enzyme inhibitors isolated from Saccharothrix sp. no. 75624 J. Antibiot. 48, 1066-1072
    • (1995) J. Antibiot. , vol.48 , pp. 1066-1072
    • Tsurumi, Y.1    Ueda, H.2    Hayashi, K.3    Takase, S.4    Nishikawa, M.5    Kiyoto, S.6    Okuhara, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.